Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
Application |
Recommended Dilution |
1:1000 - 1:20000 |
10-20 μg/ml |
Assay dependent |
10 μg/ml |
1-20 μg/ml |
2 μg |
Assay dependent |
Not tested in other applications.
Calculated MW
Product Note
This antibody does not detect HSP86. The antibody is capable of precipitating HSP84 that is complexed with other proteins such as the aryl hydrocarbon (Ah) receptor.
Form
Liquid
Buffer
Buffer, 0.1% BSA
Preservative
0.05% Sodium azide
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Mouse
Immunogen
Synthetic peptide corresponding to residues P(2) E E V H H G E E E V E(13) of mouse HSP84.
Purification
Purified by antigen-affinity chromatography
Conjugation
Unconjugated
RRID
AB_11166571
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
heat shock protein 90 alpha (cytosolic), class B member 1 , 90kDa , AL022974 , C81438 , Hsp84 , Hsp84-1 , Hsp90 , Hspcb
Cellular Localization
Cytoplasm,Nucleus,Secreted,Cell membrane
Background
Heat shock proteins (HSP) are expressed in response to various biological stresses, including heat. HSP90 is a 90 kDa protein that is induced under stress conditions, but is also one of the most abundant cellular proteins found under non-stress conditions. HSP90 has been found to be associated with a number of other intracellular proteins, including steroid receptors, actin, tubulin, aryl hydrocarbon (Ah) receptor, and some kinases. Studies have shown that murine HSP90 exists as two forms, HSP84 and HSP86, coded by related but separate genes, with 86% amino acid sequence conservation. These forms are analogous to the two forms of human HSP90, HSP89 alpha and HSP89 beta. In an unstressed mouse fibroblast, the basal level of HSP84 is found to be double that of HSP86. However, after heat shock, HSP86 shows a greater increase. Studies also suggest that upon cellular differentiation, the level of HSP86, but not HSP84, decreases. HSP84 and HSP86, which may be subject to estrogenic regulation, have been found as components of the non-DNA binding form of mouse glucocorticoid receptor, but dissociated from the transformed DNA-binding form.
Database
Research Area