Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
Greater than 95.0% as determined by SDS-PAGE.
CST3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (27-146 a.a.) and having a molecular mass of 15.6kDa.
CST3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Cystatin C belongs to the cystatin family, a group of proteins with cystatin-like sequences. Some cystatins are active cysteine protease inhibitors, while others have lost or never possessed this ability. The cystatin family is further divided into three subtypes: type 1 cystatins, type 2 cystatins, and kininogens. Chromosome twenty houses the locus for most type 2 cystatin genes, including the gene for Cystatin C. Cystatin C is the most abundant extracellular inhibitor of cysteine proteases, widely distributed in biological fluids and present in all tissues.
Recombinant human CST3, produced in E. coli, is a single, non-glycosylated polypeptide chain. It comprises 141 amino acids (residues 27-146), has a molecular weight of 15.6 kDa, and includes a 21 amino acid His tag at the N-terminus. Purification is achieved using proprietary chromatographic methods.
The CST3 solution (0.25mg/ml) is formulated in a buffer containing 0.1M NaCl, 20mM Tris-HCl (pH 8.0), and 20% glycerol.
For short-term storage (2-4 weeks), keep at 4°C. For extended periods, store frozen at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity is determined to be greater than 95.0% by SDS-PAGE analysis.
The IC50 value, determined by a fluorometric assay using Z-FR-AMC as the substrate at pH 7.5 and 25°C, is less than 2.0 nM. This indicates strong inhibitory activity of Cystatin 3 against the protease papain.
Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.
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Cystatin C is a small, non-glycosylated protein that belongs to the cystatin superfamily. This family of proteins is known for their ability to inhibit cysteine proteases, which are enzymes that break down proteins. Cystatin C is particularly important due to its role in various physiological and pathological processes, including inflammation, tumor invasion, and neurological diseases .
Cystatin C is composed of 120 amino acids and has a molecular weight of approximately 13 kDa. It is ubiquitously expressed in human tissues and body fluids, making it a valuable biomarker for various diseases. The protein inhibits several cysteine proteases, including papain and cathepsins B, H, K, L, and S .
The recombinant form of Cystatin C, often tagged with a histidine (His) tag for purification purposes, is produced in various expression systems, including E. coli and mammalian cells. The His tag allows for easy purification using nickel affinity chromatography, ensuring high purity and activity of the protein .
Recombinant Cystatin C retains its ability to inhibit cysteine proteases, making it a useful tool in research and therapeutic applications. The protein’s inhibitory activity is measured by its ability to prevent the cleavage of specific peptide substrates by cysteine proteases. For instance, the inhibition of papain-induced cleavage of a fluorogenic peptide substrate is a common assay used to determine the activity of recombinant Cystatin C .