Recombinant Rabbit Anti-HSP90AA1 Antibody (clone R08-8A1) (CAT#: VS3-FY705)

• Immunogen
• Human Hsp90β recombinant protein.

• Host Species
• Rabbit

• Type
• Rabbit IgG

• Specificity
• Human, Mouse, Rat HSP90AA1

• Species Reactivity
• Human, Mouse, Rat

• Clone
• R08-8A1

• Applications
• Western Blot, Immunohistochemistry-Frozen, Immunohistochemistry-Paraffin, Immunocytochemistry, Immunofluorescence, Immunoprecipitation

• Conjugate
• Unconjugated

• MW
• Calculated MW: 85 kDa; Observed MW: 90 kDa

• Purification
• Affinity Purified

• Purity
• >95% as determined by SDS-PAGE

• Buffer
• 50 mM Tris-Glycine, pH 7.4, 0.15 M NaCl, 40% glycerol, 0.05% BSA

• Preservative
• 0.01% Sodium azide

• Storage
• Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

• Application Notes
• Western Blot: 1/500-1/1000
  Immunohistochemistry-Paraffin: 1/50-1/100
  Immunofluorescence: 1/50-1/200
  Immunoprecipitation: 1/20

• Alternative Names
• Heat Shock Protein 90 Alpha Family Class A Member 1; Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1; Lipopolysaccharide-Associated Protein 2; Heat Shock 90kDa Protein 1, Alpha; Renal Carcinoma Antigen NY-REN-38; Heat Shock 90kD Protein 1, Alpha; LPS-Associated Protein 2; Heat Shock 86 KDa; HSP 86; HSP90A; HSPC1; HSPCA; HSP86; LAP-2; Heat Shock Protein 90kDa Alpha Family Class A Member 1; Epididymis Secretory Sperm Binding Protein Li 65p

• Gene ID
• 3320

• UniProt ID
• P07900

• Sequence Similarities
• Belongs to the heat shock protein 90 family.

• Cellular Localization
• Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

• Post Translation Modifications
• ISGylated.
  S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1.
  Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways.

• Protein Refseq
• NP_001017963.2; NP_005339.3

• 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 which is essential for its chaperone 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:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155, PubMed:12526792).
  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 (PubMed:29127155).
  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).
  Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792).
  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 (PubMed:25973397).
  In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397).
  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 (PubMed:25973397).
  Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397).
  Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205).
  Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
  Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812).
  (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion.

Secondary Antibody

• 2ND-054CQ
• Goat Anti-Rabbit IgG Antibody, R-PE

• 2ND-055CQ
• Chicken Anti-Rabbit IgG (H&L) Antibody

• 2ND-057CQ
• Donkey Anti-Rabbit IgG (H&L) Antibody

• 2ND-059CQ
• Goat Anti-Rabbit IgG (H&L) Antibody

• 2ND-060CQ
• Llama Anti-Rabbit IgG (H&L) Antibody

• 2ND-061CQ
• Sheep Anti-Rabbit IgG (H&L) Antibody

Isotype Control

• MOB-208CQ
• Rabbit IgG Isotype Control Antibody