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Chymase (human skin), (purified)

Highly active
 
BML-SE281-0010 10 U 479.00 USD
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Product Specification

MW:~30kDa (SDS-PAGE)
 
Source:Isolated from human skin.
 
UniProt ID:P23946
 
Formulation:Liquid. In 50mM sodium acetate, pH 5.0, containing 1M sodium chloride.
 
Purity:≥95% (SDS-PAGE). Although this is in highly purified form, and the source material tested negative for syphilis, HIV-1/HIV-2, Hepatitis B, Hepatitis C, and HTLV-1, handle this product with all due precautions.
 
Specific Activity:XX U/mg. One U=0.1 μmol/min at pH 7.8 and 25°C, using the substrate N-benzoyl-L-tyrosine ethyl ester (BTEE).
 
Application Notes:Useful for the study enzyme kinetics, cleave target substrates, and screen for inhibitors.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Use/Stability:The enzyme is stable on ice for at least several hours. However, it is recommended that thawing and dilution of the enzyme be done within as short a time as possible before start of the assay.NOTE: When stored under the above conditions, this enzyme is stable at the concentration supplied, in its current storage buffer. Procedures such as dilution of the enzyme followed by refreezing could lead to loss of activity.
 
Handling:Avoid freeze/thaw cycles. After opening, prepare aliquots and store at -20°C.
 
Scientific Background:Chymase, found primarily in mast cells, is a serine protease related to granzyme B and cathepsin G. Because of its involvement in many processes such as inflammation and processing of cytokines and hormones, it is an important target for drug discovery.
 

General Literature References

Inhibition of human chymase by 2-amino-3,1-benzoxazin-4-ones: U. Neumann, et al.; Bioorg. Med. Chem. 9, 947 (2001), Abstract;
Secretory production of recombinant human chymase as an active form in Pichia pastoris: H. Nakakubo, et al.; Yeast 16, 315 (2000), Abstract;
Structure-activity relationship studies of chloromethyl ketone derivatives for selective human chymase inhibitors: Y. Hayashi, et al.; Bioorg. Med. Chem. Lett. 10, 199 (2000), Abstract;
Chymase in exocytosed rat mast cell granules effectively proteolyzes apolipoprotein AI-containing lipoproteins, so reducing the cholesterol efflux-inducing ability of serum and aortic intimal fluid: L. Lindstedt, et al.; J. Clin. Invest. 97, 2174 (1996), Abstract;
Human skin chymotrypsin-like proteinase chymase. Subcellular localization to mast cell granules and interaction with heparin and other glycosaminoglycans: S. Sayama, et al.; J. Biol. Chem. 262, 6808 (1987), Abstract;

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