HSP70 Proteins, Antibodies, cDNA Clones Research Reagents

HSPA1A (Heat Shock Protein Family A (Hsp70) Member 1A, also known as HSP72; HSPA1; HSP70I; HSP70-1; HSP70-2; HSP70.1; HSP70.2; HSP70-1A; HEL-S-103), located on 6p21.33, is a Protein Coding gene. The gene produces a 70052 Da protein composed of 641 amino acids. HSPA1A is a member of the Hsp7 protein family. Diseases such as Transient Cerebral Ischemia and Carotid Artery Occlusion are associated with HSPA1A. The related pathways of HSPA1A include Apoptosis Modulation and Signaling and HIF1Alpha Pathway.

HSP70 Protein (4)

    HSP70 Antibody (6)

      HSP70 cDNA Clone (29)

      HSP70 qPCR Primer (1)

      HSP70 Lysate (4)

        HSP70 Background

        HSPA1A is a member of the Hsp70 protein family. The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. HSP are abundant and conserved proteins present in all cells. Upon temperature shock or other stress stimuli, HSP is synthesized intracellularly, which may protect cells from protein denaturation or death. Extracellularly, HSP can serve a cytokine function to initiate both innate and adaptive immunity through activation of APC. HSP serves also a chaperone function and facilitates the presentation of antigen peptide to T cells. Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the folding of newly synthesized and stress-denatured proteins, as well as the import of proteins into organelles, and the dissociation of aggregated proteins. The well-conserved Hsp70 chaperones are ATP dependent: binding and hydrolysis of ATP regulate their interactions with unfolded polypeptide substrates, and ATPase cycling is necessary for their function. All cellular functions of Hsp70 chaperones use the same mechanism of ATP-driven polypeptide binding and release.

        HSP70 References

        • Heck TG, et al. (2011) HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain Cell Biochem Funct. 29 (3): 215-26.
        • Chen T, et al. (2010) Stress for maintaining memory: HSP70 as a mobile messenger for innate and adaptive immunity. Eur J Immunol. 40 (6): 1541-4.
        • Young JC. (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol. 88 (2): 291-300.

        Note: Flag® is a registered trademark of Sigma Aldrich Biotechnology LP. It is used here for informational purposes only.