Hsc70 (Hsp73) Antibody from ROCKLAND IMMUNOCHEMICALS INC.

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Antigenic SpecificityHsc70 (Hsp73)
CloneN27F3-4
Host SpeciesMouse
Reactive Specieshuman, mouse, rat, beluga, bovine, C. elegans, carp, chicken, cucumber, d. melanogaster, dog, guinea pig, hamster, monkey, pea, porcine, rabbit, salmon, sheep, trout, Xenopus
IsotypeIgG1
FormatProtein G purified
Size100 µg
Concentration1.0 mg/mL
ApplicationsELISA, Immunohistochemistry, Western Blot
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DescriptionThis Protein G purified monoclonal antibody reacts with human Hsc70 (Hsp73) protein. A BLAST analysis was used to suggest cross-reactivity with Hsc70 from human, bovine, mouse, rat, C.elegans, beluga, dog, chicken, Drosophila, carp, salmon, trout, guinea pig, hamster, monkey, pig, cucumber, pea, rabbit, sheep and Xenopus sources based on 100% homology with the immunizing sequence. This antibody recognizes both the inducible hsp and the constitutively expressed hsc as 72 kDa and 73 kDa proteins, respectively. Cross-reactivity with Hsp70 from other sources has not been determined. Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes, hsp70 genes exist as part of a multigene family. Hsp70s 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 one-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 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 (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.
ImmunogenThis Protein G purified monoclonal antibody was prepared using conventional hybridoma technology after repeated immunizations with a synthetic peptide corresponding to a region of human Hsc70 (Hsp73) protein.
Other NamesHeat shock cognate protein 71-kDa antibody, Heat shock protein 8 antibody, Heat-shock70-KD protein 10, formerly antibody, HSC54 antibody, HSC71 antibody, Hsc54, Hsc71, Hsc73, Hsp71, Hsp73, HspA10, HspA8, LAP1, NIP71, Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8
Gene, Accession #HSPA8, Gene ID: 3312, NCBI: NP_006588.1, UniProt: P11142
Catalog #200-301-A28
Price$485
Order / More InfoHsc70 (Hsp73) Antibody from ROCKLAND IMMUNOCHEMICALS INC.
Product Specific ReferencesPubMed: 27118681 // 31387996 // 32499518 // 33796071
ROCKLAND IMMUNOCHEMICALS INC.
ROCKLAND IMMUNOCHEMICALS INC.
ROCKLAND IMMUNOCHEMICALS INC.
PO Box 5199
Limerick PA 19468
P: 484-791-3823
P: 800.656.7625
F: 484.369.8654

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Technical Support: tech@rockland.com

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