CST3 Human, His Active

Cystatin C, His BioActive Human Recombinant
Cat. No.
BT23486
Source
E.coli.
Synonyms

Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

Appearance
Sterile Filtered colorless solution.
Purity

Greater than 95.0% as determined by SDS-PAGE.

Usage
THE BioTek'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.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction

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.

Description

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.

Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation

The CST3 solution (0.25mg/ml) is formulated in a buffer containing 0.1M NaCl, 20mM Tris-HCl (pH 8.0), and 20% glycerol.

Stability

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

Purity is determined to be greater than 95.0% by SDS-PAGE analysis.

Biological Activity

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.

Synonyms

Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

Source
E.coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MSSPGKPPRL VGGPMDASVE EEGVRRALDF AVGEYNKASN DMYHSRALQV VRARKQIVAG VNYFLDVELG RTTCTKTQPN LDNCPFHDQP HLKRKAFCSF QIYAVPWQGT MTLSKSTCQD A

Product Science Overview

Introduction

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 .

Structure and Function

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 .

Biological Activity

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 .

Applications
  1. Research: Cystatin C is widely used in research to study its role in various biological processes and diseases. Its inhibitory activity against cysteine proteases makes it a valuable tool for investigating the mechanisms of protease regulation and the development of protease inhibitors.
  2. Clinical Diagnostics: Due to its stable expression in body fluids, Cystatin C is used as a biomarker for kidney function. Elevated levels of Cystatin C in the blood are indicative of impaired kidney function and are used to diagnose and monitor chronic kidney disease.
  3. Therapeutics: The protein’s ability to inhibit cysteine proteases has potential therapeutic applications. For example, Cystatin C could be used to develop treatments for diseases characterized by excessive protease activity, such as certain cancers and inflammatory conditions .

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