HSPA8 Human
Heat Shock 70kDa Protein-8 Human Recombinant
Cat. No.
BT18213
Source
Escherichia Coli.
Synonyms
LAP1, HSC54, HSC70, HSC71, HSP1, HSP73, NIP71, HSPA10, MGC29929, MGC131511, HSPA8, Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% 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 HSC70 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 666 amino acids (1-646 a.a.) and having a molecular mass of 73.1kDa.
HSC70 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
HSC70 human recombinant is fused to 20 amino acid His Tag at N-terminus and purified by convential chromatogrpahy techniques.
Product Specs
Introduction
HSPA8, a member of the heat shock protein 70 family, encompasses both heat-inducible and constitutively expressed proteins known as heat-shock cognate proteins. As a heat-shock cognate protein, HSPA8 binds to newly formed polypeptide chains, ensuring their proper folding. It functions as an ATPase, playing a crucial role in disassembling clathrin-coated vesicles by facilitating the movement of membrane components within the cell. Found in colon cancer cells, HSPA8 participates in the disassembly of the reovirus outer capsid during membrane penetration, preparing the virus for gene expression and replication. Notably, serum HSPA8 levels decrease during normal human pregnancy. HSPA8 also plays a role in the effects of androgens on dermal papilla cells. Furthermore, HSPA8 exhibits a direct interaction with the influenza virus matrix protein 1, making it essential for viral production.
Description
Recombinant Human HSC70, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 666 amino acids (specifically, amino acids 1 to 646). It possesses a molecular mass of 73.1 kDa. This recombinant human HSC70 is fused to a 20 amino acid His Tag at its N-terminus and is purified using conventional chromatography techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The HSC70 protein solution is formulated with 20mM Tris buffer at a pH of 8 and contains 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep the vial refrigerated at 4°C. For extended storage, freeze at -20°C. To ensure optimal stability during long-term storage, consider adding a carrier protein such as HSA or BSA at a concentration of 0.1%. It is important to minimize repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 90.0%, as determined by SDS-PAGE analysis.
Synonyms
LAP1, HSC54, HSC70, HSC71, HSP1, HSP73, NIP71, HSPA10, MGC29929, MGC131511, HSPA8, Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD.
Product Science Overview
Classification and Structure
HSPA8 belongs to the heat-shock cognate subgroup of the Hsp70 family, which includes both heat-inducible and constitutively expressed members . The protein has a molecular weight of approximately 70 kDa and consists of two main domains:
- N-terminal ATP-binding domain: This domain is responsible for binding and hydrolyzing ATP, which is crucial for the protein’s chaperone activity.
- C-terminal substrate-binding domain: This domain binds to nascent polypeptides and misfolded proteins, facilitating their proper folding .
The substrate-binding domain is further divided into two subdomains: a two-layered β-sandwich subdomain (SBDβ) and an α-helical subdomain (SBDα), connected by a loop. The ATP-binding domain consists of four subdomains split into two lobes by a central ATP/ADP binding pocket .
Biological Properties and Functions
HSPA8 plays a critical role in maintaining cellular protein homeostasis. It acts as a molecular chaperone, assisting in the proper folding of newly synthesized and misfolded proteins, preventing protein aggregation, and facilitating protein transport . Some of its key functions include:
- Protein folding: HSPA8 binds to nascent polypeptides and helps them achieve their correct three-dimensional structure.
- Protein transport: It is involved in the transport of proteins across cellular membranes.
- Antigen presentation: During nutrient stress, HSPA8 participates in antigen transport to regulate MHC class II presentation .
Modes of Action
Regulatory Mechanisms
Quick Inquiry
Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
