|The HSPA1A hspa1a (Catalog #MBS804083) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp70 Antibody: RPE reacts with Human, Mouse, Rat, Amphibian, Chicken, Fish, Saccharomyces cerevisiae, Fruit Fly, Artemia franciscana and may cross-react with other species as described in the data sheet. MyBioSource\'s Hsp70 can be used in a range of immunoassay formats including, but not limited to, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB).
1:100 (ICC/IF/IHC), 1:5000 (WB). Researchers should empirically determine the suitability of the HSPA1A hspa1a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
The HSPA1A hspa1a product has the following accession number(s) (GI #194248072) (NCBI Accession #NP_005336.3) (Uniprot Accession #P08107). Researchers may be interested in using Bioinformatics databases such as those available at The National Center for Biotechnology Information (NCBI) website for more information about accession numbers and the proteins they represent. Even researchers unfamiliar with bioinformatics databases will find the NCBI databases to be quite user friendly and useful.
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Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the Hsp70 Antibody: RPE with the following immunoassay(s):
Testing Data (Western blot analysis of Hsp70 in rat tissue mix using a 1:5000 dilution.)
Background Info: Detects several members of the hsp 70kDa gene family including Hsp70, Hsc70, and following heat shock, Hsp72 from yeast, Drosophila, fish, mouse, avian, amphibian and human samples. IF staining of Hsp70 in HS HeLa cells results in cytoplasmic staining
Scientific Background: Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (1). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (5). The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.