Product: Hsp90 alpha Antibody
Catalog: AF5368
Description: Rabbit polyclonal antibody to Hsp90 alpha
Application: WB IHC IF/ICC
Cited expt.: WB, IHC, IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Rabbit, Dog, Chicken
Mol.Wt.: 83 kDa; 85kD(Calculated).
Uniprot: P07900
RRID: AB_2837853

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 100ul $280 In stock
 200ul $350 In stock

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%), Dog(100%), Chicken(100%)
Clonality:
Polyclonal
Specificity:
Hsp90 alpha Antibody detects endogenous levels of total Hsp90 alpha.
RRID:
AB_2837853
Cite Format: Affinity Biosciences Cat# AF5368, RRID:AB_2837853.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

EL52; epididymis luminal secretory protein 52; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; Heat shock 90kD protein 1, alpha like 4; heat shock 90kD protein, alpha-like 4; Heat shock 90kDa protein 1 alpha; Heat shock protein 90kDa alpha (cytosolic) class A member 1; Heat shock protein HSP 90-alpha; HS90A_HUMAN; HSP 86; HSP86; Hsp89; HSP89A; Hsp90; HSP90A; HSP90AA1; HSP90ALPHA; HSP90N; HSPC1; HSPCA; HSPCAL1; HSPCAL4; HSPN; LAP 2; LAP2; lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38;

Immunogens

Immunogen:

A synthesized peptide derived from human Hsp90 alpha, corresponding to a region within C-terminal amino acids.

Uniprot:
Gene(ID):
Description:
FunctionMolecular chaperone. Has ATPase activity.Sequence similaritiesBelongs to the heat shock protein 90 family.Post-translational modificationsISGylated.
Sequence:
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Dog
100
Chicken
100
Rabbit
100
Sheep
0
Xenopus
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

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. 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.

PTMs:

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.

Subcellular Location:

Nucleus. Cytoplasm. Melanosome. Cell membrane.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Family&Domains:

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperone STUB1.

Belongs to the heat shock protein 90 family.

Research Fields

· Cellular Processes > Cell growth and death > Necroptosis.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Genetic Information Processing > Folding, sorting and degradation > Protein processing in endoplasmic reticulum.   (View pathway)

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Prostate cancer.   (View pathway)

· Organismal Systems > Immune system > Antigen processing and presentation.   (View pathway)

· Organismal Systems > Immune system > NOD-like receptor signaling pathway.   (View pathway)

· Organismal Systems > Immune system > IL-17 signaling pathway.   (View pathway)

· Organismal Systems > Immune system > Th17 cell differentiation.   (View pathway)

· Organismal Systems > Endocrine system > Progesterone-mediated oocyte maturation.

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)

References

1). Hsp90β promotes aggressive vasculogenic mimicry via epithelial-mesenchymal transition in hepatocellular carcinoma. ONCOGENE, 2023 (PubMed: 30087438) [IF=6.9]

Application: IHC    Species: human    Sample: HCC cells

Fig. 1| Hsp90βassociates with vasculogenic mimicry and poor prog-nosis in HCC. e Representative images of Hsp90β, Hsp90α, VE-cadherin,E-cadherin, Vimentin, MMP2, and MMP9 expression in VM/Hsp90βnegative and positive HCC tissue samples. All images are repre-sentative.

Application: WB    Species: human    Sample: PLC-PRF-5 cells

Fig. 3| Hsp90β interacts with Twist1 in HCC. a Immunopurification and mass spectrometry analysis of Hsp90β-(left) and Twist1-associated proteins (right). b Whole-cell lysates from PLC-PRF-5 cells were immunoprecipitated (IP) followed by immunoblotting (IB)with antibodies against the indicated proteins.

2). RETRACTED ARTICLE: Hsp90β promotes aggressive vasculogenic mimicry via epithelial–mesenchymal transition in hepatocellular carcinoma. Oncogene, 2018 (PubMed: 30087438) [IF=6.9]

3). Sequential targeting biomimetic nano platform for enhanced mild photothermal therapy and chemotherapy of tumor. Computational and structural biotechnology journal, 2023 (PubMed: 37181660) [IF=4.4]

Application: WB    Species: Mouse    Sample: CAFs and 4T1cells

Fig. 4. Synergistic in vitro cancer inhibition effects of PTT and chemotherapy strategy mediated by mPDA/Cur@M/CM. (A) In vitro viability of CAFs treated with mPDA/Cur@M/CM at different curcumin concentrations with or without laser irradiation (808 nm, 0.4 W/cm2, 10 min) (A). Viability of CAFs cells received different treatment (B). In vitro viability of 4T1 cells treated with mPDA/Cur@M/CM containing different curcumin concentrations in the presence or absence of laser irradiation (808 nm, 0.4 W/cm2, 10 min) (C). Viability of 4T1 cells received different treatment (D), n = 4, ∗p 

4). HSP90 Inhibitor Ganetespib (STA-9090) Inhibits Tumor Growth in c-Myc-Dependent Esophageal Squamous Cell Carcinoma. OncoTargets and Therapy, 2020 (PubMed: 32308431) [IF=2.7]

Application: IF/ICC    Species: Human    Sample: Eca-109 cells

Figure 1 MYC was over-expressed and interacted with HSP90 in ESCC. (A and B) MYC’ nuclear expression in ESCC. Images from TMA immunostained for MYC. Scale bars represent 50 μm. (C) MYC expression against HSP90 expression status showing 50% of double-positive samples. (D) Western blotting examined the expression of MYC in ESCC tumor tissues and adjacent normal tissues (n=12). (E) Localization of HSP90 and MYC in Eca-109 cells by immunofluorescence. Scale bars represent 25 μm. (F) Interaction of endogenous HSP90 with MYC was detected by co-IP assays in Eca-109 cells. ***P < 0.001.

Application: WB    Species: Human    Sample: Eca-109 cells

Figure 1 MYC was over-expressed and interacted with HSP90 in ESCC. (A and B) MYC’ nuclear expression in ESCC. Images from TMA immunostained for MYC. Scale bars represent 50 μm. (C) MYC expression against HSP90 expression status showing 50% of double-positive samples. (D) Western blotting examined the expression of MYC in ESCC tumor tissues and adjacent normal tissues (n=12). (E) Localization of HSP90 and MYC in Eca-109 cells by immunofluorescence. Scale bars represent 25 μm. (F) Interaction of endogenous HSP90 with MYC was detected by co-IP assays in Eca-109 cells. ***P < 0.001.

5). Comparative proteomics identify HSP90A, STIP1 and TAGLN‑2 in serum extracellular vesicles as potential circulating biomarkers for human adenomyosis. Experimental and Therapeutic Medicine, 2022 (PubMed: 35495589) [IF=2.4]

Application: WB    Species: human    Sample: T‑AMEVs and B‑AMEVs

Figure 4. | HSP90A, STIP1 and TAGLN‑2 are expressed in B‑AMEVs and T‑AMEVs. (D and E) HSP90A, STIP1 and TAGLN‑2 were present in T‑AMEVs and B‑AMEVs from patients with adenomyosis,but not in those of patients in the control group.

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