• Western blot analysis of various lysates, using HSP90AA1 Rabbit polyclonal antibody (STJ11105239) at 1:500 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (STJS000856) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit. Exposure time: 90s.

Anti-HSP90AA1 antibody (STJ11105239)

SKU:
STJ11105239

Current Stock:
Host: Rabbit
Applications: WB
Reactivity: Human/Mouse
Note: STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Short Description: Rabbit polyclonal antibody anti-Heat Shock Protein Hsp 90-Alpha is suitable for use in Western Blot research applications.
Clonality: Polyclonal
Conjugation: Unconjugated
Isotype: IgG
Formulation: PBS with 0.05% Proclin300, 50% Glycerol, pH7.3.
Purification: Affinity purification
Dilution Range: WB 1:100-1:500
Storage Instruction: Store at-20°C for up to 1 year from the date of receipt, and avoid repeat freeze-thaw cycles.
Gene Symbol: HSP90AA1
Gene ID: 3320
Uniprot ID: HS90A_HUMAN
Immunogen: Recombinant protein of human HSP90AA1.
Immunogen Sequence: AAKKHLEINPDHSIIETLRQ KAEADKNDKSVKDLVILLYE TALLSSGFSLEDPQTHANRI YRMIKLGLGIDEDDPTADDT SAAVTEEMPPLEGDDDTSRM EEVD
Post Translational 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.
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. 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. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. 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. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response. (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.
Protein Name Heat Shock Protein Hsp 90-Alpha
Heat Shock 86 Kda
Hsp 86
Hsp86
Lipopolysaccharide-Associated Protein 2
Lap-2
Lps-Associated Protein 2
Renal Carcinoma Antigen Ny-Ren-38
Database Links Reactome: R-HSA-1227986
Reactome: R-HSA-1236382
Reactome: R-HSA-1474151
Reactome: R-HSA-168928
Reactome: R-HSA-192905
Reactome: R-HSA-2029482
Reactome: R-HSA-203615
Reactome: R-HSA-2565942
Reactome: R-HSA-3000484
Reactome: R-HSA-3371497
Reactome: R-HSA-3371511
Reactome: R-HSA-3371568
Reactome: R-HSA-3371571
Reactome: R-HSA-380259
Reactome: R-HSA-380270
Reactome: R-HSA-380284
Reactome: R-HSA-380320
Reactome: R-HSA-399954
Reactome: R-HSA-4420097
Reactome: R-HSA-5218920
Reactome: R-HSA-5336415
Reactome: R-HSA-5601884
Reactome: R-HSA-5620912
Reactome: R-HSA-5637810
Reactome: R-HSA-5675482
Reactome: R-HSA-6785807
Reactome: R-HSA-6798695
Reactome: R-HSA-8852276
Reactome: R-HSA-8854518
Reactome: R-HSA-8863795
Reactome: R-HSA-8939211
Reactome: R-HSA-9009391
Reactome: R-HSA-9013418
Reactome: R-HSA-9018519
Reactome: R-HSA-9613829
Reactome: R-HSA-9634285
Reactome: R-HSA-9646399
Reactome: R-HSA-9652282
Reactome: R-HSA-9664565
Reactome: R-HSA-9665233
Reactome: R-HSA-9665244
Reactome: R-HSA-9665245
Reactome: R-HSA-9665246
Reactome: R-HSA-9665247
Reactome: R-HSA-9665249
Reactome: R-HSA-9665250
Reactome: R-HSA-9665251
Reactome: R-HSA-9665348
Reactome: R-HSA-9665686
Reactome: R-HSA-9665737
Reactome: R-HSA-9679191
Reactome: R-HSA-9705671
Cellular Localisation Nucleus
Cytoplasm
Melanosome
Cell Membrane
Mitochondrion
Identified By Mass Spectrometry In Melanosome Fractions From Stage I To Stage Iv
Alternative Antibody Names Anti-Heat Shock Protein Hsp 90-Alpha antibody
Anti-Heat Shock 86 Kda antibody
Anti-Hsp 86 antibody
Anti-Hsp86 antibody
Anti-Lipopolysaccharide-Associated Protein 2 antibody
Anti-Lap-2 antibody
Anti-Lps-Associated Protein 2 antibody
Anti-Renal Carcinoma Antigen Ny-Ren-38 antibody
Anti-HSP90AA1 antibody
Anti-HSP90A antibody
Anti-HSPC1 antibody
Anti-HSPCA antibody

Information sourced from Uniprot.org

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