Recombinant Human HSP70 / HSPA1A Protein (Catalog#11660-H07B)
This antibody was produced from a hybridoma resulting from the fusion of a mouse myeloma with B cells obtained from a mouse immunized with purified, recombinant Human HSP70 / HSPA1A (rh HSP70 / HSPA1A; Catalog#11660-H07B; NP_005337.2; Ala2-Asp641). The IgG fraction of the cell culture supernatant was purified by Protein A affinity chromatography.
Monoclonal Mouse IgG1 Clone #12
0.2 μm filtered solution in PBS
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Anti-HSP70 Antibody, Mouse Monoclonal 经验证的应用
Please Note: Optimal concentrations/dilutions should be determined by the end user.
Anti-HSP70 Antibody, Mouse Monoclonal 图片
Immunochemical staining of human HSPA1A in human hepatoma with mouse monoclonal antibody (1:60, formalin-fixed paraffin embedded sections).
Immunochemical staining of human HSPA1A in human prostatic carcinoma with mouse monoclonal antibody (1:60, formalin-fixed paraffin embedded sections).
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.
heat shock 70kDa protein 1A
Death Receptor Signaling
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.