HSP70/HSPA1A Antibody (SA0379) Summary
Additional Information |
Recombinant Monoclonal Antibody. |
Immunogen |
Recombinant protein within Human HSP70/HSPA1A aa 403-641 / 641. (SwissProt: P0DMV9 Human; SwissProt: P0DMV8 Human; SwissProt: P17879 Mouse; SwissProt: Q61696 Mouse; SwissProt: Q07439 Rat) |
Localization |
Cytoplasm |
Isotype |
IgG |
Clonality |
Monoclonal |
Host |
Rabbit |
Gene |
HSPA1A |
Purity |
Protein A purified |
Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Applications/Dilutions
Dilutions |
- Flow Cytometry 1:50-1:100
- Immunocytochemistry/ Immunofluorescence 1:50-1:200
- Immunohistochemistry
- Immunohistochemistry-Paraffin 1:50-1:500
- Western Blot 1:500-1:5000
|
Packaging, Storage & Formulations
Storage |
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles. |
Buffer |
TBS (pH7.4), 0.05% BSA, 40% Glycerol |
Preservative |
0.05% Sodium Azide |
Concentration |
1 mg/ml |
Purity |
Protein A purified |
Alternate Names for HSP70/HSPA1A Antibody (SA0379)
Background
Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eucaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eucaryotes 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. 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. 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. 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. 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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Secondary Antibodies
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Isotype Controls
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