antibody

Anti-Hsp90 Mouse mAb

MBS475175

0.1 mL

335 USD

monoclonal

mouse

nonconjugated

[4B6-G2-H6]

human, mouse, rat

Antibody

Anti-Hsp90 Mouse mAb

[Hsp90]

[D6S182; FLJ26984; FLJ31884; Heat shock 86 kDa; heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha cytosolic class A member 1; Heat shock protein 90kDa alpha cytosolic class B member 1; Heat shock protein HSP 90 alpha; Heat shock protein HSP 90 beta; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 84; HSP 86; Hsp 90; HSP84; HSP86; Hsp89; Hsp90; HSP90 Beta; HSP90A; HSP90AA1; HSP90AB1; HSP90B; HSP90N; HSPC1; HSPC2; HSPCA; HSPCAL1; HSPCAL4; HSPCB; HSPN; LAP2; Lipopolysaccharide associated protein2; LPS associated protein 2; NY REN 38 antigen; Renal carcinoma antigen NY-REN-38]

[heat shock protein HSP 90-alpha isoform 1; Heat shock protein HSP 90-alpha; heat shock protein HSP 90-alpha; heat shock protein 90 alpha family class A member 1; Heat shock 86 kDa; HSP 86; HSP86; Lipopolysaccharide-associated protein 2; LAP-2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38]

[Hsp90]

[EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4.]

[HSP90AA1; HSP90AA1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; LAP-2; HSP89A; HSP90A; HSP90N; Hsp103; HSPCAL1; HSPCAL4; HEL-S-65p; HSP90A; HSPC1; HSPCA; HSP 86; HSP86; LAP-2; LPS-associated protein 2]

Monoclonal

IgG1

[4B6-G2-H6]

Mouse. Source: Human

Human, Mouse, Rat

854

Affinity Purified

Purified mouse monoclonal in PBS (pH 7.4) containing with 0.02% sodium azide and 50% glycerol.

2.25mg/ml

Western Blot (WB)

WB: 1:2000

Western Blot (WB)

Immunogen: Purified recombinant human HSP90AA1 protein fragments expressed in E Coli. Sensitivity: This antibody detects endogenous levels of Hsp90 alpha and Hsp90 beta. Sequence Similarities: Belongs to the heat shock protein 90 family.

Subunit Structure: Homodimer.Identified in NR3C1/GCR steroid receptor-chaperone complexes formed at least by NR3C1, HSP90AA1 and a variety of proteins containing TPR repeats such as FKBP4, FKBP5, PPID, PPP5C STIP1.Interacts with AHSA1, FNIP1, HSF1, SMYD3 and TOM34.Interacts with TERT; the interaction, together with PTGES3, is required for correct assembly and stabilization of the TERT holoenzyme complex.Interacts with CHORDC1 and DNAJC7.Interacts with STUB1 and UBE2N; may couple the chaperone and ubiquitination systems.Interacts (via TPR repeat-binding motif) with PPP5C (via TPR repeats); the interaction is direct and activates PPP5C phosphatase activity. Subcellular Location: Cytoplasm. Melanosome. Note:Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Signal Transduction; Protein Trafficking; Chaperones; Heat Shock Proteins; Cancer T; umor biomarkers; Other.

Entrez Summary: The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer.The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones.Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Jan 2012]

153792590

NP_001017963.2

NM_001017963

P07900

90

AhR Pathway (755436); Antigen Processing And Presentation Pathway (83074); Antigen Processing And Presentation Pathway (485); Axon Guidance Pathway (105688); Cell Cycle Pathway (530733); Cell Cycle, Mitotic Pathway (105765); Centrosome Maturation Pathway (105807); Class I PI3K Signaling Events Pathway (138022); Class I PI3K Signaling Events Mediated By Akt Pathway (138020); Developmental Biology Pathway (477129)

The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

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). 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). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205).

0.1 mL

335 USD