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HSP90B Colorimetric Cell-Based ELISA Kit

CAT: 0519-EKC1289Size: 1 Kit, containing one 96 Well Plate and all necessary reagentsDry Ice: NoHazardous: No
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CAT#:0519-EKC1289Size:1 Kit, containing one 96 Well Plate and all necessary reagents
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Description
The HSP90B Cell-Based ELISA Kit is a convenient, lysate-free, high throughput and sensitive assay kit that can monitor HSP90B protein expression profile in cells. The kit can be used for measuring the relative amounts of HSP90B in cultured cells as well as screening for the effects that various treatments, inhibitors (ie. siRNA or chemicals), or activators have on HSP90B.
Synonyms
HS90B; HSP 84; HSP90-beta; HSP90AB1; HSPC2; HSPCB; Heat shock protein HSP 90-beta
Gene Name
HSP90AB1
UniProt
P08238
Reactivity
Human, Mouse, Rat
Applications
ELISA
Sample Type
Cell lines
Detection Range
> 5000 cells/well
Function
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 that is 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 (PubMed:16478993, PubMed:19696785) . 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 (PubMed:27295069, PubMed:26991466) . 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. In the first place, they 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 (PubMed:25973397) . Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385) . Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673) . Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823) .
Molecular Weight
83264 MW
Shipping Conditions
Available
Storage Conditions
Store at 4°C for up to 6 months.
Other Gene Names
Heat shock protein HSP 90-beta
Subcellular Location
Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065) . Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673) . Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762) .

UniProtKB · P08238

Heat shock protein HSP 90-beta

HS90B_HUMAN · Homo sapiens

View on UniProt ↗
Primary accession
P08238
Review status
UniProtKB reviewed (Swiss-Prot)
Gene
HSP90AB1
Protein existence
1: Evidence at protein level
Organism
Homo sapiens (Human)
Taxonomy ID
9606
Alternative names
HSP 90
EC number
—
Processing
—
Secondary accessions
B2R5P0, Q5T9W7, Q9NQW0, Q9NTK6
Protein keywords

Technical term

3D-structureDirect protein sequencingProteomics identificationReference proteome

PTM

AcetylationGlycoproteinMethylationPhosphoproteinS-nitrosylationUbl conjugation

Ligand

ATP-bindingNucleotide-binding

Cellular component

Cell membraneCytoplasmMembraneNucleusSecreted

Molecular function

Chaperone

Biological process

Stress response