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Mouse HSP90AB1 (Heat Shock Protein Hsp 90-beta) ELISA Kit
Mouse HSP90AB1 (Heat Shock Protein Hsp 90-beta) ELISA Kit
The Mouse (HSP90AB1) Heat Shock Protein Hsp 90-beta ELISA Kit measures Heat Shock Protein Hsp 90-Beta in Mouse samples. The plate has been pre-coated with Mouse HSP90AB1 antibody. HSP90AB1 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Mouse HSP90AB1 Antibody is added and binds to HSP90AB1 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated HSP90AB1 antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Mouse HSP90AB1. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
Catalog No:
E2124Mo
Regular price
$595.00 USD
Regular price
$458.00 USD
Sale price
$595.00 USD
Unit price
/
per
2.5 weeks
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Product Details
Species Reactivity
Mouse
Sensitivity
5.28 ng/L
Detection Range
10-2000 ng/L
Sample Type
Serum, plasma, cell culture supernates
Incubation(s)
1.5 hour(s)
Research Areas
Neuroscience
Background
Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10. Source: UniProt Consortium (2025)
Shipping Condition
Shipped on cold gel packs.
Storage Condition and Shelf Life
2-8C
Analyte
Heat Shock Protein Hsp 90-Beta
Regulatory Status
For Research Use Only
