- CITATIONS: 1
|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||70052 Da|
|Other Names||Heat shock 70 kDa protein 1A/1B, Heat shock 70 kDa protein 1/2, HSP70-1/HSP70-2, HSP701/HSP702, HSPA1A, HSPA1, HSX70|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-term of human Hsp70 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP70 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).|
|Cellular Location||Cytoplasm. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs|
|Tissue Location||HSPA1B is testis-specific.|
Provided below are standard protocols that you may find useful for product applications.
The 70-kDa Heat Shock Protein (Hsp70) is a highly conserved member of the molecular chaperone network commonly found in nuclear, cytosolic, mitochondrial and endoplasmic reticulum compartments of all eukaryotic and prokaryotic cells. Hsp70 uses ATP binding and hydrolysis to assist in efficient folding of both newly created and stress-denatured polypeptides. (1). Under environmental stress conditions, synthesis of Hsp70 is quickly up-regulated and redistributed throughout the cell. (2). It has been shown that Hsp70 has the ability to bind with high affinity to the plasma membrane, activate NF-KappaB and also up-regulate expression of pro-inflammatory cytokines tumor necrosis factor (TNF)-?, interleukin (IL)-1? and IL-6 in human monocytes (3).
1. Yam AY, et al. J Biol Chem 50:41252-61, 2005
2. Prohaszka Z, et al. Cell Stress Chaperones 1:17-22, 2002
3. Asea A. J Biol Chem 17:15028-34, 2002
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