CST3 Mouse, Active

Cystatin-C Mouse Recombinant, Active
Cat. No.
BT23833
Source
Sf9, Baculovirus cells.
Synonyms

Cystatin-C, Cystatin-3,  Cst3,  CST3    

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

CST3 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 126 amino acids (21-140 a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).
CST3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cystatins are a large group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Found in various tissues and fluids throughout the body, cystatins play a crucial role in regulating the activity of these proteases. One well-studied member of this family, cystatin C, has garnered significant interest in the fields of biochemistry, medicine, and evolution. This small, secreted protein, consisting of 120 amino acids and weighing 13260 Da, features two disulfide bridges near its carboxyl terminus. Notably, cystatin C levels are elevated in patients diagnosed with malignant diseases and are associated with impaired kidney function, suggesting its potential as a more reliable marker for kidney health compared to creatinine. Conversely, insufficient cystatin C levels have been linked to the degradation of elastic laminae, potentially contributing to conditions such as atherosclerosis and abdominal aortic aneurysm.
Description
CST3 Mouse, produced in Sf9 Insect cells, is a single, glycosylated polypeptide chain comprising 126 amino acids (specifically, amino acids 21 to 140). It has a molecular mass of 14.2 kDa, though on SDS-PAGE, it appears between 13.5 and 18 kDa. This protein is engineered with a 6-amino-acid His tag at its C-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The CST3 protein solution is provided at a concentration of 1 mg/ml. It is prepared in a solution of Phosphate Buffered Saline (pH 7.4) and contains 10% glycerol.
Stability
For short-term storage (up to 4 weeks), the CST3 protein solution should be stored at 4°C. For longer storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein, such as HSA or BSA at a concentration of 0.1%, can further enhance stability during long-term storage. It's important to avoid repeatedly freezing and thawing the solution to maintain protein integrity.
Purity
The purity of this CST3 protein is determined to be greater than 95% based on SDS-PAGE analysis.
Biological Activity
The IC50 value, representing the concentration at which the protein inhibits 50% of protease activity, is less than 1.0 nM. The ability of Cystatin 3 to inhibit the protease activity of papain, a cysteine protease, was assessed using a fluorescence-based assay. This assay employed Z-FR-AMC as the substrate and was conducted at a pH of 7.5 and a temperature of 25°C.
Synonyms

Cystatin-C, Cystatin-3,  Cst3,  CST3    

Source
Sf9, Baculovirus cells.
Amino Acid Sequence

ATPKQGPRML GAPEEADANE EGVRRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGV NYFLDVEMGR TTCTKSQTNL TDCPFHDQPH LMRKALCSFQ IYSVPWKGTH SLTKFSCKNA HHHHHH

Product Science Overview

Introduction

Cystatin-C is a member of the cystatin superfamily, which comprises cysteine protease inhibitors. These inhibitors are widely distributed in tissues and body fluids and play a crucial role in regulating protease activity. Cystatin-C, specifically, is a secreted protein that has garnered significant interest due to its physiological and pathological roles.

Structure and Expression

Recombinant mouse Cystatin-C is typically produced in expression systems such as Baculovirus or Escherichia coli. The recombinant protein is often tagged for purification purposes, such as with a His tag at the N-terminus . The protein is a single, non-glycosylated polypeptide chain consisting of 134 amino acids and has a molecular mass of approximately 15 kDa . The recombinant form is highly purified, with a purity greater than 95% as determined by SDS-PAGE .

Biological Function

Cystatin-C functions as an inhibitor of cysteine proteases, including cathepsins B, H, L, and S . By forming tight complexes with these proteases, Cystatin-C regulates their activity, which is essential for maintaining cellular homeostasis. This regulation is particularly important in processes such as protein degradation, antigen presentation, and apoptosis.

Clinical Significance

Cystatin-C levels are of clinical interest due to their association with various diseases. Elevated levels of Cystatin-C have been observed in patients with malignant diseases and are related to renal function insufficiency . It is considered a better marker than creatinine for assessing kidney function. Conversely, low levels of Cystatin-C can lead to the breakdown of elastic laminae, contributing to conditions such as atherosclerosis and abdominal aortic aneurysm .

Applications

Recombinant mouse Cystatin-C is used in various research applications, including:

  • SDS-PAGE: For analyzing protein purity and molecular weight .
  • Functional Studies (FuncS): To study the inhibitory function of Cystatin-C on protease activity .
Handling and Storage

The recombinant protein is typically supplied as a lyophilized powder and should be reconstituted in deionized water to a working concentration . It is recommended to store the lyophilized protein at -20°C and avoid repeated freeze-thaw cycles to maintain its stability .

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