HSPA1B Human

Heat Shock 70kDa protein 1B Human Recombinant

Cat. No.

BT17688

Source

Escherichia Coli.

Synonyms

Heat shock 70kDa protein 1B, HSP70-2, HSP70-1/HSP70-2, FLJ54328, HSPA1A, heat shock 70kDa protein 1A/1B, HSPA1.

Appearance

Filtered White lyophilized (freeze-dried) powder.

Purity

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

The HSPA1B Protein Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 650 amino acids having a molecular mass of 71.16kDa.
HSPA1B is fused to a 10 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

The HSP70 protein family is present in various cellular compartments, including chloroplasts, endoplasmic reticulum, mitochondria, and the cytosol. These proteins are produced in response to diverse biological stresses, such as heat stress, across all organisms. HSP70 proteins have multiple functions, such as acting as molecular chaperones that assist in assembling multi-protein complexes, participating in polypeptide translocation across cell membranes and into the nucleus, and aiding in the correct folding of newly synthesized polypeptide chains.
HSP70 is an essential component of the mitochondrial import machinery and plays a crucial role in the cytosolic endoplasmic reticulum. Recent studies have also revealed that extracellular HSP70 is involved in triggering cellular immune responses.

Description

Recombinant Human HSPA1B protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 650 amino acids with a molecular weight of 71.16 kDa.
HSPA1B is expressed with a 10 amino acid His-Tag fused to the N-terminus and purified using proprietary chromatographic methods.

Physical Appearance

The product appears as a white lyophilized (freeze-dried) powder after filtration.

Formulation

The protein solution, at a concentration of 0.5 mg/ml in 50 mM phosphate buffer with 75 mM NaCl at pH 7.4, was filtered through a 0.4 μm filter before lyophilization.

Solubility

To prepare a 0.5 mg/ml working stock solution, add deionized water to the lyophilized pellet and allow it to dissolve completely. It is important to note that the product is not sterile. Before using in cell culture, filter the product through an appropriate sterile filter.

Stability

While lyophilized HSPA1B remains stable at room temperature for up to 3 weeks, it is recommended to store the desiccated product at a temperature below -18°C. After reconstitution, store HSPA1B at 4°C for 2-7 days. For long-term storage, keep it frozen below -18°C.
Repeated freeze-thaw cycles should be avoided.

Synonyms

Heat shock 70kDa protein 1B, HSP70-2, HSP70-1/HSP70-2, FLJ54328, HSPA1A, heat shock 70kDa protein 1A/1B, HSPA1.

Source

Escherichia Coli.

Amino Acid Sequence

MKHHHHHHAS AKAAAIGIDL GTTYSCVGVF QHGKVEIIAN DQGNRTTPSY VAFTDTERLI GDAAKNQVAL NPQNTVFDAK RLIGRKFGDP VVQSDMKHWP FQVINDGDKP KVQVSYKGET KAFYPEEISS MVLTKMKEIA EAYLGYPVTN AVITVPAYFN DSQRQATKDA GVIAGLNVLR IINEPTAAAI AYGLDRTGKG ERNVLIFDLG GGTFDVSILT IDDGIFEVKA TAGDTHLGGEDFDNRLVNHF VEEFKRKHKK DISQNKRAVR RLRTACERAK RTLSSSTQAS LEIDSLFEGI DFYTSITRAR FEELCSDLFR STLEPVEKAL RDAKLDKAQI HDLVLVGGST RIPKVQKLLQ DFFNGRDLNK SINPDEAVAY GAAVQAAILM GDKSENVQDL LLLDVAPLSL GLETAGGVMT ALIKRNSTIP TKQTQIFTTY SDNQPGVLIQ VYEGERAMTK DNNLLGRFEL SGIPPAPRGVPQIEVTFDID ANGILNVTAT DKSTGKANKI TITNDKGRLS KEEIERMVQE AEKYKAEDEV QRERVSAKNA LESYAFNMKS AVEDEGLKGK ISEADKKKVL DKCQEVISWL DANTLAEKDE FEHKRKELEQ VCNPIISGLY QGAGGPGPGG FGAQGPKGGS GSGPTIEEVD.

Product Science Overview

Introduction

Heat Shock 70kDa Protein 1B (HSPA1B) is a member of the heat shock protein 70 (Hsp70) family, which plays a crucial role in cellular processes. These proteins are highly conserved and are known for their ability to protect cells from stress by stabilizing proteins and assisting in their proper folding.

Gene and Protein Structure

The HSPA1B gene is located on the short arm of chromosome 6, within the major histocompatibility complex (MHC) class III region . This gene is intronless and encodes a protein that is approximately 70 kDa in size. The HSPA1B protein shares a high degree of similarity with other members of the Hsp70 family, particularly HSPA1A, due to synonymous substitutions in their DNA sequences.

Function

HSPA1B functions as a molecular chaperone, which means it assists in the folding and stabilization of newly synthesized proteins and the refolding of misfolded proteins . It also plays a role in the ubiquitin-proteasome pathway by interacting with the AU-rich element RNA-binding protein 1. This interaction is crucial for the degradation of misfolded proteins, thereby maintaining cellular proteostasis.

Expression and Regulation

The expression of HSPA1B is highly inducible under stress conditions such as heat shock, exposure to toxic chemicals, and other environmental stresses. This induction is part of the cellular stress response mechanism, which helps in protecting cells from damage.

Clinical Significance

HSPA1B has been implicated in various diseases and conditions. For instance, its expression is associated with acute pancreatitis and chronic hepatitis B and C infections. Additionally, it plays a role in the rapid proliferation, metastasis, and inhibition of apoptosis in certain cancers, including ovarian, bladder urothelial, and breast cancers.

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HSPA1B Human

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