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Results for "

Trypsin, Rat

" in MedChemExpress (MCE) Product Catalog:

4

Inhibitors & Agonists

1

Biochemical Assay Reagents

2

Recombinant Proteins

Cat. No. Product Name Target Research Areas Chemical Structure
  • HY-W014134

    p-Amidinophenylmethylsulfonylfluoride hydrochloride

    Ser/Thr Protease Inflammation/Immunology
    p-APMSF (p-Amidinophenylmethylsulfonylfluoride) hydrochloride is a serine protease and trypsin inhibitor with the characteristic of rapid onset of action. p-APMSF hydrochloride reduces the enzymatic hydrolysis of recombinant human G-CSF in rat pulmonary mucosa. Combined intratracheal treatment with p-APMSF hydrochloride and Laureth-9 significantly enhances its absorption efficiency in rat lungs. Following intranasal administration, p-APMSF hydrochloride does not increase the concentration of recombinant human G-CSF in rat plasma, nor does it alter the effect of G-CSF on inducing an increase in total white blood cell count .
    p-APMSF hydrochloride
  • HY-W127391

    (Rac)-1,2-Didodecanoylglycerol

    Biochemical Assay Reagents Others
    1,2-Dilaurin is a diacylglycerol containing lauric acid at the sn-1 and sn-2 positions. It has been used as an internal standard for the quantification of diglycerides in rat desheathed sciatic nerves. [1] Monomolecular films containing 1,2-dilauroyl-rac-glycerol have been used as substrates to measure surface pressure and the effect of pancreatic procolipase and colipase on porcine pancreatic lipase activity. [2] References: [1]. Zhu, X. and Eichberg, J. 1,2-Diacylglycerol content and its arachidonyl-containing molecular species are reduced in the sciatic nerve of streptozotocin-induced diabetic rats. J. Neurochemistry. 55(3), 1087-1090 (1990).[2]. Wieloch, T., Borgstr m, B., Piéroni, G. et al. Porcine trypsinogen and its trypsin-activated form: lipid binding and lipase activation on monomolecular membranes. FEBS Express. 128(2), 217-220 (1981).
    1,2-Dilaurin
  • HY-129047H

    Ser/Thr Protease Metabolic Disease
    Trypsin, Rat (EC 3.4.21.4) is a serine protease belonging to the PA superfamily. It is present in the digestive systems of many vertebrates and hydrolyzes proteins. Trypsin, Rat (EC 3.4.21.4) primarily cleaves peptide chains at the carboxyl terminus of lysine or arginine, but cleavage does not occur when lysine or arginine is followed by proline.
    Trypsin, Rat
  • HY-P2974A

    Elastase Metabolic Disease
    Elastase, Rat (EC 3.4.21.35) is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta-barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together.
    Elastase, Rat

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