Rabbit HSP90AB1 Antibody | anti-HSP90AB1 antibody

HSP90AB1 Antibody

Cat. Num. AAA8503226

• Gene Names: HSP90AB1; HSP84; HSPC2; HSPCB; D6S182; HSP90B
• Reactivity: Human, Mouse, Rat
• Applications: Western Blot, Immunohistochemistry
• Purity: Affinity purification
• Synonyms: HSP90AB1; HSP90AB1 Antibody; D6S182; FLJ26984; HSP90-BETA; HSP90B; HSPC2; HSPCB; anti-HSP90AB1 antibody

• Host: Rabbit
• Reactivity: Human, Mouse, Rat
• Isotype: IgG
• Purity/Purification: Affinity purification
• Sequence Length: 724

• Applicable Applications for anti-HSP90AB1 antibody: Western Blot (WB), Immunohistochemistry (IHC)
• Application Notes: WB: 1:500-1:2000; IHC: 1:50-1:200
• Immunogen: Recombinant protein of human HSP90AB1
• Storage Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
• Preparation and Storage: Store at-20 degree C or-80 degree C. Avoid freeze/thaw cycles.

Related Product Information for anti-HSP90AB1 antibody

HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2, 3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1, 4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1, 3). They also play a role in vesicle formation and protein trafficking (2).

Product Categories/Family for anti-HSP90AB1 antibody

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

References

1. Nollen, E.A. and Morimoto, R.I. (2002) J. Cell Sci. 115, 2809-2816. 2. Young, J.C. et al. (2003) Trends Biochem. Sci. 28, 541-547. 3. Pratt, W.B. and Toft, D.O. (2003) Exp. Biol. Med. 228, 111-133. 4. Hohfeld, J. et al. (2001) EMBO Rep. 2, 885-890.

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: 83kDa
• 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
• Protein Family: Heat shock protein
• 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).