Anti-Phospho-HSP90β (S254) antibody

Rs. 50,211.00
SKU stj91017

General Information

Product name Anti-Phospho-HSP90β (S254) antibody
Short Description
Description Rabbit polyclonal to Phospho-HSP90β (S254).
Applications WB,IHC,IF,ELISA
Dilution range WB 1:500-1:2000IHC 1:100-1:300IF 1:200-1:1000ELISA 1:40000
Protein Name Anti-Phospho-HSP90β (S254) antibody
Immunogen Synthesized peptide derived from human HSP90β around the phosphorylation site of S254.
Storage Instruction Store at -20°C, and avoid repeat freeze-thaw cycles.
Type of Usage For Research Use Only (RUO).

Product Properties

Host Rabbit
Clonality Polyclonal
Reactivity Mouse,Rat,Monkey
Conjugation Unconjugated
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Target

Gene ID
Gene Symbol
Molecular Weight 90 kDa
Database Links
Alternative Names Phospho-HSP90β (S254)
Heat shock protein HSP 90-beta antibody
HSP 90 antibody
Heat shock 84 kDa antibody
HSP 84 antibody
HSP84 antibody
HSP90B antibody
HSPC2 antibody
HSPCB antibody
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 . 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. 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 . 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 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 .
Cellular Localization Cytoplasm Melanosome Nucleus Secreted Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV . Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation . Secreted when associated with TGFB1 processed form (LAP) .
Tissue Specificity
Swiss-Prot Key

 

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