Western Blot: HSP70/HSPA1A Antibody (C92F3A-5) [NB110-61582] - analysis of Human cell lysates from various cell lines showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone C92 . Load: 15 ...read more
1 ug/ml of HSP70 Antibody was sufficient for detection of HSP70 in 20 ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary Antibody.
Reviewed Applications
Read 1 Review rated 5 using NB110-61582 in the following applications:
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
PBS (pH 7.4), 50% Glycerol
Preservative
0.1% Sodium Azide
Concentration
1 mg/ml
Purity
Protein G purified
Alternate Names for HSP70/HSPA1A Antibody (C92F3A-5)
dnaK-type molecular chaperone HSP70-1
FLJ54303
FLJ54370
FLJ54392
FLJ54408
FLJ75127
Heat shock 70 kDa protein 1/2
heat shock 70 kDa protein 1A/1B
heat shock 70kD protein 1A
heat shock 70kDa protein 1A
heat shock-induced protein
HSP70
HSP70.1/HSP70.2
HSP70-1
HSP70-1/HSP70-2
HSP70-1A
HSP70I
HSP72
HSPA1
HSPA1A
HSPA1B
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 50% identity (2). 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 (3). When hsp70 (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 (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). 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 (6). 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.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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