Rabbit Recombinant Monoclonal HS90A antibody. Suitable for IHC-P, WB and reacts with Human, Mouse, Rat samples. Cited in 7 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
IHC-P | IP | Flow Cyt | WB | |
---|---|---|---|---|
Human | Tested | Not recommended | Not recommended | Tested |
Mouse | Expected | Not recommended | Not recommended | Tested |
Rat | Expected | Not recommended | Not recommended | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/50 | Notes The mouse and rat recommendation is based on the WB results. We do not guarantee IHC-P for mouse and rat. For unpurified use at 1/100 - 1/250. Perform heat-mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol. |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat, Human | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse, Rat, Human | Dilution info - | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Human | Dilution info 1/1000 - 1/10000 | Notes - |
Species Mouse | Dilution info 1/1000 - 1/10000 | Notes - |
Species Rat | Dilution info 1/1000 - 1/10000 | Notes - |
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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.
HSP90A, HSPC1, HSPCA, HSP90AA1, Heat shock protein HSP 90-alpha, Heat shock 86 kDa, Heat shock protein family C member 1, Lipopolysaccharide-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP 86, HSP86, LAP-2, LPS-associated protein 2
Rabbit Recombinant Monoclonal HS90A antibody. Suitable for IHC-P, WB and reacts with Human, Mouse, Rat samples. Cited in 7 publications.
pH: 7.2 - 7.4
Preservative: 0.01% Sodium azide
Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA
The mouse and rat recommendation is based on the WB results. We do not guarantee IHC-P for mouse and rat.
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.
This product is a recombinant monoclonal antibody, which offers several advantages including:
For more information, read more on recombinant antibodies.
Hsp90 also known as heat shock protein 90 is a molecular chaperone with a mass of about 90 kDa. It assists in the proper folding of client proteins stabilization of proteins against heat stress and degradation of misfolded proteins. Hsp90 is present in various cellular compartments including the cytoplasm nucleus and mitochondria. It is highly expressed in most eukaryotic cells reflecting its fundamental role in maintaining cellular protein homeostasis. Additionally Hsp90 serves as a loading control in western blot experiments due to its consistent expression levels across samples.
Hsp90 interacts with many co-chaperones to form multi-protein complexes that aid its function. This protein is necessary for the maturation and stability of many signaling proteins including steroid hormone receptors and kinases like the tyrosine kinase D7A. Hsp90's chaperone activity is ATP-dependent with its N-terminal domain binding and hydrolyzing ATP leading to conformational changes that promote protein folding and assembly. Its influence extends to regulating cell cycle control and apoptosis highlighting its importance in cellular processes.
Hsp90 participates in key biological pathways such as the protein folding response and the MAPK signaling pathway. In the protein folding process Hsp90 collaborates with co-chaperones like Aha1 and p23 to ensure accurate protein synthesis and repair. Its role in the MAPK signaling pathway influences cell growth proliferation and differentiation interacting with proteins like Raf-1 and MEK. These interactions highlight Hsp90's involvement in signal transduction and cellular stress responses.
Hsp90 is implicated in cancer and neurodegenerative diseases. Its overexpression often correlates with tumor progression and poor prognosis in cancers where it stabilizes client proteins like HER2 and AKT that drive oncogenic processes. In neurodegenerative disorders such as Alzheimer's disease altered Hsp90 function affects the degradation of proteins like tau contributing to pathogenic protein aggregation. Understanding Hsp90's role in these conditions offers avenues for therapeutic interventions targeting its chaperone activity.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
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All lanes: Western blot - Anti-Hsp90 antibody [EPR3953] (ab109248) at 1/1000 dilution
Lane 1: HeLa (Human cervix adenocarcinoma epithelial cell) whole cell lysates at 20 µg
Lane 2: HEK-293 (Human embryonic kidney epithelial cell) whole cell lysates at 20 µg
Lane 3: RAW264.7 (Mouse Abelson murine leukemia virus-induced tumor macrophage) whole cell lysates at 20 µg
Lane 4: NIH/3T3 (Mouse embryonic fibroblast) whole cell lysates at 20 µg
Lane 5: PC-12 (Rat adrenal gland pheochromocytoma ) whole cell lysates at 20 µg
All lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) (Goat Anti-Rabbit IgG H&L (HRP) ab97051) at 1/20000 dilution
Predicted band size: 85 kDa
Observed band size: 90 kDa
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) analysis of Human lung carcinoma tissue sections labeling Hsp90 with purified ab109248 at 1:50 dilution (19.42 μg/ml). Heat mediated antigen retrieval was performed using Antigen Retrieval Buffer (100X Tris-EDTA Buffer, pH 9.0) ab93684 (Tris/EDTA buffer, pH 9.0). ImmunoHistoProbe one step HRP Polymer (ready to use)was used as the secondary antibody. Negative control:PBS instead of the primary antibody. Hematoxylin was used as a counterstain.
ab109248, at 1/100, staining Hsp90 in paraffin-embedded Human gastric adenocarcinoma tissue by Immunohistochemistry.
Heat mediated antigen retrieval was performed with citrate buffer pH 6 before commencing with IHC staining protocol.
ab109248, at 1/100, staining Hsp90 in paraffin-embedded Human kidney tissue by Immunohistochemistry.
Heat mediated antigen retrieval was performed with citrate buffer pH 6 before commencing with IHC staining protocol.
Blocking and dilution buffer: 5% NFDM/TBST.
All lanes: Western blot - Anti-Hsp90 antibody [EPR3953] (ab109248) at 1/1000 dilution
Lane 1: Western blot - Recombinant Human Hsp90 alpha protein (His tag) (Recombinant Human Hsp90 alpha protein (His tag) ab48801) at 0.015 µg
Lane 2: Western blot - Recombinant human Hsp90 beta protein (Active) (Recombinant human Hsp90 beta protein (Active) ab80033) at 0.015 µg
All lanes: Western blot - Goat Anti-Rabbit IgG H&L (HRP) (Goat Anti-Rabbit IgG H&L (HRP) ab97051) at 1/20000 dilution
Predicted band size: 85 kDa
Observed band size: 90 kDa
Exposure time: 5s
Image collected and cropped by CiteAb under a CC-BY license from the publication
Hsp90 western blot using anti-Hsp90 antibody [EPR3953] ab109248. Publication image and figure legend from Guo, W., Yan, L., et al., 2014, PLoS One, PubMed 24465691.
ab109248 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab109248 please see the product overview.
MKT-077 potentiates 17-AAG-induced translocation of p53 to the nuclei in HCC cells.(A, B) Bel-7402 and HuH7 cells were treated with MKT-077, 17-AAG or a combination of both agents at the indicated concentrations for 24 hours. Cytoplasmic and nuclear fractions of Bel-7402 and HuH7 cells were separated, and subjected to Western blot analysis of p53 expression. α-tublin and Lamin B1 served as loading controls for cytoplasmic and nuclear fractions respectively. (C) Hep3B cells infected with Lenti-p53 (Hep3B-p53+/+) were treated with MKT-077, 17-AAG or MKT-077+17-AAG at indicated dosages for 24 hours, and immunofluorescent staining was performed to determine p53 subcellular localization. (D) Bel-7402 cells treated with MKT-077 or 17-AAG alone, or MKT-077+17-AAG for 24 hours were harvested and subjected to co-immunoprecipitation using GRP75-specific antibodies. Levels of p53, Akt and HSP90 were detected by Western blot analysis. (E) MKT-077 and 17-AAG synergistically enhanced mRNA levels of the p53 target genes p21 and PUMA, and reduced MDM2 mRNA levels. The mRNA levels of these genes were quantified using real-time RT-PCR and normalized to levels of GAPDH mRNA. * denotes P < 0.05 comparing 17-AAG to MKT-077+17-AAG.
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