CST6 Human
Cystatin E/M Human Recombinant
Cat. No.
BT25138
Source
E.coli.
Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% 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.
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Description
CST6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 142 amino acids (29-149) and having a molecular mass of 15.9 kDa.
The CST6 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
The CST6 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
CST6, a member of the type 2 cystatin family, differs from other members by not actively inhibiting cysteine proteases. While it does not inhibit cathepsin C, it does have a restraining effect on cathepsin B inhibition. As a secreted protein, CST6 plays a role in several biological processes, including osteogenesis, bone resorption, regulation of hepatocyte growth factor receptors, and the response to systemic inflammation.
Description
Recombinant CST6 Human, produced in E.coli, is a single, non-glycosylated polypeptide chain consisting of 142 amino acids (29-149). It has a molecular weight of 15.9 kDa. A 21 amino acid His-Tag is fused to the N-terminus of CST6, and purification is achieved through proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The CST6 solution is provided at a concentration of 0.5mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, freezing at -20°C is recommended. Adding a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined to be greater than 95% using SDS-PAGE analysis.
Synonyms
Cystatin E/M, cystatin 6, Cystatin M, Cystatin-E, Cysteine proteinase inhibitor.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRPQERMVGE LRDLSPDDPQ VQKAAQAAVA SYNMGSNSIY YFRDTHIIKA QSQLVAGIKY FLTMEMGSTD CRKTRVTGDH VDLTTCPLAA GAQQEKLRCD FEVLVVPWQN SSQLLKHNCV QM.
Product Science Overview
Structure and Properties
Cystatin E/M is a low molecular mass secreted protein that exists in both glycosylated (17 kDa) and unglycosylated (14 kDa) forms. It features two characteristic intrachain disulfide bridges . The recombinant form of Cystatin E/M is typically produced in HEK293 cells and has a calculated molecular weight of approximately 15 kDa .
Expression and Localization
Functions
Cystatin E/M serves multiple functions:
- Protease Inhibition: It inhibits cysteine proteases, which are enzymes that break down proteins. This inhibition is crucial for maintaining cellular homeostasis and preventing excessive protein degradation .
- Barrier Formation and Maintenance: Cystatin E/M is involved in the formation and maintenance of the skin barrier. It acts as a target for cross-linking by transglutaminases, enzymes that help form the protective barrier of the skin .
- Tumor Suppression: Studies have shown that Cystatin E/M is frequently epigenetically inactivated during breast carcinogenesis, suggesting its role as a potential tumor suppressor gene .
Recombinant Production
Recombinant Cystatin E/M is produced using various expression systems, with HEK293 cells being a common host. The recombinant protein is often tagged with a His-tag for purification purposes and is available in both glycosylated and unglycosylated forms . The protein is typically lyophilized and can be reconstituted for use in various research applications .
Applications
Recombinant Cystatin E/M is used in a variety of research applications, including:
- Protease Inhibition Studies: To study the inhibition of cysteine proteases and understand the mechanisms of protease regulation.
- Cancer Research: To investigate its role as a tumor suppressor and its potential therapeutic applications in cancer treatment.
- Skin Barrier Research: To explore its involvement in skin barrier formation and maintenance, and its potential use in dermatological research .
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