CST4 Human

Cystatin 4 Human Recombinant
Cat. No.
BT24404
Source
E.coli.
Synonyms
Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.
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.
Shipped with Ice Packs
In Stock

Description

CST4 Human Recombinant produced in E. coli is a single polypeptide chain containing 145 amino acids (21-141) and having a molecular mass of 16.8kDa.
CST4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
CST4, a member of the cystatin superfamily, encompasses proteins with multiple cystatin-like sequences. While some members actively inhibit cysteine proteases, others lack or haven't developed this capability. Notably, CST4 potently inhibits papain (non-competitively) and ficin, partially inhibits stem bromelain and bovine cathepsin C, but shows no inhibition towards porcine cathepsin B or clostripain.
Description
Recombinant human CST4, produced in E. coli, is a single polypeptide chain consisting of 145 amino acids (21-141). With a molecular weight of 16.8 kDa, it features a 24 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
Sterile, filtered solution, colorless in appearance.
Formulation
The CST4 solution (1 mg/ml) is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 50 mM NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For longer storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended periods. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95% as determined by SDS-PAGE analysis.
Synonyms
Cystatin-SA-III, Cystatin-4, cystatin S, Salivary acidic protein 1.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSSSKEE NRIIPGGIYD ADLNDEWVQR ALHFAISEYN KATEDEYYRR PLQVLRAREQ TFGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WEDRMSLVNS RCQEA

Product Science Overview

Introduction

Cystatin 4, also known as Cystatin-S, Salivary acidic protein 1, Cystatin-SA-III, and CST4, is a member of the cystatin superfamily. This family of proteins is characterized by their ability to inhibit cysteine proteases, which are enzymes that break down proteins by cleaving peptide bonds. Cystatin 4 is a secreted protein that plays a crucial role in various physiological processes.

Expression and Localization

Cystatin 4 is predominantly expressed in submandibular and sublingual saliva, but it is not found in parotid saliva . Additionally, it is present in other bodily fluids such as tears, urine, and seminal fluid . This widespread distribution suggests that Cystatin 4 has multiple functions in different tissues and organs.

Structure and Function

The cystatin superfamily includes proteins with multiple cystatin-like sequences. Some members of this family are active cysteine protease inhibitors, while others have lost or never acquired this inhibitory activity . Cystatin 4 belongs to the type 2 cystatins, which are a class of cysteine proteinase inhibitors found in various human fluids and secretions .

Cystatin 4 strongly inhibits enzymes such as papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain . This selective inhibition is important for regulating proteolytic activity in different physiological contexts.

Recombinant Production

Recombinant human Cystatin 4 is produced using DNA sequences encoding the human CST4 gene. The recombinant protein is typically expressed in host cells such as HEK293 cells and is purified to high levels of purity . The recombinant protein is often tagged with a polyhistidine tag to facilitate purification and detection .

Applications

Recombinant Cystatin 4 is used in various research applications to study its inhibitory effects on cysteine proteases and its role in different physiological processes. It is also used in the development of therapeutic agents targeting protease-related diseases.

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