Recombinant Human HSPA1A Protein (M1-D641), Tag Free

• Cat.No.: HSPA1A-0701H
• Product Overview: Recombinant Human GG-HSP70(M1-D641 end) Protein was expressed in Insect cell.

Specification

• Description: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation.
• Source: Insect cell
• Species: Human
• Tag: Non
• Form: Liquid
• Protein length: M1-D641
• Endotoxin: < 0.01 EU per μg of the protein
• Purity: 85%
• Stability: Samples are stable for up to twelve months from date of receipt at -20 to -80 centigrade.
• Storage: Store it under sterile conditions at -20 to -80 centigrade. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Storage Buffer: Supplied as sterile 50 mM Tris-HCl (pH 7.5), 200 mM NaCl, 5% glycerol, 1mM DTT
• Shipping: It is shipped out with blue ice.

Gene Information

• Gene Name: HSPA1A heat shock 70kDa protein 1A [ Homo sapiens (human) ]
• Official Symbol: HSPA1A
• Synonyms: HSPA1A; heat shock 70kDa protein 1A; heat shock 70kD protein 1A, HSPA1; heat shock 70 kDa protein 1A/1B; HSP70 1; HSP70-1/HSP70-2; HSP70.1/HSP70.2; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70 kDa protein 1/2; dnaK-type molecular chaperone HSP70-1; HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127
• Gene ID: 3303
• mRNA Refseq: NM_005345
• Protein Refseq: NP_005336
• MIM: 140550
• UniProt ID: P0DMV8

Reviews

05/11/2022

Using HSPA1A experiments can obtain consistent results and reduce the uncertainty of experiments.

01/26/2022

HSPA1A has good stability and is suitable for long-term storage and use.

01/10/2021

HSPA1A can effectively simulate the function of the target protein in vitro.

Q&As

How is HSPA1A associated with other proteins or diseases?

HSPA1A has multiple associations with other proteins and diseases. For example, it may interact with the p53 protein to affect the occurrence and progression of tumors, and may also be associated with neurodegenerative diseases and be involved in the pathogenesis of diseases such as Alzheimer's disease.

What is the role of HSPA1A in stressful conditions?

HSPA1A can protect cells from damage through synergistic effects with other molecular chaperones such as HSP70 and HSP40 under stressful conditions. In addition, it can also be involved in the regulation of apoptosis.

Does HSPA1A have therapeutic potential?

Yes, HSPA1A has therapeutic potential. In tumor therapy, drug suppression or gene therapy against HSPA1A may become a new way to treat tumors. At the same time, inhibitors against HSPA1A are also being developed.

What are the health effects of aberrant expression of HSPA1A?

Aberrant expression of HSPA1A may be associated with a variety of diseases, especially cancer, neurodegenerative diseases, etc. For example, in tumors such as lung, breast, and colon cancer, HSPA1A expression levels may be abnormally elevated.

How is the level of HSPA1A detected?

Levels of HSPA1A can be detected by methods such as immunohistochemistry, western blotting, and real-time PCR, which can assess the amount of HSPA1A in tissues and cells.

How is HSPA1A involved in the proper folding and transport of proteins?

This protein can bind to unfolded proteins to form multimeric complexes that facilitate proper folding and transport of proteins. In addition, it can also work synergistically with other molecular chaperones such as HSP70 and HSP40 to participate in the correct folding and transport of proteins.