All HSP70 reagents are produced in house and quality controlled, including 6 HSP70 Antibody, 29 HSP70 Gene, 2 HSP70 IPKit, 2 HSP70 Lysate, 2 HSP70 Protein, 1 HSP70 qPCR. All HSP70 reagents are ready to use.
Recombinant HSP70 proteins are expressed by Baculovirus-Insect Cells, HEK293 Cells with fusion tags as N-His.
HSP70antibodies are validated with different applications, which are ELISA, FCM, WB, IP, IHC-P, ICC/IF, IF.
HSP70cDNA clones are full length sequence confirmed and expression validated. There are 13 kinds of tags for each HSP70 of different species, especially GFP tag, OFP tag, FLAG tag and so on. There are three kinds of vectors for choice, cloning vector, expression vector and lentivrial expression vector.
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.