Description
Recombinant Human HSP70/HSPA1A Protein (His Tag)(Active) | PKSH030303 | Gentaur US, UK & Europe Disrtribition
Synonyms: HEL-S-103;HSP70-1;HSP70-1A;HSP70I;HSP72;HSPA1
Active Protein: Active protein
Activity: A DNA sequence encoding the human HSPA1A (NP_005337.2) (Ala2-Asp641) was expressed, with a polyhistidine tag at the N-terminus.
Protein Construction: A DNA sequence encoding the human HSPA1A (NP_005337.2) (Ala2-Asp641) was expressed, with a polyhistidine tag at the N-terminus.
Fusion Tag: N-His
Species: Human
Expressed Host: Baculovirus-Insect Cells
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 85 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per µg as determined by the LAL method.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 72.2 kDa
Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4, 10% gly
Reconstitution: Please refer to the printed manual for detailed information.
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 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.
Research Area: N/A
