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HSP90AB1 (Heat Shock Protein 90) Antibody [HSP90AB1/3954]

In Stock
Catalog Number Formulation Size Price
3326-MSM4-P0
Purified Ab with BSA and Azide at 200ug/ml
20ug
$229.00
3326-MSM4-P1
Purified Ab with BSA and Azide at 200ug/ml
100ug
$519.00
3326-MSM4-P1ABX
Purified Ab WITHOUT BSA or Azide at 1.0mg/ml
100ug
$519.00
Flat Rate Domestic: $75 | Orders outside the US - Contact Us for Order Information | Ships next business day

Applications & Dilutions

Applications Tested Dillution Protocol Note
Immunohistochemistry (IHC)
1-2ug/ml
30 min at RT. Staining of formalin-fixed tissues requires heating tissue sections in 10mM Tris with 1mM EDTA, pH 9.0, for 45 min at 95°C followed by cooling at RT for 20 minutes
Western Blot (WB)
2-4ug/ml

Summary

This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes.

Product Properties & Targets

Antibody Type
Host
Mouse
Species Reactivity
Isotype / Light Chain
IgG1 / Kappa
Cellular Localization
Cell membrane, Cell surface, Cytoplasm, Dynein axonemal particle, Melanosome, Nucleus, Secreted
Gene Name
Positive Control
Human spleen, stomach or pancreas tissue. MCF-7 cells.
Immunogen
Recombinant human HSP90AB1 protein fragment (around aa581-704) (exact sequence is proprietary)
Alternate Names
Heat shock protein HSP 90-beta, Heat shock 84 kDa, HSP84; HSPC2; HSPCB; D6S182; HSP90B

Database Links

Entrez Gene ID
SwissProt

Additional Information

Clone
HSP90AB1/3954
Chromosome Location
6p21.1
Mol. Weight of Antigen
~90kDa

Functions

  • 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 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 (PubMed:16478993, PubMed:19696785). 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 (PubMed:27295069, PubMed:26991466). 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. They first 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 (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
  • (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable).

Key References

  • J, Cui S, et al. (2013) High Expression of Heat Shock Protein 90 Is Associated with Tumor Aggressiveness and Poor Prognosis in Patients with Advanced Gastric Cancer. PLoS ONE 8(4): e62876.

PubMed Links

Storage & Stability

Antibody with azide - store at 2 to 8 °C. Antibody is stable for 24 months. ,Non-hazardous. No MSDS required.

Limitations

This antibody is available for research use only and is not approved for use in diagnosis.

Supplied as

200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with0.05% BSA & 0.05% azide. Also available WITHOUT BSA at 1.0mg/ml.

Warranty

There are no warranties, expressed or implied, which extend beyond this description. Company is not liable for any personal injury or economic loss resulting from this product.

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