Rabbit Polyclonal Antibody to HSP70(Discontinued)
Figure-1 : Western blot analysis of HSP70 Antibody at 1 µg/ml on Hela, HEK29, NIH/3T3 cell lysate and Mouse brain tissue lysate.
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Format : | Purified |
Amount : | 40 µg |
Isotype : | Rabbit IgG |
Purification : | Immunoaffinity chromatography |
Content : | 0.5 mg/ml, lyophilized with PBS, pH 7.4, containing 0.02% sodium azide |
Storage condition : | The antibody is stable in lyophilized form if stored at -20°C or below. The reconstituted antibody can be stored for 2-3 weeks at 2-8°C. For long term storage, aliquot and store at -20°C or below. Avoid repeated freezing and thawing cycles. |
HSP70 is a member of the chaperonin family. It stabilizes existing proteins against aggregation and mediates the folding of newly translated polypeptides in both cytosol and organelles. HSP70 participates in all of these processes through its ability to recognize nonnative conformations of other proteins. It binds extended peptide segments with a net hydrophobic character exposed during translation and membrane translocation or following stress-induced damage. Rabbit Anti-HSP70 Polyclonal Antibody is developed in rabbit hosts using a KLH-coupled synthetic peptide within N-terminal of human HSP70 protein.
ELISA: 0.05-0.2 µg/ml
Western blot: 1-2 µg/ml
Immunhistochemistry: 10-15µg/ml
Flowcytometry :1-2 µg/10^6 Cells
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
Subcellular location: | Cytoplasm, Nucleus, Cytoplasm |
Post transnational modification: | In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages. Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1. The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively. Acetylation also protects cells against various types of cellular stress. |
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