APPLICATION
Application Note
For IP: Use at an assay dependent dilution. This antibody can be used for immunoprecipitation of free and complexed Hsp90. For WB: Use at a dilution of 1:500. Detects a band of approximately 90 kDa (predicted molecular weight: 84.7 kDa(alpha) and 83.2 kDa (beta)). Optimal dilutions/concentrations should be determined by the researcher.
Positive Control
HeLa Cell Lysate (Heat Shocked). Hsp90 Protein.
Product Note
Recognises both alpha and beta forms of Hsp90.
PROPERTIES
Form
Liquid
Buffer
PBS pH7.2, 0.1mM PMSF, 50% Glycerol
Preservative
No preservative
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
Batch dependent (Please refer to the vial label for the specific concentration.)
Antigen Species
Mouse
Immunogen
Mouse Hsp90 isolated from Hepa 1 cytosol (murine hepatoma cell line 1c1c7
Purification
Purified IgM
Ammonium sulphate precipitated.
Conjugation
Unconjugated
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.
TARGET
Synonyms
FLJ31884 , HSP86 , HSP89A , HSP90A , HSP90N , HSPC1 , HSPCA , HSPCAL1 , HSPCAL4 , HSPN , Hsp89 , Hsp90 , LAP2
Cellular Localization
Cytoplasmic
Background
The 90kDa molecular chaperone family comprises several proteins including the 90kDa heat shock protein, Hsp90 and the 94kDa glucose regulated protein, grp94 which are major molecular chaperones of the cytosol and of the endoplasmic reticulum. In mammalian cells there are at least two Hsp90 isoforms, Hsp90a and hsp90s which are encoded by separate genes. The amino acid sequence of human and yeast Hsp90a is 85% and 90% homologous to that of Hsp90s respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N terminal and C terminal regions which have been shown to contain independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 is part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by nonphysiological conditions. However, in the absence of stress, Hsp90 is a necessary component of fundamental cellular processes such as hormone signaling and cell cycle control. In this context several key regulatory proteins such as steriod receptors, cell cycle kinases involved in signal transduction and p53 have been identified as substrates of Hsp90. It has been suggested that Hsp90 acts as a capacitor for morphological evolution by buffering widespread variation, which may affect morphogenic pathways.
Research Area
DATA IMAGES
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GTX13480 WB Image
Western Blot analysis of HSP90 mAb (2D12).
Lane 1: MW marker
Lane 2: HSP90 (human) (native)
Lane 3: HeLa HS, (cell lysate)
Lane 4: Vero Heat Shock Cell Lysate
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REFERENCE
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REVIEW
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