CST7 Human

Cystatin 7 Human Recombinant
Cat. No.
BT25265
Source
Escherichia Coli.
Synonyms
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.
CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor believed to play a role in immune regulation by inhibiting a specific target within the hematopoietic system. CST7 possesses multiple cystatin-like sequences and belongs to the cystatin superfamily, which consists of three inhibitory families: type 1 cystatins (stefins), type 2 cystatins, and kininogens. While some members actively inhibit cysteine proteases, others lack or may have never possessed this inhibitory function. Type 2 cystatin proteins, a class of cysteine proteinase inhibitors, are present in various human fluids and secretions. CST7 protein expression has been detected in numerous human cancer cell lines derived from malignant tumors.
Description
Recombinant human CST7, produced in E. coli, is a single polypeptide chain comprising 132 amino acids (residues 20-145) with a molecular weight of 15.3 kDa. A 7-amino acid His-tag is fused to the C-terminus of CST7. The protein is purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The CST7 solution (0.5 mg/mL) is prepared in phosphate-buffered saline (pH 7.4).
Stability
For short-term storage (up to 2-4 weeks), keep at 4°C. For extended storage, freeze 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 exceeds 95.0% as determined by SDS-PAGE analysis.
Synonyms
Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.
Source
Escherichia Coli.
Amino Acid Sequence
GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.

Product Science Overview

Introduction

Cystatin 7, also known as Cystatin F, is a member of the cystatin superfamily, which consists of natural cysteine protease inhibitors. These inhibitors are present in a wide variety of organisms and play crucial roles in regulating protease activity. Cystatin 7 is particularly notable for its involvement in immune regulation and its potential implications in cancer research.

Structure and Expression

Cystatin 7 is a type 2 cystatin, which means it belongs to a class of cysteine proteinase inhibitors found in various human fluids and secretions. The protein is glycosylated and has a molecular weight of approximately 15.2 kDa, although it is observed to be around 25 kDa due to glycosylation . The recombinant form of Cystatin 7 is typically expressed in HEK293 cells, a human embryonic kidney cell line commonly used for protein production .

Biological Function

Cystatin 7 is primarily expressed in hematopoietic cells, with the highest levels observed in monocytes, dendritic cells, and certain types of T-cells . Its expression is up-regulated during the maturation of dendritic cells, suggesting a specific role in immune regulation . Cystatin 7 functions as an inhibitor of cysteine proteases, enzymes that break down proteins by cleaving peptide bonds. By inhibiting these proteases, Cystatin 7 helps regulate various physiological processes, including immune responses and inflammation.

Role in Cancer Research

Cystatin 7 has been observed in various human cancer cell lines, indicating its potential role in cancer progression and metastasis . The protein is produced as a dimer, an inactive form that becomes an active cathepsin inhibitor upon chemical reduction . This activation mechanism suggests that Cystatin 7 could be involved in controlling protease activity in the tumor microenvironment, thereby influencing cancer cell behavior.

Applications in Research

Recombinant Cystatin 7 is widely used in research to study its role in immune regulation and cancer. The protein is typically provided as a lyophilized powder, which can be reconstituted for experimental use . It is essential to handle and store the protein properly to maintain its stability and activity. Researchers often use Cystatin 7 to investigate its interactions with cysteine proteases and to explore its potential as a therapeutic target for immune-related disorders and cancer.

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