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Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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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. In addition, these proteins bind the ARP2/3 complex, which can nucleate actin polymerization at sites that lead to branched actin structures. WASP is expressed primarily in hematopoietic cells, while its homolog N-WASP is widely expressed. These proteins have 48% identity in human with the highest homology in the functional regions of these proteins. Phosphorylation regulates the activity of both proteins. Dual phosphorylation of WASP on serine 483 and 484 by casein kinases increase the affinity for the ARP2/3 complex. Thus, dual serine phosphorylation may be important for formation of actin-based structures in various cell types.
References
Product Information
Format
Affinity Purified
Presentation
This antibody was cross-adsorbed to unphosphorylated-N-WASP (S484/S485) peptide (without carrier) then affinity purified using phospho-N-WASP (S484/S485) peptide (without carrier). Antibody is supplied in 100 μl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide.
Detect N-WASP using this Anti-N-WASP Antibody, phospho-specific [Ser484/Ser485] validated for use in ELISA & WB.
Key Applications
ELISA
Western Blotting
Application Notes
Western blot: 1:1000 ELISA: 1:2000
Biological Information
Immunogen
Phospho-N-WASP (S484/S485) synthetic peptide (coupled to KLH) corresponding to amino acid residues around serine 484 and 485 of human N-WASP. The human WASP sequence has a similar peptide sequence surrounding serine 483 and 484.
Epitope
phosphoserine484/phosphserine485
Host
Rabbit
Specificity
The antibody detects a 63 kDa protein corresponding to the molecular weight of phosphorylated WASP on SDS-PAGE immunoblots of Jurkat cell lysate. In rat brain, A431, human endothelial and SKN-SH cells, this antibody detects a 65 kDa protein corresponding to phosphorylated N-WASP.
The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. The presence of a number of different motifs suggests that they are regulated by a number of different stimuli, and interact with multiple proteins. Recent studies have demonstrated that these proteins, directly or indirectly, associate with the small GTPase, Cdc42, known to regulate formation of actin filaments, and the cytoskeletal organizing complex, Arp2/3. The WASL gene product is a homolog of WAS protein, however, unlike the latter, it is ubiquitously expressed and shows highest expression in neural tissues. It has been shown to bind Cdc42 directly, and induce formation of long actin microspikes.
FUNCTION: SwissProt: O00401 # Regulates actin polymerization by stimulating the actin- nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. SIZE: 505 amino acids; 54827 Da SUBUNIT: Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with the WW domains of PRPF40A/FBP11 (By similarity). Interacts with NOSTRIN. Interacts with Shigella flexneri protein icsA. The interaction with icsA enhances the affinity of WASL for Arp2/3, thus assembling a tight complex which has maximal activity in actin assembly. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). Nucleus (By similarity). Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). SIMILARITY: SwissProt: O00401 ## Contains 1 CRIB domain. & Contains 1 WH1 domain. & Contains 2 WH2 domains.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
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.
Storage and Shipping Information
Storage Conditions
Maintain at 20°C for up to one year from date of receipt. Do not aliquot.
The ability of cancer cells to move and invade the surrounding environment is the basis of local and distant metastasis. Cancer cell movement requires dynamic remodeling of the cytoskeleton and cell membrane and is controlled by multiprotein complexes including focal adhesion kinase (FAK) or the Neural Wiskott-Aldrich Syndrome Protein (N-WASP). We show that 17β-estradiol induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extranuclear signaling of estrogen receptor α interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase, and FAK. Within this complex FAK autophosphorylation ensues, and activated FAK recruits the small GTPase cdc42, which, in turn, triggers N-WASP phosphorylation. This results in the translocation of Arp2/3 complexes at sites where membrane structures related to cell movement are formed. Recruitment of FAK and N-WASP is necessary for cell migration and invasion induced by 17β-estradiol in breast cancer cells. Our findings identify an original mechanism through which estrogen promotes breast cancer cell motility and invasion. This information helps to understand the effects of estrogen on breast cancer metastasis and may provide new targets for therapeutic interventions.
