HSPB6 Human

Heat Shock 27kDa Protein 6 Human Recombinant
Cat. No.
BT18591
Source
Escherichia Coli.
Synonyms
Heat Shock Protein, Alpha-Crystallin-Related, B6, Heat Shock 20 KDa-Like Protein P20, Hsp20, Protein Phosphatase 1, Regulatory Subunit 91, Epididymis Luminal Protein 55, Heat Shock Protein Beta-6, Protein Phosphatase 1, Regulatory Subunit 91, PPP1R91, HEL55, HspB6, Heat shock protein beta-6.
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

HSPB6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (1-160 a.a) and having a molecular mass of 19.7kDa.
HSPB6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Heat shock protein beta-6, also known as HSPB6, is a member of the small heat shock protein (HSP20) family. This gene encodes a heat shock protein. HSPB6 plays a role in smooth muscle relaxation. HSPB6 has been associated with diseases such as cerebral hemorrhage and cerebral amyloid angiopathy.
Description
Recombinant human HSPB6 protein was produced in E. coli. It is a single, non-glycosylated polypeptide chain containing 184 amino acids (residues 1-160) with a molecular mass of 19.7 kDa. The protein is fused to a 24 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A sterile, colorless solution.
Formulation
The HSPB6 protein solution (0.25 mg/mL) contains phosphate buffered saline (pH 7.4), 30% glycerol, 1 mM DTT, 1 mM EDTA, and 0.1 mM PMSF.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is greater than 95.0% as determined by SDS-PAGE.
Synonyms
Heat Shock Protein, Alpha-Crystallin-Related, B6, Heat Shock 20 KDa-Like Protein P20, Hsp20, Protein Phosphatase 1, Regulatory Subunit 91, Epididymis Luminal Protein 55, Heat Shock Protein Beta-6, Protein Phosphatase 1, Regulatory Subunit 91, PPP1R91, HEL55, HspB6, Heat shock protein beta-6.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMEIPVP VQPSWLRRAS APLPGLSAPG RLFDQRFGEG LLEAELAALC PTTLAPYYLR APSVALPVAQ VPTDPGHFSV LLDVKHFSPE EIAVKVVGEH VEVHARHEER PDEHGFVARE FHRRYRLPPG VDPAAVTSAL SPEGVLSIQA APASAQAPPP AAAK.

Product Science Overview

Introduction

Heat Shock Proteins (HSPs) are a group of proteins that are produced by cells in response to stressful conditions. They play a crucial role in protecting cells from damage and assisting in the proper folding and functioning of other proteins. Among these, the Heat Shock 27kDa Protein 6 (HSP27) is particularly significant due to its diverse roles in cellular processes.

What is Heat Shock 27kDa Protein 6?

Heat Shock 27kDa Protein 6, also known as HSP27 or HSPB1, is a small heat shock protein that functions as a molecular chaperone. It helps maintain denatured proteins in a folding-competent state, ensuring they do not aggregate and cause cellular damage . HSP27 is involved in various cellular processes, including stress resistance, actin organization, and apoptosis regulation .

Human Recombinant HSP27

Recombinant proteins are proteins that are genetically engineered in the laboratory. Human Recombinant HSP27 is produced by inserting the gene encoding HSP27 into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of HSP27, which can be used for research and therapeutic purposes .

Biological Functions

HSP27 is known for its role in:

  • Stress Response: HSP27 expression increases in response to environmental stressors such as heat, oxidative stress, and heavy metals. It helps protect cells by stabilizing proteins and preventing their aggregation .
  • Actin Cytoskeleton Organization: HSP27 interacts with actin, a structural protein, and helps in the organization and stabilization of the cytoskeleton .
  • Apoptosis Regulation: HSP27 can inhibit apoptosis (programmed cell death) by interacting with key components of the apoptotic machinery, thereby promoting cell survival under stress conditions .
Clinical Significance

HSP27 has been implicated in various diseases and conditions:

  • Cancer: Elevated levels of HSP27 have been observed in several types of cancer. It is believed to contribute to tumor progression and resistance to chemotherapy by inhibiting apoptosis .
  • Neurodegenerative Diseases: HSP27 is involved in the protection of neurons and has been studied for its potential therapeutic role in neurodegenerative diseases such as Alzheimer’s and Parkinson’s .
  • Cardiovascular Diseases: HSP27 has been shown to have a protective role in cardiovascular diseases by reducing oxidative stress and inflammation .
Research and Therapeutic Applications

Human Recombinant HSP27 is widely used in research to study its functions and mechanisms. It is also being explored for therapeutic applications, including:

  • Cancer Therapy: Targeting HSP27 to enhance the efficacy of chemotherapy and reduce resistance .
  • Neuroprotection: Developing treatments for neurodegenerative diseases by leveraging the protective effects of HSP27 .
  • Cardioprotection: Investigating the potential of HSP27 in protecting the heart from ischemic injury and other cardiovascular conditions .

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