HSP90B Antibody | anti-HSP90B antibody

HSP90B (Ab-254) Antibody

Cat. Num. AAA857210

• Gene Names: HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunofluorescence
• Purity: Affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
• Synonyms: HSP90B; HSP90B (Ab-254) Antibody; anti-HSP90B antibody

• Reactivity: Human, Mouse, Rat
• Specificity: HSP90B (Ab-254) antibody detects endogenous levels of total HSP90B protein.
• Purity/Purification: Affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
• Form/Format: In phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Sequence Length: 724

• Applicable Applications for anti-HSP90B antibody: Western Blot (WB), Immunohistochemistry (IHC), Immunofluorescence (IF)
• Application Notes: WB: 1:500~1:1000; IHC: 1:50-1:100; IF: 1:100-200
• Immunogen: The antiserum was produced against synthesized non-phosphopeptide derived from human HSP90B around the phosphorylation site of serine 254 (V-G-SP-D-E)
• Preparation and Storage: Store at-20 degree C for 1 year

Immunohistochemistry (IHC)

(Peptide-+ Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue, using HSP90B (Ab-254) antibody.)

Western Blot (WB)

(Western blot analysis of extract from HeLa cells, untreated or treated with UV or Heat shock, using HSP90B (Ab-254) antibody.)

Product Categories/Family for anti-HSP90B antibody

Autophagy antibody; Cancer; Cardiovascular; Cell Biology; Epigenetics & Nuclear Signaling; Developmental Biologys; Immunology; Drug Discovery Products; Metabolism; Neuroscience; Signal Transduction; Stem Cells

References

Zhao R, Houry WA.(2007) Adv Exp Med Biol; 594: 27-36. Olsen JV, et al. (2006) Cell; 127(3): 635-648 Ogiso H, et al. (2004) Biochemistry; 43(49): 15510-15519.

NCBI and Uniprot Product Information

• NCBI GI #: 431822401
• NCBI GeneID: 3326
• NCBI Accession #: NP_001258898.1
• NCBI GenBank Nucleotide #: NM_001271969.1
• UniProt Accession #: P08238; Q5T9W7; Q9NQW0; Q9NTK6; B2R5P0
• Molecular Weight: 83,264 Da
• NCBI Official Full Name: heat shock protein HSP 90-beta isoform a
• NCBI Official Synonym Full Names: heat shock protein 90 alpha family class B member 1
• NCBI Official Symbol: HSP90AB1
• NCBI Official Synonym Symbols: HSP84; HSPC2; HSPCB; D6S182; HSP90B
• NCBI Protein Information: heat shock protein HSP 90-beta
• UniProt Protein Name: Heat shock protein HSP 90-beta
• UniProt Gene Name: HSP90AB1
• UniProt Synonym Gene Names: HSP90B; HSPC2; HSPCB; HSP 90; HSP 84; HSP84

NCBI Description

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]

Uniprot Description

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).