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Key Documents

AB1966

Sigma-Aldrich

Anti-N-WASP Antibody, phospho-specific [Tyr256]

Chemicon®, from rabbit

Sinonimo/i:

Neural Wiskott-Aldrich Syndrome Protein

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About This Item

Codice UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Origine biologica

rabbit

Livello qualitativo

Forma dell’anticorpo

affinity isolated antibody

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Purificato mediante

affinity chromatography

Reattività contro le specie

human

Produttore/marchio commerciale

Chemicon®

tecniche

ELISA: suitable
western blot: suitable

Isotipo

IgG

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

wet ice

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... WASL(8976)

Descrizione generale

Members of the Wiskott-Aldrich sydrome protein (WASP) family regulate the formation of actin-based cell structures in many cell types. These proteins contain C-terminal actin-binding domains that can stimulate actin polymerization. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with higher homology in the functional regions of these proteins. Phosphorylation at serine and tyrosine residues regulates the activity of both proteins. WASP is tyrosine phosphorylated at tyrosine 291 after antigen receptor activation in B-cells and collagen stimulation of platelets. Phosphorylation of the analogous site in N-WASP (Tyr256) stimulates its activity, reduces nuclear N-WASP, and is required for neurite extension.

Specificità

The antibody detects a 65 kDa protein corresponding to the molecular weight of phosphorylated N-WASP on SDS-PAGE Western blots of A431 cells treated with pervanadate. A similar band is observed in pervanadate treated HeLa and endothelial cells. Weak bands are also observed at higher molecular weights after pervanadate treatment. These bands may be due to low cross-reactivity with phosphotyrosine.

Immunogeno

Epitope: phosphotyrosine 256
Phospho-N-WASP (Tyr256) synthetic peptide (coupled to BSA) corresponding to amino acid residues around tyrosine 256 of human N-WASP. The human WASP sequence has a two amino acid difference in the same region surrounding tyrosine 291.

Applicazioni

Anti-N-WASP Antibody, phospho-specific [Tyr256] detects level of N-WASP & has been published & validated for use in ELISA & WB.
Research Category
Signaling
Research Sub Category
Cytoskeletal Signaling
Western blot: 1:10,000 ELISA: 1:20,000

Stato fisico

This antibody was cross-adsorbed to phosphotyrosine then affinity purified using phospho-N-WASP (Tyr256) peptide (without carrier). Antibody is supplied in 100 μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.

Stoccaggio e stabilità

Maintain at 20°C for up to one year from date of receipt. Do not aliquot.

Note legali

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Codice della classe di stoccaggio

10 - Combustible liquids


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PLoS biology, 11(11), e1001704-e1001704 (2013-11-14)
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FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 35(9), e21811-e21811 (2021-08-10)
Actin cytoskeletal reorganization plays an important role in regulating smooth muscle contraction, which is essential for the modulation of various physiological functions including airway tone. The adapter protein Abi1 (Abelson interactor 1) participates in the control of smooth muscle contraction.
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American journal of respiratory cell and molecular biology, 62(5), 645-656 (2020-01-09)
It has been reported that actin polymerization is regulated by protein tyrosine phosphorylation in smooth muscle on contractile stimulation. The role of protein serine/threonine phosphorylation in modulating actin dynamics is underinvestigated. SLK (Ste20-like kinase) is a serine/threonine protein kinase that

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