Cystatin-C, Cystatin-3, Cst3, CST3
MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.
CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).
CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Sterile Filtered colorless solution.
CST3 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Avoid multiple freeze-thaw cycles.
Greater than 95% as determined by SDS-PAGE.
Amino acid sequence
ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH
The IC50 value is < 1.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.