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.
We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More
Citations
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Huszar, G; Stone, K; et al. Putative creatine kinase M-isoform in human sperm is identified as the 70-kilodalton heat shock protein HspA2. BIOLOGY OF REPRODUCTION 63:925-932(2000).
Scieglinska, D; Piglowski, W; et al. The HspA2 protein localizes in nucleoli and centrosomes of heat shocked cancer cells. JOURNAL OF CELLULAR BIOCHEMISTRY 104:2193-2206(2008).
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