HSP27 Human, His

Heat Shock Protein 27 Human Recombinant, His Tag
Cat. No.
BT17213
Source
Escherichia Coli.
Synonyms
HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.
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.
Shipped with Ice Packs
In Stock

Description

Recombinant Human HSP-27 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 24.9kDa. Hsp27 is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

Product Specs

Introduction
HSP27, also referred to as Estrogen-Regulated 24K protein or hsp 28, belongs to the mammalian small heat shock protein family. Its presence is observed in numerous tissues at basal levels, which significantly increase upon exposure to various stressors such as high temperatures, toxic metals, drugs, and oxidants. Furthermore, HSP27 undergoes phosphorylation at three specific sites (Ser15, Ser78, and Ser82) in vivo. This phosphorylation is mediated by protein kinases, including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38).
Description
Recombinant Human HSP-27, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 225 amino acids (specifically, amino acids 1 to 205). This protein has a molecular weight of 24.9 kDa. Notably, a 20 amino acid histidine tag is fused to the N-terminus of HSP-27. The purification process involves conventional chromatography techniques.
Physical Appearance
The product is a sterile, colorless solution that has been filtered for sterility.
Formulation
The HSP27 protein solution is formulated in a buffer containing 20mM Tris-Hcl, 1mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Minimize freeze-thaw cycles to maintain product integrity.
Purity
Analysis by SDS-PAGE confirms a purity greater than 95.0%.
Synonyms
HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK.

Product Science Overview

Introduction

Heat Shock Protein 27 (HSP27), also known as HSPB1, is a small chaperone protein that plays a crucial role in cellular stress responses. It is part of the small heat shock protein (sHsp) family, which includes other members like α-crystallin and Hsp20. HSP27 is involved in various cellular processes, including thermotolerance, inhibition of apoptosis, regulation of cell development, and differentiation .

Structure and Function

HSP27 has a highly conserved α-crystallin domain near its C-terminus, which is essential for its chaperone activity. This domain consists of 80 to 100 amino acids that fold into β-sheets, forming stable dimers. The N-terminus contains a less conserved WD/EPF domain, followed by a short variable sequence. The C-terminal region is highly flexible and polar, contributing to the protein’s solubility and stability .

HSP27 forms large oligomers with an average mass of around 500 kDa in vitro. These oligomers consist of stable dimers formed by the α-crystallin domains of neighboring monomers. The N-terminus is essential for the development of these large oligomers .

Mechanisms and Roles

HSP27 is overexpressed in various cellular stress states and is involved in regulating proteostasis by stabilizing protein conformation and promoting the refolding of misfolded proteins. It plays a significant role in protecting cells from multiple sources of stress injury, including oxidative stress, inflammatory responses, and apoptosis .

In addition to its intracellular functions, recent studies have shown that HSP27 can be found in the extracellular space, where it may signal via membrane receptors to alter gene transcription and cellular function .

Therapeutic Potential

HSP27 has been implicated in various disease states, including cardiovascular diseases, where it plays both protective and counter-protective roles. Targeting HSP27 is considered a promising strategy for the treatment of cardiovascular diseases due to its involvement in oxidative stress, inflammatory responses, and apoptosis .

Human Recombinant HSP27 with His Tag

Human recombinant HSP27 with a His tag is a form of the protein that has been genetically engineered to include a polyhistidine tag. This tag facilitates the purification of the protein using affinity chromatography techniques. The recombinant form retains the functional properties of the native protein and is used in various research applications to study its structure, function, and therapeutic potential.

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