Human HSPA1A recombinant protein (N-His)

Human HSPA1A recombinant protein (N-His)

• DataSheet
• Material Safety Data Sheets (MSDS)

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 are synthesized intracellularly, which may protect cells from protein denaturation or from 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 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 regulates 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. 

Epididymis secretory protein Li 103

HEL-S-103,HSP70-1,HSP70-1A,HSP70I,HSP72,HSPA1

A8K5I0

Epididymis secretory protein Li 103; Heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; cDNA FLJ75127, highly similar to Homo sapiens heat shock 70kDa protein 1A, mRNA

Human Cells

A DNA sequence encoding the human HSPA1A (NP_005336.3) (Ala2-Asp641) was expressed with a polyhistidine tag at the N-terminus.

Human

The recombinant human HSPA1A consists of 651 amino acids and predicts a molecular mass of 71.4 kDa.

> 95 % as determined by SDS-PAGE.