HSPB3 Human

Heat Shock 27kDa Protein 3 Human Recombinant
Cat. No.
BT18516
Source
E.coli.
Synonyms
Heat shock 27kDa protein 3, HSPL27, Protein 3, HSP 17, DHMN2C, HMN2C, heat shock protein beta-3, HspB3.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% 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

HSPB3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-150) and having a molecular mass of 19.1 kDa.
The HSPB3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
HSPB3, primarily found in heart and skeletal muscle, is a small heat shock protein specific to muscle tissue. Belonging to a family of highly expressed proteins, mammalian small heat shock proteins (sHSPs) play diverse roles. These roles include the assembly and sequestration of multi-protein complexes, facilitating the transport of newly synthesized polypeptide chains across cell membranes, and modulating protein folding processes. HSPB3 functions as an ATP-dependent chaperone protein, actively participating in the refolding of misfolded proteins and regulating actin polymerization.
Description
Recombinantly produced in E. coli, HSPB3 Human Recombinant is a single, non-glycosylated polypeptide chain consisting of 170 amino acids (residues 1-150) and possessing a molecular weight of 19.1 kDa. For purification purposes, a 20 amino acid His-Tag is fused to the N-terminus of HSPB3, and proprietary chromatographic techniques are employed.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HSPB3 solution is provided at a concentration of 1mg/ml and is formulated in a buffer containing 20mM Tris-HCl (pH 8.0), 1M Urea, and 5% glycerol.
Stability
For short-term storage (2-4 weeks), the entire vial can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein such as 0.1% HSA or BSA is advisable for long-term storage. Repeated freezing and thawing cycles should be avoided.
Purity
SDS-PAGE analysis indicates a purity exceeding 85%.
Synonyms
Heat shock 27kDa protein 3, HSPL27, Protein 3, HSP 17, DHMN2C, HMN2C, heat shock protein beta-3, HspB3.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAKIILRHLI EIPVRYQEEF EARGLEDCRL DHALYALPGP TIVDLRKTRA AQSPPVDSAA ETPPREGKSH FQILLDVVQF LPEDIIIQTF EGWLLIKAQH GTRMDEHGFI SRSFTRQYKL PDGVEIKDLS AVLCHDGILV VEVKDPVGTK

Product Science Overview

Classification and Structure

HSPB3 is classified under the small heat shock proteins, which typically range from 12 to 43 kDa in size. The human recombinant form of HSPB3 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 170 amino acids, with a molecular mass of approximately 19.1 kDa .

Biological Properties and Functions

HSPB3, like other small heat shock proteins, functions as a molecular chaperone. This means it helps in maintaining the proper folding of other proteins, especially under stress conditions. It prevents the aggregation of denatured proteins, thereby protecting cells from damage .

Mode of Action

The primary mode of action of HSPB3 involves binding to partially unfolded proteins, stabilizing them, and preventing their aggregation. This chaperone activity is crucial during cellular stress, where the risk of protein misfolding and aggregation is high .

Regulatory Mechanisms

The expression of HSPB3 is regulated by various stress conditions. Heat shock proteins, including HSPB3, are typically upregulated in response to increased temperatures, oxidative stress, and other environmental stressors. This upregulation is mediated by heat shock factors (HSFs), which are transcription factors that bind to heat shock elements (HSEs) in the promoter regions of heat shock protein genes .

Clinical Significance

HSPB3 has been implicated in several diseases and conditions. Its role in protein folding and protection against stress makes it a potential target for therapeutic interventions in diseases characterized by protein misfolding and aggregation, such as neurodegenerative diseases .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.