| Description | Caveolin-1 (82-101) amide (human, mouse, rat) (Caveolin-1 scaffolding domain peptide) is a peptide that reverses aging-associated deleterious changes in multiple organs. Caveolin-1 (82-101) amide (human, mouse, rat) inhibits tyrosine kinases | Product introduction：Used to isolate lymphocytes from human organsMatters needing attention：1. samples, reagents and experimental environment in the whole process shall be carried out at 20 ± 2 ℃. In order to obtain the best experimental results, it is best to carry out the Product introduction：Used to isolate lymphocytes from human organsMatters needing attention：1. samples, reagents and experimental environment in the whole process shall be carried out at 20 ± 2 ℃. In order to obtain the best experimental results, it is best to carry out the experiment within 2 h of sampling. The longer the sample is stored, the worse the cell separation effect is. The separation effect is even worse after the sample is placed for more than 6 h, or even cannot achieve the purpose of separation. 2. in this experiment, it is better not to use plastic products with high polymerization materials (such as polystyrene), but use non-static, low static ionization heart tubes and glass products without alkali treatment, because the electrostatic effect will lead to cell adhesion, and the surface of alkali treated glass will become rough, which will affect the effect of cell separation. 3. aspirating too many lymphocyte layers and separation liquid layers will cause the granulocytes at the junction of separation liquid to be aspirated, thus increasing the number of mixed granulocytes. 4. when the amount of separating solution is greater than that of tissue single cell suspension sample, the separation effect is better.Scope of application：Lymphocyte isolation... Read More | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description:Cyclophilin B (SCYLP, CyPB, and peptidyl-prolyl cis-trans isomerase B) is a 24 kDa glycoprotein member of the B subfamily of the cyclophilin-type PPIase family of molecules. It is both secreted and retained in the ER. When secreted, it mediates chemotaxis and T cell adhesion to fibronectin. This is likely due to its prolyl cis/trans isomerase activity. Intracellularly, Cyclophilin B appears to serve as a molecular chaperone for molecules destined for secretion. It does so via stabilization and facilitating the activity of additional chaperones. The human CyPB precursor is 216 amino acids (aa) in length. It contains a 25 aa signal sequence plus a 191 aa mature region. There is a partial heparin-binding sequence (aa 27‑34), a PPIase domain (aa 47‑204), and a C-terminal ER retention motif (aa 213‑216). Over aa 34‑216, the human and mouse sequences are 95% aa identical... Read More | Inquire |