Product: Hsp90 beta Antibody
Catalog: AF6126
Description: Rabbit polyclonal antibody to Hsp90 beta
Application: WB IHC IF/ICC IP
Cited expt.: WB, IF/ICC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Chicken, Xenopus
Mol.Wt.: 96/83kDa; 83kD(Calculated).
Uniprot: P08238
RRID: AB_2835010

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IP, 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,Monkey
Prediction:
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
Hsp90 beta Antibody detects endogenous levels of total Hsp90 beta.
RRID:
AB_2835010
Cite Format: Affinity Biosciences Cat# AF6126, RRID:AB_2835010.
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

90 kda heat shock protein beta HSP90 beta; D6S182; FLJ26984; Heat shock 84 kDa; Heat shock 90kD protein 1, beta; Heat shock 90kDa protein 1 beta; Heat shock protein 90 alpha family class B member 1; Heat shock protein 90 kDa; Heat shock protein 90kDa alpha (cytosolic) class B member 1; Heat shock protein 90kDa alpha family class B member 1; Heat shock protein beta; Heat shock protein HSP 90 beta; Heat shock protein HSP 90-beta; HS90B_HUMAN; HSP 84; HSP 90; HSP 90 b; HSP 90b; HSP84; HSP90 BETA; hsp90ab1; HSP90B; HSPC2; HSPCB;

Immunogens

Immunogen:

A synthesized peptide derived from human Hsp90 beta, corresponding to a region within the internal amino acids.

Uniprot:
Gene(ID):
Description:
Molecular chaperone. Has ATPase activity.
Sequence:
MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD

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
Sheep
100
Xenopus
100
Zebrafish
100
Chicken
100
Rabbit
100
Dog
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. 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription.

PTMs:

Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).

ISGylated.

S-nitrosylated; negatively regulates the ATPase activity.

Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.

Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation.

Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins.

Subcellular Location:

Cytoplasm. Melanosome. Nucleus. Secreted. Cell membrane.
Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762).

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.

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). EEF1A2 interacts with HSP90AB1 to promote lung adenocarcinoma metastasis via enhancing TGF-β/SMAD signalling. BRITISH JOURNAL OF CANCER, 2021 (PubMed: 33473168) [IF=6.4]

Application: WB    Species: human    Sample: A549 cells

Fig. 5 |EEF1A2 interacts with the ATP-binding domain of HSP90AB1. a Cell lysates from 293 T cells transfected with Flag-EEF1A2 were immunoprecipitated using anti-Flag agarose and visualised by Coomassie blue staining. Interacting proteins were identified by liquid chromatography mass spectrometry (LC-MS)/MS. b A549 cells were transfected with Flag-EEF1A2, and the proteins were immunoprecipitated with Flag monoclonal antibody. The HSP90AB1 and HSP90AA1 were detected by immunoblotting.

Application: WB    Species: human    Sample: A549 cells

Supplementary Figure 3.| EEF1A2 interacts with HSP90AB1. (D) Confocal images shown position of co-location EEF1A2 (green) and HSP90AB1 (red) after transfection of si-EEF1A2 or si-HSP90AB1 in A549 cells. Images were acquired at 400×. Scale bar = 50 µm.

2). Myricetin ameliorates bleomycin-induced pulmonary fibrosis in mice by inhibiting TGF-β signaling via targeting HSP90β. BIOCHEMICAL PHARMACOLOGY, 2020 (PubMed: 32535102) [IF=5.3]

3). CTNNAL1 enhances glucocorticoid sensitivity in HDM-induced asthma mouse model through deactivating hsp90 signaling pathway. LIFE SCIENCES, 2023 (PubMed: 36535402) [IF=5.2]

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: ESCC

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: ESCC

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). Vorapaxar Prove to Be a Promising Candidate for Pulmonary Fibrosis by Intervening Thrombin/PAR1/JAK/STAT Signaling Pathway. , 2022

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