Mouse Hsp90 beta Monoclonal Antibody | anti-Hsp90beta antibody

Hsp90 beta (6A7) Mouse mAb

Cat. Num. AAA4753808

• Gene Names: HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry, Immunocytochemistry, Immunofluorescence
• Purity: Affinity purified
• Synonyms: Hsp90 beta; Monoclonal Antibody; Hsp90 beta (6A7) Mouse mAb; Heat shock 90KD protein 1 beta; HS90B; HSP90B; HSP90 beta; HSPCB; HSPC2; HSP 90b; HSP84; anti-Hsp90beta antibody

• Host: Mouse
• Reactivity: Human, Mouse, Rat
• Clonality: Monoclonal
• Isotype: IgG1
• Clone Number: 6A7-9E10-8G6
• Specificity: The antibody detects endogenous HSP90beta protein.
• Purity/Purification: Affinity purified
• Form/Format: PBS, pH7.4, containing 0.02% sodium azide as Preservative and 50% Glycerol.

• Applicable Applications for anti-Hsp90beta antibody: Western Blot (WB), Immunohistochemistry-Paraffin (IHC-P), Immunocytochemistry (ICC), Immunofluorescence (IF)
• Application Notes: WB: 1:1000-3000; FC/FACS: 1:200; IHC: 1:50-300
• Immunogen: Synthetic Peptide of HSP90beta
• Conjugation: Unconjugated
• Modification: Unmodified
• Cell Position: Cell membrane, Cytoplasm, Membrane, Nucleus, Secreted
• Preparation and Storage: Store at 4 degree C for short term. Store at -20 degree C for long term. Avoid freeze/thaw cycle.

Immunofluorescence (IF)

(Immunofluorescence analysis of Mouse-spleen tissue. 1,HSP90beta Monoclonal Antibody(M2)(red) was diluted at 1:200(4 degree C,overnight). 2, Cy3 labled Secondary antibody was diluted at 1:300(room temperature, 50min).3, Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B)

Immunofluorescence (IF)

(Immunofluorescence analysis of Rat-lung tissue. 1,HSP90beta Monoclonal Antibody(M2)(red) was diluted at 1:200(4 degree C,overnight). 2, Cy3 labled Secondary antibody was diluted at 1:300(room temperature, 50min).3, Picture B: DAPI(blue) 10min. Picture A:Target. Picture B: DAPI. Picture C: merge of A+B)

Western Blot (WB)

(Western blot analysis of 1) Hela, 2) Mouse Brain tissue, 3) Rat Brain tissue, diluted at 1:2000.)

Related Product Information for anti-Hsp90beta antibody

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).

Product Categories/Family for anti-Hsp90beta antibody

Primary antibody

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 90kDa alpha (cytosolic), 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; HSP90-beta; heat shock 84 kDa; heat shock 90kD protein 1, 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
• UniProt Entry Name: HS90B_HUMAN

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

HSP90B: 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. Homodimer. Interacts with p53/TP53. Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7. Interacts with FKBP4. Belongs to the heat shock protein 90 family.

Protein type: Chaperone; Heat shock protein

Chromosomal Location of Human Ortholog: 6p12

Cellular Component: nucleoplasm; signalosome; cell surface; membrane; mitochondrion; brush border membrane; basolateral plasma membrane; cytoplasm; apical plasma membrane; melanosome; inclusion body; cytosol

Molecular Function: protein binding; GTP binding; TPR domain binding; nitric-oxide synthase regulator activity; unfolded protein binding; double-stranded RNA binding; dATP binding; sulfonylurea receptor binding; kinase binding; protein kinase binding; ATP binding

Biological Process: axon guidance; positive regulation of nitric oxide biosynthetic process; protein folding; positive regulation of cell size; positive regulation of protein import into nucleus, translocation; positive regulation of protein binding; innate immune response; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; response to unfolded protein; response to salt stress; placenta development