HSPA5 (19-654) Human

Heat Shock 70kDa protein 5 (19-654 a.a.) Human Recombinant
Cat. No.
BT17828
Source
Escherichia Coli.
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTeks 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

HSPA5 (19-654) Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 659 amino acids (19-654) and having a molecular mass of 72.9kDa.
HSPA5 (19-654) is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Binding immunoglobulin protein (BiP or HSPA5), a member of the heat shock protein family (HSP70), is a 70kDa stress response protein. Its production increases when the endoplasmic reticulum (ER) experiences stress due to various factors or conditions. HSPA5 plays a crucial role in ensuring proper protein glycosylation and folding, maintaining cellular equilibrium, and preventing cell death.
Description
Recombinant human HSPA5 (19-654), produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 659 amino acids (19-654) and has a molecular weight of 72.9kDa. This protein includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear solution that has been sterilized by filtration.
Formulation
The HSPA5 (19-654) solution is provided at a concentration of 1mg/ml and contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT, and 20% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing.
Purity
Purity is greater than 90% as assessed by SDS-PAGE.
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEEEDKKE DVGTVVGIDL GTTYSCVGVF KNGRVEIIAN DQGNRITPSY VAFTPEGERL IGDAAKNQLT SNPENTVFDA KRLIGRTWND PSVQQDIKFL PFKVVEKKTK PYIQVDIGGG QTKTFAPEEI SAMVLTKMKE TAEAYLGKKV THAVVTVPAY FNDAQRQATK DAGTIAGLNV MRIINEPTAA AIAYGLDKRE GEKNILVFDL GGGTFDVSLL TIDNGVFEVV ATNGDTHLGG EDFDQRVMEH FIKLYKKKTG KDVRKDNRAV QKLRREVEKA KRALSSQHQA RIEIESFYEG EDFSETLTRA KFEELNMDLF RSTMKPVQKV LEDSDLKKSD IDEIVLVGGS TRIPKIQQLV KEFFNGKEPS RGINPDEAVA YGAAVQAGVL SGDQDTGDLV LLDVCPLTLG IETVGGVMTK LIPRNTVVPT KKSQIFSTAS DNQPTVTIKV YEGERPLTKD NHLLGTFDLT GIPPAPRGVP QIEVTFEIDV NGILRVTAED KGTGNKNKIT ITNDQNRLTP EEIERMVNDA EKFAEEDKKL KERIDTRNEL ESYAYSLKNQ IGDKEKLGGK LSSEDKETME KAVEEKIEWL ESHQDADIED FKAKKKELEE IVQPIISKLY GSAGPPPTGE EDTAEKDEL.

Product Science Overview

Introduction

Heat Shock 70kDa Protein 5, also known as HSPA5, is a member of the heat shock protein 70 (HSP70) family. This protein plays a crucial role in the cellular response to stress and is involved in the folding and assembly of proteins within the endoplasmic reticulum (ER). The recombinant form of this protein, specifically the 19-654 amino acid sequence, is often used in research to study its functions and interactions.

Discovery and Function

The heat shock proteins were first discovered in the 1960s by Ferruccio Ritossa, who observed that heat stress induced the production of specific proteins in Drosophila (fruit flies) . HSPA5, in particular, is localized to the lumen of the ER, where it operates as a chaperone. It assists in the proper folding of nascent proteins and the assembly of multi-protein complexes, ensuring that proteins achieve their correct conformation and functionality .

Role in Cellular Stress Response

HSPA5 is a master regulator of ER homeostasis. It is strongly upregulated in response to various stress conditions, including heat stress and exposure to toxic chemicals such as heavy metals (e.g., arsenic, cadmium, copper, mercury) . By preventing the aggregation of misfolded proteins and facilitating their degradation, HSPA5 helps maintain cellular health and function under stress conditions.

Recombinant HSPA5 (19-654 a.a.)

The recombinant form of HSPA5, encompassing amino acids 19 to 654, is produced using recombinant DNA technology. This involves inserting the gene encoding HSPA5 into an expression vector, which is then introduced into a host cell (such as bacteria or yeast) to produce the protein. The recombinant protein is purified and used in various research applications, including studies on protein folding, stress response, and ER function .

Applications in Research

Recombinant HSPA5 is widely used in biochemical and cell biology research. It serves as a valuable tool for studying the mechanisms of protein folding and the cellular response to stress. Additionally, it is used in drug discovery and development, particularly in the context of diseases associated with protein misfolding and ER stress, such as neurodegenerative disorders and cancer .

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