RP02123
Recombinant Human HSP70 Protein
Size
£259.00
- SKU:
- RP02123
- Additional Names:
- HSPA1A, HSP72, HSPA1, HSX70,Heat shock 70 kDa protein 1
- Molecular Weight:
- 70-80 kDa
- Purity:
- ≥90%
- Storage Conditions:
- -20[o]C reconstituted. Avoid freeze/thaw cycles., 2-8[o]C reconstituted., -20[o]C/-70[o]C lyophilized. Avoid freeze/thaw cycles.
- Supplier:
- Abclonal
- Immunogen:
- Ala2-Asp641
- Formulation:
- Recombinant Human HSP70 Protein is produced by HEK293 cells expression system. The target protein is expressed with sequence (Ala2-Asp641) of Human HSP70 (Accession #NP_005336.3) fused with His tag at the N-Terminus.
- Species:
- Human
- Uniprot:
- P0DMV8
- Synonyms:
- 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;heat shock 70 kDa protein 1A/1B;Heat shock 70 kDa protein 1B;Heat shock 70 kDa protein 2;heat shock 70kD protein 1A;heat shock 70kD protein 1B;heat shock 70kDa protein 1A;heat shock 70kDa protein 1B;heat shock-induced protein;HEL-S-103;HSP70-1;HSP70-1/HSP70-2;HSP70-1A;HSP70-1B;HSP70-2;HSP70.1;HSP70.1/HSP70.2;HSP70.2;HSP70I;HSP72;HSPA1;HSX70
- Extra Details:
- 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.
- Shipping Conditions:
- Blue Ice