Active Recombinant Human HSPA1A

• Cat.No.: HSPA1A-266H
• Product Overview: Recombinant Human HSPA1A (Accession # AAD21816) was produced in E. coli-derived.

Specification

• Source: E. coli
• Species: Human
• Form: X mg/ml (X µM) in 50 mM HEPES pH 8, 100 mM NaCl, 5 mM DTT
• Bio-activity: HSP70/HSPA1A is a molecular chaperone that assists in the folding of nascent polypeptides and the refolding of denatured proteins, but can also promote their degradation in conjunction with specific E3 ligases, such as CHIP, if either of these processes proceeds inefficiently. Reaction conditions will need to be optimized for each specific application. We recommend an initial HSP70/HSPA1A concentration of 2-3 µM for in vitro use. IMPORTANT: HSP40/DNAJB1, or another suitable co-chaperone, is required for HSP70/HSPA1A activity and should be used at a concentration that is equimolar to HSP70/HSPA1A.
• Molecular Mass: Recombinant Human HSPA1A has a calculated MW of 70 kDa.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
• Storage: Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: In lyophilized state for 1 year (4ºC); After reconstitution under sterile conditions for 3 months (-70ºC).
• Tag: Non

Gene Information

• Gene Name: HSPA1A heat shock 70kDa protein 1A [ Homo sapiens ]
• 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: P08107
• Chromosome Location: 6p21.3

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.