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Mouse Monoclonal HS90A antibody. Carrier free. Suitable for Flow Cyt, WB and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human HSP90AA1.


Images

Flow Cytometry - Anti-Hsp90 antibody [H90-10] (AB58950), expandable thumbnail
  • Western blot - Anti-Hsp90 antibody [H90-10] (AB58950), expandable thumbnail
  • Western blot - Anti-Hsp90 antibody [H90-10] (AB58950), expandable thumbnail
  • Western blot - Anti-Hsp90 antibody [H90-10] (AB58950), expandable thumbnail

Publications

Key facts

Isotype
IgG2a
Host species
Mouse
Storage buffer

pH: 7.4
Constituents: 99% PBS

Form
Liquid
Clonality
Monoclonal

Immunogen

  • Native Full Length Protein corresponding to Human HSP90AA1. Database link P07900

Reactivity data

Select an application
Product promiseTestedExpectedPredictedNot recommended
Flow CytWB
Human
Tested
Tested

Tested
Tested

Species
Human
Dilution info
0.01000-0.10000 µg for 106 Cells
Notes

ab170191 - Mouse monoclonal IgG2a, is suitable for use as an isotype control with this antibody.

Tested
Tested

Species
Human
Dilution info
1.00000-5.00000 µg/mL
Notes

-

Associated Products

Select an associated product type

6 products for Alternative Product

Target data

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.

Alternative names

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

Recommended products

Mouse Monoclonal HS90A antibody. Carrier free. Suitable for Flow Cyt, WB and reacts with Human samples. Cited in 3 publications. Immunogen corresponding to Native Full Length Protein corresponding to Human HSP90AA1.

Key facts

Isotype
IgG2a
Form
Liquid
Clonality
Monoclonal
Immunogen
  • Native Full Length Protein corresponding to Human HSP90AA1. Database link P07900
Carrier free
Yes
Clone number
H90-10
Purification technique
Affinity purification Protein G
Specificity

ab58950 recognizes both Hsp90 alpha and Hsp90 beta

Concentration
Loading...
Purification notes

Purified from TCS

Storage

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Notes

Dilute in PBS or medium which is identical to that used in the assay system.

This product was changed from ascites to tissue culture supernatant on 19/12/2018. Please note that the dilutions may need to be adjusted accordingly. If you have any questions please do not hesitate to contact our scientific support team.

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Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.
Activity summary

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.

Biological function summary

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.

Pathways

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.

Associated diseases and disorders

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.

Product promise

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4 product images

  • Flow Cytometry - Anti-Hsp90 antibody [H90-10] (ab58950), expandable thumbnail

    Flow Cytometry - Anti-Hsp90 antibody [H90-10] (ab58950)

    Overlay histogram showing HeLa cells stained with ab58950 (red line). The cells were fixed with 4% paraformaldehyde (10 min) and then permeabilized with 0.1% PBS-Tween for 20 min. The cells were then incubated in 1x PBS / 10% normal goat serum / 0.3M glycine to block non-specific protein-protein interactions followed by the antibody (ab58950, 0.01μg/1x106 cells) for 30 min at 22°C. The secondary antibody used was Alexa Fluor® 488 goat anti-mouse IgG (H&L) (Goat Anti-Mouse IgG H&L (Alexa Fluor® 488) ab150113) at 1/2000 dilution for 30 min at 22°C. Isotype control antibody (black line) was mouse IgG2a [ICIGG2A] (Mouse IgG2a, Kappa Monoclonal [B12/8] - Isotype Control ab91361, 0.1μg/1x106 cells) used under the same conditions. Unlabelled sample (blue line) was also used as a control. Acquisition of >5,000 events were collected using a 20mW Argon ion laser (488nm) and 525/30 bandpass filter.

    This image was generated using the ascites version of the product.

  • Western blot - Anti-Hsp90 antibody [H90-10] (ab58950), expandable thumbnail

    Western blot - Anti-Hsp90 antibody [H90-10] (ab58950)

    Lanes 1 - 4: Merged signal (red and green). Green - ab58950 observed at 85 kDa. Red - loading control Anti-GAPDH antibody [EPR16891] - Loading Control ab181602 (Rabbit Anti-GAPDH antibody [EPR16891]) observed at 37kDa.

    ab58950 was shown to react with Hsp90 in wild-type HEK-293T cells in western blot with loss of signal observed in HSP90AB1 knockout cell line Human HSP90AB1 (Hsp90 beta) knockout HEK-293T cell line ab266117 (HSP90AB1 knockout cell lysate Human HSP90AB1 (Hsp90 beta) knockout HEK-293T cell lysate ab257190). Wild-type and HSP90AB1 knockout HEK-293T cell lysates were subjected to SDS-PAGE. Membranes were blocked in 3% milk in TBS-T (0.1% Tween®) before incubation with ab58950 and Anti-GAPDH antibody [EPR16891] - Loading Control ab181602 (Rabbit Anti-GAPDH antibody [EPR16891]) overnight at 4°C at 0.5 μg/ml and a 1 in 20000 dilution respectively. Blots were incubated with Goat anti-Mouse IgG H&L (IRDye® 800CW) preabsorbed (Goat anti-Mouse IgG H&L (IRDye® 800CW) preadsorbed ab216772) and Goat anti-Rabbit IgG H&L (IRDye® 680RD) preabsorbed (Goat Anti-Rabbit IgG H&L (IRDye® 680RD) preadsorbed ab216777) secondary antibodies at 1 in 20000 dilution for 1 hour at room temperature before imaging.

    All lanes: Western blot - Anti-Hsp90 antibody [H90-10] (ab58950) at 0.5 µg/mL

    Lane 1: Wild-type HEK-293T cell lysate at 20 µg

    Lane 2: HSP90AB1 knockout HEK-293T cell lysate at 20 µg

    Lane 2: Western blot - Human HSP90AB1 (Hsp90 beta) knockout HEK-293T cell line (Human HSP90AB1 (Hsp90 beta) knockout HEK-293T cell line ab266117)

    Lane 3: Saos-2 cell lysate at 20 µg

    Lane 4: HL-60 cell lysate at 20 µg

    Performed under reducing conditions.

    Predicted band size: 83 kDa, 85 kDa

    Observed band size: 85 kDa

  • Western blot - Anti-Hsp90 antibody [H90-10] (ab58950), expandable thumbnail
    Image from Niture SK et al, J Biol Chem. 2010 Nov 19;285(47):36865-75. Epub 2010 Sep 23, Fig 6. DOI 10.1074/jbc.M110.175802.

    Western blot - Anti-Hsp90 antibody [H90-10] (ab58950)

    Western Blot analysis of the effect of siRNA inhibition of Hsp90 on INrf2. Murine hepatoma (Hepa-1) cells were transfected with control siRNA or Hsp90-specific siRNA and Hsp90 (ab58950), INrf2, and actin levels were analyzed by immunoblotting.

    This image was generated using the ascites version of the product.

    All lanes: Western blot - Anti-Hsp90 antibody [H90-10] (ab58950)

    Predicted band size: 85 kDa

  • Western blot - Anti-Hsp90 antibody [H90-10] (ab58950), expandable thumbnail

    Image collected and cropped by CiteAb under a CC-BY license from the publication

    Western blot - Anti-Hsp90 antibody [H90-10] (ab58950)

    Hsp90 western blot using anti-Hsp90 antibody [H90-10] ab58950. Publication image and figure legend from Hellbach, N., Peterson, S., et al., 2018, PLoS One, PubMed 30304024.


    ab58950 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 ab58950 please see the product overview.

    Impaired SMN2 splicing and reduced SMN protein in myoblasts from SMA patients.Molecular analysis of the two hESC unaffected and the two hESC SMA Type 1 lines revealed no SMN1 expression in the genomic PCR analysis, but 2 SMN2 copy numbers (A). SMN2FL (FL) and SMNΔ7 (Δ7) transcripts were significantly reduced (B). SMN protein levels in SMA Type 1 remained low compared to unaffected myoblasts (C), and were stable over 3 days after change to differentiation medium (D). Data represented as mean ± SEM of n = 6–12 individual samples and normalized to unaffected and endogenous controls (B: GAPDH, C: HSP90, D: Actin). *: p < 0.05; **: p < 0.01; ***: p < 0.001, two-tailed unpaired Student's t-test.

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