Hsp90 alpha Antibody (YA3692)(PBS only)

Cat. No.: HY-P83995A: Data Sheet User Guide for Antibodies
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Hsp90 alpha Antibody (YA3692) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp90 alpha.

For research use only. We do not sell to patients.

Size		Stock
50 μL		Get quote
100 μL		Get quote

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Documentation

Description

Hsp90 alpha Antibody (YA3692) is a Mouse-derived and non-conjugated IgG1 monoclonal antibody, targeting to Hsp90 alpha.

Host

Mouse

Molecular Weight

Predicted band size: 85 kDa;

Observed band size: 90 kDa

Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.

Species Reactivity

Human, Mouse, Monkey

SwissProt ID

P07900

Gene ID

3320 [NCBI]

Immunogen

Purified recombinant fragment of human HSP90AA1 aa 275-484.

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:500-1:2000
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:200-1:1000
FC FC: Flow Cytometry	1:200-1:400
ELISA ELISA: Enzyme Linked Immunosorbent Assay	1:10000

Purity	affinity purified.	Conjugation	Non-conjugated
Isotype	IgG1

Appearance

Liquid

Formulation

Supplied in PBS, pH 7.4.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Shipping

Shipping with blue ice.

Background

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:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). 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:26991466, PubMed:27295069). 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

Subcellular Localization：Nucleus; Cytoplasm; Melanosome; Cell membrane; Mitochondrion

Isoforms & Post-Translational Modification：P07900 has 2 isomers: P07900-1: 84660 Da (predicted); P07900-2: 98161 Da (predicted).
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

Subunit：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 or STIP1 (PubMed:15383005, PubMed:9195923). Forms a complex containing HSP90AA1, TSC1 and TSC2; TSC1 is required to recruit TCS2 to the complex (PubMed:29127155).

Synonyms

HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4

Documentation

User Guide for Antibodies (1077 KB)