|The Hsp70/Hsc70 n/a (Catalog #MBS802688) is an Antibody produced from Mouse and is intended for research purposes only. The product is available for immediate purchase. The Hsp70/Hsc70 (Plant) Antibody: ATTO 390 reacts with Various plant species. Does not cross-react with human, rat, bacteria (DNAKK) or human BIP. and may cross-react with other species as described in the data sheet. MyBioSource\'s Hsp70/Hsc70 can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB), ELISA (EIA).
1:1000 (WB). Researchers should empirically determine the suitability of the Hsp70/Hsc70 n/a 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.
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Please refer to the product datasheet for known applications of a given antibody. We\'ve tested the Hsp70/Hsc70 (Plant) Antibody: ATTO 390 with the following immunoassay(s):
Western Blot (WB) (Western Blot analysis of Duckweed (Lemma minor) Heat Shocked cell lysates showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone 5G1-95. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:1000.)
Background Info: Detects ~70kDa. Recognizes constitutive and inducible plant Hsp70 (Hsc70/Hsp72).
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.
Conjugate: ATTO 390. Storage Buffer: PBS pH 7.4, 50% glycerol, 0.09% sodium azide. In general, we may offer more than one antibody to a given target to enable options for the researcher. Available antibodies recognizing Hsp70/Hsc70 are readily searchable from our website. Different antibodies against the same target such as Hsp70/Hsc70 may be optimized or tested for different applications and species. This enables researchers to select the option that may be best for their model system, to screen more than antibody to determine which one may be best for their model system, as well as to use more than one antibody to follow up on and validate their results.