Active Recombinant Human HSPA1A Protein, His-tagged

• Cat.No.: HSPA1A-066H
• Product Overview: Active N-terminal Histidine-tagged full length human Hsp70 protein (2-641) wsa purified from insect cells.

Specification

• Description: This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins.
• Source: Insect cell
• Species: Human
• Tag: His
• Bio-activity: ATPase activity confirmed by ADP detection assay.
• Molecular Mass: 71.7 kDa
• Protein length: 2-641
• Purity: ≥75% estimated by SDS-PAGE
• Stability: ≥ 1 year
• Storage: At -80 centigrade.
• Storage Buffer: 50 mM HEPES, pH 8.0, 150 mM sodium chloride, 1 mM DTT, and 10% glycerol

Gene Information

• Gene Name: HSPA1A heat shock protein family A (Hsp70) member 1A [ Homo sapiens (human) ]
• Official Symbol: HSPA1A
• Synonyms: HSPA1A; heat shock protein family A (Hsp70) member 1A; HSP72; HSPA1; HSP70I; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1A; HEL-S-103; heat shock 70 kDa protein 1A; HSP70-1/HSP70-2; HSP70.1/HSP70.2; Heat shock 70 kDa protein 1B; Heat shock 70 kDa protein 2; dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; epididymis secretory sperm binding protein; heat shock 70 kDa protein 1; heat shock 70 kDa protein 1/2; heat shock 70 kDa protein 1A/1B; heat shock 70kD protein 1A; heat shock 70kDa protein 1A; heat shock-induced protein
• 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.