MA3-007 detects several members of the heat shock protein 70 kDa (HSP70) gene family including HSP70, HSC70, GRP78, and following heat shock, HSP72 from yeast, rat, Drosophila, fish, mouse, avian, amphibian and human samples.
MA3-007 has been successfully used in Western blot, immunofluorescence, gel shift, immunohistochemistry (frozen), and immunoprecipitation procedures. By Western blot, this antibody detects proteins from ~70 kDa to ~78 kDa representing different members of the HSP70 family. 2-dimensional gel electrophoresis is required to resolve the heat induced form of these proteins from their constitutively expressed counterparts. Immunofluorescence staining of HSP70 in heat shocked HeLa cells with MA3-007 results in cytoplasmic staining.
The MA3-007 antigen is recombinant human HSP70 over-expressed in E. coli. Epitope mapping with a panel of HSP70 deletion mutants suggests that the epitope recognized is located between amino acids 122-264 of human HSP70, a region that has been shown to be involved in ATP binding. This is the first monoclonal antibody reported to react with: 1) the ATP binding region of HSP70, 2) an epitope in the amino terminus of HSP70.
HSP70 is a Heat shock protein (HSP) which are expressed in response to various biological stresses, including high temperatures. There are several major families of HSPs that include HSP70, there are HSP90 and HSP100. The HSP70 family is a set of highly conserved proteins that are induced by a variety of biological stresses, including heat stress, in every organism in which the proteins have been examined. The human HSP70 family members include: HSP70, a protein which is strongly inducible in all organisms but which is also constitutively expressed in primate cells; HSP72, a 72 kDa protein that is induced exclusively under stress conditions; HSC70, or cognate protein, is a 72 kDa, constitutively expressed, protein which is involved in the uncoating of clathrin coated vesicles; GRP78, or BiP, is a glucose regulated 78 kDa protein localized in the endoplasmic reticulum; and p75, or HSP75, a 75 kDa protein that is found within the mitochondria. Further, HSP70 is encoded by an intronless gene and, in conjunction with other heat shock proteins, HSP70 stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and organelles. HSP70 is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The HSP70 gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins.
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Protein Aliases: 68 kDa heat shock protein; dnaK-type molecular chaperone HSP70-1; epididymis secretory protein Li 103; 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 70 kDa protein 3; heat shock 70kD protein 1A; heat shock 70kDa protein 1A; heat shock protein 70-1; heat shock protein, 70 kDa 3; heat shock-induced protein; heat shock-induced protein, Hspa70; Hsp68; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70-2; HSP70.1; HSP70.1/2; HSP70.1/HSP70.2; HSP70.2; HSP70.3; HSP70I; HSP72; HSPA1; inducible heat shock protein 70
Gene Aliases: HEL-S-103; hsp68; HSP70-1; HSP70-1A; Hsp70-2; Hsp70-3; HSP70.1; Hsp70.3; Hsp70A1; HSP70I; HSP72; HSPA1; HSPA1A; HSPA1B; Hspa2; HSX70