Recombinant Human Heat Shock 70 kDa Protein 1A

• Cat.No.: HSPA1A-321H
• Product Overview: Recombinant human Hsp70, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques (661 aa,72.2 kDa).

Specification

• Cat. No.: HSPA1A-321H
• Description: Hsp70 is a human heat shock protein. Hsp70 is an important part of the cell"s machinery for protein folding, and help to protect cells from stress. In most species, there are many proteins that belong to the hsp70 family. Some of these are only expressed under stress conditions, while some are present in cells under normal growth conditions and are not heat-inducible. They can be found in different cellular compartments (nuclear, cytosolic, mitochondrial, endoplasmic reticulum, etc.).
• Source: E.coli.
• Formulation: Liquid. In 20 mM Tris-HCl buffer (pH 7.5) containing 2 mM DTT.
• Molecular Weight: 72.2 kDa (661aa).
• Purity: > 95% by SDS – PAGE.
• Concentration: 1 mg/ml (determined by Bradford assay).
• Sequence: MGSSHHHHHH SSGLVPRGSH MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGD TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D
• Storage: Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.

Gene Information

• Gene Name: HSPA1A
• Synonyms: HSPA1A; heat shock 70kDa protein 1A; HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127; HSP70-1A; HSP70.1; HSP70-1/HSP70-2; HSP70-1A; OTTHUMP00000029287; heat shock 70kD protein 1A; heat shock-induced protein; heat shock 70kDa protein 1B; dnaK-type molecular chaperone HSP70-1; dnaK-type molecular chaperone HSP70-1.
• Gene ID: 3303
• mRNA Refseq: NM_005345.5
• Protein Refseq: NP_005336.3
• 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.