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Anti-Hsp90 Alpha Picoband Antibody

     
  • WB - Anti-Hsp90 Alpha Picoband Antibody ABO12321
    Anti- Hsp90 alpha Picoband antibody, ABO12321, Western blottingAll lanes: Anti Hsp90 alpha (ABO12321) at 0.5ug/mlLane 1: Rat Brain Tissue Lysate at 50ugLane 2: Rat Cardiac Muscle Tissue Lysate at 50ugLane 3: Rat Liver Tissue Lysate at 50ugLane 4: HELA Whole Cell Lysate at 40ugLane 5: JURKAT Whole Cell Lysate at 40ugLane 6: 22RV1 Whole Cell Lysate at 40ugPredicted bind size: 90KDObserved bind size: 90KD
  • IHC - Anti-Hsp90 Alpha Picoband Antibody ABO12321
    Anti- Hsp90 alpha Picoband antibody, ABO12321, IHC(P)IHC(P): Mouse Testis Tissue
  • IHC - Anti-Hsp90 Alpha Picoband Antibody ABO12321
    Anti- Hsp90 alpha Picoband antibody, ABO12321, IHC(P)IHC(P): Rat Testis Tissue
  • IHC - Anti-Hsp90 Alpha Picoband Antibody ABO12321
    Anti- Hsp90 alpha Picoband antibody, ABO12321, IHC(P)IHC(P): Human Testis Tissue
  • SPECIFICATION
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB, IHC-P
Primary Accession P07900
Host Rabbit
Reactivity Human, Mouse, Rat
Clonality Polyclonal
Format Lyophilized
Description Rabbit IgG polyclonal antibody for Heat shock protein HSP 90-alpha(HSP90AA1) detection. Tested with WB, IHC-P in Human;Mouse;Rat.
Reconstitution Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
Additional Information
Gene ID 3320
Other Names Heat shock protein HSP 90-alpha, Heat shock 86 kDa, HSP 86, HSP86, Lipopolysaccharide-associated protein 2, LAP-2, LPS-associated protein 2, Renal carcinoma antigen NY-REN-38, HSP90AA1, HSP90A, HSPC1, HSPCA
Calculated MW 84660 MW KDa
Application Details Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Mouse, Rat, By Heat

Western blot, 0.1-0.5 µg/ml, Human, Mouse, Rat
Subcellular Localization Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Name Heat shock protein HSP 90-alpha
Contents Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
Immunogen A synthetic peptide corresponding to a sequence at the C-terminus of human Hsp90 alpha (454-488aa QNRKKLSELLRYYTSASGDEMVSLKDYCTRMKEN Q), identical to the related mouse and rat sequences.
Purification Immunogen affinity purified.
Cross Reactivity No cross reactivity with other proteins
Storage At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing.
Protein Information
Name HSP90AA1
Synonyms HSP90A, HSPC1, HSPCA
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: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: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 (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).
Cellular Location Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV
Research Areas
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Background

Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene. The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expressed paralog Hsp90B which shares over 85% amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation.

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$ 280.00
Cat# ABO12321
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