HSPB8 Human, His

Heat Shock 22kDa Protein 8 Human Recombinant, His Tag
Cat. No.
BT18783
Source
Escherichia Coli.
Synonyms
HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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

HSPB8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 23.7kDa. The HSPB8 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography.

Product Specs

Introduction
As a member of the small heat-shock protein superfamily, HSPB8 possesses a conserved alpha-crystallin domain located at its C-terminal. Estrogen induces HSPB8 expression in estrogen receptor-positive breast cancer cells. Functioning as a chaperone protein, HSPB8 associates with BAG3, a macroautophagy stimulator. HSPB8 plays a role in regulating cell proliferation, apoptosis, and carcinogenesis. Mutations in the HSPB8 gene have been linked to various neuromuscular diseases, including Charcot-Marie-Tooth disease.
Description
Recombinant HSPB8 Human, manufactured in E. coli, is a single, non-glycosylated polypeptide chain comprising 216 amino acids (1-196 a.a.). It has a molecular weight of 23.7kDa. The HSPB8 protein is fused to a 20 amino acid His Tag at the N-terminus and purified using conventional chromatography.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HSPB8 protein solution is formulated in 20mM Tris-HCl (pH 8), 100mM NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined to be greater than 95.0% by SDS-PAGE analysis.
Synonyms
HSPB8, H11, HMN2, CMT2L, DHMN2, E2IG1, HMN2A, HSP22, Heat shock protein beta-8, Alpha-crystallin C chain, Small stress protein-like protein HSP22, E2-induced gene 1 protein, Protein kinase H11, CRYAC.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MADGQMPFSC HYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTASWPD WALPRLSSAW PGTLRSGMVP RGPTATARFG VPAEGRTPPP FPGEPWKVCV NVHSFKPEEL MVKTKDGYVE VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD PVTVFASLSP EGLLIIEAPQ VPPYSTFGES SFNNELPQDS QEVTCT.

Product Science Overview

Introduction

Heat Shock 22kDa Protein 8 (HSPB8), also known as Heat Shock Protein Beta-8 or HSP22, is a member of the small heat shock protein (sHSP) family. These proteins play crucial roles in cellular protection under stress conditions, such as elevated temperatures, toxins, and other environmental stressors .

Structure

HSPB8 contains a conserved alpha-crystallin domain at the C-terminal part of the molecule, which is characteristic of the small heat shock protein family . The recombinant form of HSPB8 is often tagged with a His (histidine) tag to facilitate purification and detection in experimental settings .

Function

HSPB8 exhibits chaperone-like activity, which is essential for its role in various cellular processes, including protein folding, stabilization, and repair . It is predominantly expressed in skeletal muscle and heart tissues . HSPB8 is involved in the regulation of cell proliferation, apoptosis, and macroautophagy, often in association with the co-chaperone Bag3 .

Mode of Action

HSPB8 functions as a molecular chaperone, preventing improper intra- and intermolecular interactions. It helps in the folding and stabilization of newly synthesized proteins and the repair of damaged proteins . Additionally, HSPB8 undergoes autophosphorylation and can phosphorylate exogenous protein substrates, indicating its role as an atypical serine/threonine protein kinase .

Regulation

The expression of HSPB8 is induced by various stress conditions, including heat shock, toxins, and inflammation . It is also regulated by estrogen in estrogen receptor-positive breast cancer cells . Mutations in the HSPB8 gene have been associated with neuromuscular diseases such as Charcot-Marie-Tooth disease and distal hereditary motor neuropathy .

Clinical Significance

HSPB8’s chaperone activity and its role in cellular stress responses make it a potential target for therapeutic interventions in neurodegenerative diseases and cancers . Its involvement in protein homeostasis and cell survival pathways highlights its importance in maintaining cellular integrity under stress conditions .

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