Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™ | Boster PB9635 product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Boster

product type :

antibody

product name :

Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™

catalog :

PB9635

quantity :

100μg/vial

clonality :

polyclonal

host :

domestic rabbit

conjugate :

nonconjugated

reactivity :

human, mouse, rat

application :

western blot, immunocytochemistry, flow cytometry, immunohistochemistry - paraffin section

product information

SKU :

PB9635

Product Name :

Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™

Size :

100μg/vial

Clonality :

Polyclonal

Host :

Rabbit

Reactivity :

Human, Monkey, Mouse, Rat

Predicted Reactivity :

Hamster

Application(s) :

Flow Cytometry, IF, IHC-P, ICC, WB

Application Details :

Western blot, 0.1-0.5µg/ml, Human, Monkey, Mouse, Rat. Immunohistochemistry (Paraffin-embedded Section), 0.5-1µg/ml, Human, Mouse, Rat, By Heat. Immunocytochemistry/Immunofluorescence, 2µg/ml, Human. Flow Cytometry, 1-3μg/1x10^6 cells, Human

Application Notes :

Tested Species: In-house tested species with positive results. By Heat: Boiling the paraffin sections in 10mM citrate buffer, pH6.0, for 20mins is required for the staining of formalin/paraffin sections. Other applications have not been tested. Optimal dilutions should be determined by end users.

Description :

Boster Bio Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™ catalog # PB9635. Tested in Flow Cytometry, IF, IHC-P, ICC, WB applications. This antibody reacts with Human, Monkey, Mouse, Rat.

Concentration :

Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.

Gene Name :

HSP90AA1

Uniprot ID :

P07900

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.

Form :

Lyophilized

Contents :

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.

Purification :

Immunogen affinity purified.

Cross-reactivity :

No cross reactivity with other proteins

Storage :

Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles.

Reconstitution :

Add 0.2ml of distilled water will yield a concentration of 500ug/ml.

Gene Full Name :

Heat shock protein HSP 90-alpha

Synonyms :

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;

Protein Name :

Heat shock protein HSP 90-alpha

Molecular Weight :

84660 MW

Protein 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.

Subcellular Localization :

Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.

Recommended Detection Systems :

Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and ICC.

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.

Research Category :

Cancer, Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction, Tumor Biomarkers