Introduction: Dipeptidyl peptidase 4 (DPP4) ranges are related to metabolic and cardiovascular illnesses in people; preliminary proof reported a relationship between DPP4 and continual liver illnesses. Intention of this examine was to research hepatic and systemic DPP4 ranges/exercise in relation to NAFLD/NASH in people with and with out metabolic illness.
Strategies: We recruited fifty-two overweight people present process bariatric surgical procedure and intra-operative liver biopsy at Sapienza College, Rome, Italy. The affiliation between DPP4 ranges/exercise and NAFLD was additionally evaluated in 126 non-obese people recruited in the identical setting.
Outcomes: NAFLD sufferers had considerably larger circulating DPP4 exercise than no-NAFLD in each the overweight and non-obese cohorts; plasma DPP4 exercise and ranges linearly correlated with steatosis grade and irritation on the liver biopsy. Hepatic DPP4 mRNA was not related to both its circulating ranges/exercise or NAFLD. Within the multivariate logistic regression evaluation on all of the examine contributors (n = 178), larger circulating DPP4 exercise was related to NAFLD independently of potential confounders with OR (95% CI): 3.5 (1.2-10.21), p = 0.022.
Conclusions: This examine demonstrates the coexistence of elevated plasma DPP4 ranges and exercise in NAFLD. Circulating DPP4 measurement might signify a novel cost-effective technique for NAFLD/NASH danger stratification and a possible device for monitoring illness’s development in established NAFLD.
The first outcomes have been the reductions in glycated hemoglobin (HbA1c) and glucose oscillation, recognized utilizing steady glucose monitoring, after 12 weeks. The secondary consequence was the change in carotid intima-media thickness (IMT), measured by ultrasonography, after 48 weeks. A complete of 61 sufferers have been recruited and analyzed within the examine. Twelve weeks of therapy with 1.5 mg repaglinide or 1 mg glimepiride considerably decreased HbA1c, and a bigger discount in HbA1c occurred within the repaglinide group than the glimepiride group. Imply subcutaneous glucose focus was considerably decreased in each teams, however the glucose oscillation didn’t lower.
Nitric oxide debilitates the neuropathogenic schistosome Trichobilharzia regenti in mice, partly by inhibiting its important peptidases
Background: Avian schistosomes, the causative brokers of human cercarial dermatitis (or swimmer’s itch), die in mammals however the mechanisms accountable for parasite elimination are unknown. Right here we examined the position of reactive nitrogen species, nitric oxide (NO) and peroxynitrite, within the immune response of mice experimentally contaminated with Trichobilharzia regenti, a mannequin species of avian schistosomes exceptional for its neuropathogenicity.
Strategies: Inducible NO synthase (iNOS) was localized by immunohistochemistry within the pores and skin and the spinal twine of mice contaminated by T. regenti. The affect of iNOS inhibition by aminoguanidine on parasite burden and progress was then evaluated in vivo. The vulnerability of T. regenti schistosomula to NO and peroxynitrite was assessed in vitro by viability assays and electron microscopy. Moreover, the impact of NO on the exercise of T. regenti peptidases was examined utilizing a fluorogenic substrate.
Outcomes: iNOS was detected across the parasites within the dermis eight h post-infection and in addition within the spinal twine Three days post-infection (dpi). Inhibition of iNOS resulted in slower parasite progress Three dpi, however the reverse impact was noticed 7 dpi. On the latter time level, reasonably elevated parasite burden was additionally seen within the spinal twine. In vitro, NO didn’t impair the parasites, however inhibited the exercise of T. regenti cathepsins B1.1 and B2, the peptidases important for parasite migration and digestion. Peroxynitrite severely broken the floor tegument of the parasites and decreased their viability in vitro, however fairly didn’t take part in parasite clearance in vivo.
Conclusions: Reactive nitrogen species, particularly NO, don’t immediately kill T. regenti in mice. NO promotes the parasite progress quickly after penetration (Three dpi), however prevents it later (7 dpi) when additionally suspends the parasite migration within the CNS. NO-related disruption of the parasite proteolytic equipment is partly accountable for this impact.
Circulating dipeptidyl peptidase-4 is independently associated with the presence and severity of NAFLD/NASH in individuals with and without obesity and metabolic disease
The Impact of Dipeptidyl Peptidase-Four Inhibitors on Macrovascular and Microvascular Issues of Diabetes Mellitus: A Systematic Overview
Background: The World Well being Group estimates that diabetes is the seventh main reason for loss of life. Uncontrolled diabetes might trigger extreme penalties similar to cardiovascular (CV) occasions (myocardial infarction, stroke, or CV mortality), lower-extremity amputations, and end-stage renal illness. Microvascular issues embrace retinopathy, autonomic and peripheral neuropathy, nephropathy, and diabetic ulcers. Main CV outcomes trials that have been by the Meals and Drug Administration for all new antihyperglycemia drugs for sufferers at excessive danger for CV occasions have been just lately accomplished for all Four US-marketed dipeptidyl peptidase-4 (DPP-4) inhibitors.
Goal: To current a complete assessment of the medical trials that consider macrovascular and microvascular issues reported with DPP-Four inhibitors in sufferers with kind 2 diabetes mellitus.
Strategies: On this assessment, we analyzed printed articles in PubMed and Ovid databases between January 2008 and September 2019 that evaluated the impact of DPP-Four inhibitors on macrovascular and microvascular issues in sufferers with kind 2 diabetes mellitus.
Outcomes: A complete of 18 research, which included randomized managed trials and meta-analyses have been assessed. Present proof demonstrates that the addition of DPP-Four inhibitors to plain antihyperglycemic and CV danger discount therapy has not proven CV profit relative to placebo in distinction to just lately printed research for different drugs throughout the glucagon-like peptide 1 agonist and sodium-glucose co-transporter 2 inhibitor courses. Notably, the potential danger for coronary heart failure hospitalizations might exist for saxagliptin, and this impact is just not extrapolated as a category impact.
 SERPINA10 Antibody |
|
1-CSB-PA891944ESR2HU |
Cusabio |
|
|
|
|
|
Description: A polyclonal antibody against SERPINA10. Recognizes SERPINA10 from Human, Mouse. This antibody is Unconjugated. Tested in the following application: ELISA, WB, IHC; Recommended dilution: WB:1:500-1:2000, IHC:1:20-1:200 |
 SERPINA10 antibody |
|
70R-20166 |
Fitzgerald |
50 ul |
EUR 522 |
|
Description: Rabbit polyclonal SERPINA10 antibody |
SERPINA10 antibody |
|
70R-9712 |
Fitzgerald |
50 ug |
EUR 560.4 |
|
Description: Affinity purified rabbit polyclonal SERPINA10 antibody |
 SERPINA10 Peptide |
|
46-895P |
ProSci |
0.1 mg |
EUR 405.6 |
|
Description: SERPINA10 / ZPI Peptide |
SERPINA10 antibody |
|
70R-13353 |
Fitzgerald |
100 ul |
EUR 548.4 |
|
Description: Affinity purified Rabbit polyclonal SERPINA10 antibody |
 anti- SERPINA10 antibody |
|
FNab07739 |
FN Test |
100µg |
EUR 658.5 |
|
|
|
Description: Antibody raised against SERPINA10 |
anti- SERPINA10 antibody |
|
FNab07740 |
FN Test |
100µg |
EUR 702 |
|
|
|
Description: Antibody raised against SERPINA10 |
 Anti-SERPINA10 antibody |
|
STJ29186 |
St John's Laboratory |
100 µl |
EUR 332.4 |
|
Description: The protein encoded by this gene belongs to the serpin family. It is predominantly expressed in the liver and secreted in plasma. It inhibits the activity of coagulation factors Xa and XIa in the presence of protein Z, calcium and phospholipid. Mutations in this gene are associated with venous thrombosis. Alternatively spliced transcript variants have been found for this gene. |
) Anti-SERPINA10 (1E11) |
|
YF-MA18425 |
Abfrontier |
100 ug |
EUR 435.6 |
|
Description: Mouse monoclonal to SERPINA10 |
Anti-SERPINA10 antibody |
|
STJ116256 |
St John's Laboratory |
100 µl |
EUR 332.4 |
|
Description: The protein encoded by this gene belongs to the serpin family. It is predominantly expressed in the liver and secreted in plasma. It inhibits the activity of coagulation factors Xa and XIa in the presence of protein Z, calcium and phospholipid. Mutations in this gene are associated with venous thrombosis. Alternatively spliced transcript variants have been found for this gene. |
 SERPINA10 Polyclonal Conjugated Antibody |
|
C30600 |
SAB |
100ul |
EUR 476.4 |
SERPINA10 Polyclonal Conjugated Antibody |
|
C30825 |
SAB |
100ul |
EUR 476.4 |
 Chymase reagent |
|
30C-CP1129 |
Fitzgerald |
5 units |
EUR 2622 |
|
Description: Purified native Human Chymase reagent |
 BOP reagent |
|
A7015-100000 |
ApexBio |
100 g |
EUR 240 |
|
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis. |
BOP reagent |
|
A7015-25000 |
ApexBio |
25 g |
EUR 135.6 |
|
Description: A peptide coupling reagent. Can be used in the preparation of phenyl esters of amino acids which have been shown to be valuable as blocked derivatives of amino acids in the field of peptide synthesis. |
 Kidney Lysate |
|
21-104 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Bovine kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Liver Lysate |
|
21-105 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Bovine liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The bovine liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Heart Lysate |
|
21-115 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Guinea Pig heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Kidney Lysate |
|
21-116 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Guinea Pig kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The guinea pig kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Adrenal Lysate |
|
21-160 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Cynomolgus) adrenal tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) adrenal tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the adrenal tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The adrenal tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Colon Lysate |
|
21-179 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Cynomolgus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Gallbladder Lysate |
|
21-188 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Cynomolgus) gallbladder tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) gallbladder tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the gallbladder tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The gallbladder tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Kidney Lysate |
|
21-190 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Cynomolgus) kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Lung Lysate |
|
21-194 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Cynomolgus) lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Skin Lysate |
|
21-204 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Cynomolgus) skin tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) skin tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the skin tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The skin tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Spleen Lysate |
|
21-209 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Cynomolgus) spleen tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Cynomolgus) spleen tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the spleen tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The spleen tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Brain Lysate |
|
21-272 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Rhesus) brain tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) brain tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the brain tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The brain tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Colon Lysate |
|
21-288 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Rhesus) colon tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) colon tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the colon tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The colon tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Gallbladder Lysate |
|
21-298 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Rhesus) gallbladder tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) gallbladder tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the gallbladder tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The gallbladder tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Heart Lysate |
|
21-299 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Rhesus) heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Lung Lysate |
|
21-305 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Monkey (Rhesus) lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Skin Lysate |
|
21-315 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Monkey (Rhesus) skin tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The monkey (Rhesus) skin tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the skin tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The skin tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Placenta Lysate |
|
21-393 |
ProSci |
0.1 mg |
EUR 500.1 |
|
Description: Mouse placenta tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The mouse placenta tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the placenta tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The placenta tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Rectum Lysate |
|
21-394 |
ProSci |
0.1 mg |
EUR 663.9 |
|
Description: Mouse rectum tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The mouse rectum tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the rectum tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The rectum tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Heart Lysate |
|
21-404 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Porcine heart tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The porcine heart tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the heart tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The heart tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Kidney Lysate |
|
21-405 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Porcine kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The porcine kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Liver Lysate |
|
21-406 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Porcine liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The porcine liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Brain Lysate |
|
21-414 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Rabbit brain tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rabbit brain tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the brain tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The brain tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Kidney Lysate |
|
21-418 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Rabbit kidney tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rabbit kidney tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the kidney tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The kidney tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Liver Lysate |
|
21-419 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Rabbit liver tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rabbit liver tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the liver tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The liver tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Lung Lysate |
|
21-420 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Rabbit lung tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rabbit lung tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the lung tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The lung tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Ovary Lysate |
|
21-468 |
ProSci |
0.1 mg |
EUR 468.6 |
|
Description: Rat ovary tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rat ovary tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the ovary tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The ovary tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
Placenta Lysate |
|
21-469 |
ProSci |
0.1 mg |
EUR 342.6 |
|
Description: Rat placenta tissue lysate was prepared by homogenization using a proprietary technique. The tissue was frozen in liquid nitrogen immediately after excision and then stored at -70°C. The rat placenta tissue total protein is provided in a buffer including HEPES (pH 7.9), MgCl2, KCl, EDTA, Sucrose, Glycerol, Sodium deoxycholate, NP-40, and a cocktail of protease inhibitors. For quality control purposes, the placenta tissue pattern on SDS-PAGE gel is shown to be consistent for each lot by visualization with coomassie blue staining. The placenta tissue is then Western analyzed by either GAPDH or β-actin antibody, and the expression level is consistent with each lot. |
 Esophagus Lysate |
|
1365 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Esophagus tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Ileum Lysate |
|
1367 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Ileum tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Rectum Lysate |
|
1373 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Rectum tissue lysate was prepared by homogenization in homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Skin Lysate |
|
1376 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Skin tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Thyroid Lysate |
|
1380 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Thyroid tissue lysate was prepared by homogenization in lysis buffer (10 mM HEPES pH7.9, 1.5 mM MgCl2, 10 mM KCl, 1 mM ethylenediaminetetraacetic acid, 10% glycerol, 1% NP-40, and a cocktail of protease inhibitors). Tissue and cell debris was removed by centrifugation. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Spleen Lysate |
|
1406 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Bladder Lysate |
|
1410 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Bladder tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Cerebellum Lysate |
|
1412 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Cerebellum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Cerebrum Lysate |
|
1413 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Cerebrum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Pancreas Lysate |
|
1414 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Stomach Lysate |
|
1415 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Stomach tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Testis Lysate |
|
1416 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Testis tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Adrenal Lysate |
|
1417 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Adrenal tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Skin Lysate |
|
1419 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Skin tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Eye Lysate |
|
1420 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Eye tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Trachea Lysate |
|
1422 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Trachea tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Lung Lysate |
|
1462 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Lung tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Liver Lysate |
|
1464 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Liver tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Kidney Lysate |
|
1465 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Kidney tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Spleen Lysate |
|
1466 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Spleen tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Pancreas Lysate |
|
1469 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Pancreas tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Adrenal Lysate |
|
1470 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Adrenal tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Thymus Lysate |
|
1471 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Thymus tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Colon Lysate |
|
1472 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Colon tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Cerebellum Lysate |
|
1473 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Cerebellum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Cerebrum Lysate |
|
1474 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Cerebrum tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Stomach Lysate |
|
1475 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Stomach tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Testis Lysate |
|
1476 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Testis tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Bladder Lysate |
|
1478 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Bladder tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Eye Lysate |
|
1479 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Eye tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Skin Lysate |
|
1480 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Skin tissue lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Tissue and cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The product was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 Jurkat Lysate |
|
1205 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: Jurkat lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The Jurkat lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 MOLT4 Lysate |
|
1206 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: MOLT4 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The MOLT4 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 HL60 Lysate |
|
1209 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: HL60 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The HL60 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
 T24 Lysate |
|
1213 |
ProSci |
0.1 mg |
EUR 229.2 |
|
Description: T24 lysate was prepared by homogenization in modified RIPA buffer (150 mM sodium chloride, 50 mM Tris-HCl, pH 7.4, 1 mM ethylenediaminetetraacetic acid, 1 mM phenylmethylsulfonyl fluoride, 1% Triton X-100, 1% sodium deoxycholic acid, 0.1% sodium dodecylsulfate, 5 μg/ml of aprotinin, 5 μg/ml of leupeptin. Cell debris was removed by centrifugation. Protein concentration was determined with Bio-Rad protein assay. The T24 lysate was boiled for 5 min in 1 x SDS sample buffer (50 mM Tris-HCl pH 6.8, 12.5% glycerol, 1% sodium dodecylsulfate, 0.01% bromophenol blue) containing 50 mM DTT. |
Primarily based on our assessment, DPP-Four inhibitors might not affect microvascular issues in sufferers with diabetes. Nonetheless, some research have proven that saxagliptin and linagliptin might decelerate the development of albuminuria in sufferers with kind 2 diabetes mellitus. The general high quality of the research included on this assessment was excessive as a result of inclusion of randomized managed trials and meta-analyses.
