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Validated All-in-One™ qPCR Primer for WAS(NM_000377.2) Search again
Product ID:
HQP018507
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
IMD2, SCNX, THC, THC1, WASP, WASPA
Gene Description:
WASP actin nucleation promoting factor
Target Gene Accession:
NM_000377.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- WASp mediates actin polymerization and leads to ultimately to occupancy-induced TCR endocytosis
- mutational analysis in patients with Wiskott-Aldrich syndrome in Argentina
- Missense mutations of the WASP gene cause intermittent X-linked thrombocytopenia
- Normal chemotactic responses were restored in WASp macrophages transfected with a full-length human WAS construct. Expression of exogenous WAS protein (WASp) in these cells also restored normal polarised cell morphology and the ability to form podosomes.
- An Alu-mediated deletion at Xp11.23 leading to Wiskott-Aldrich syndrome.
- Five novel WASP mutations have been identified that are all predicted to lead to premature translational termination of the WAS protein.
- Activation of Wiskott-Aldrich syndrome protein and its association with other proteins by stromal cell-derived factor-1alpha is associated with cell migration in Jurkat cells, a T-lymphocyte line.
- Required for NK cell cytotoxicity and colocalizes with actin to NK cell-activating immunologic synapses
- Wiskott-Aldrich Syndrome protein regulates lipid raft dynamics during immunological synapse formation
- Platelets activate Arp2/3 complex, assemble actin, and change shape in the absence of WASp, indicating a more specialized role for WASp in these cells.
- Data show that the Src family kinase Hck induces phosphorylation of Wiskott Aldrich syndrome protein (WASp)-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE.
- mutated in Wiskott Aldrich syndrome
- Results suggest that recruitment of factors by Wiskott-Aldrich Syndrome protein (WASP) and Scar1 stimulates cellular actin-based motility and actin nucleation with the Arp2/3 complex.
- results suggest that the ZAP-70-CrkL-WIP pathway and PKCtheta link TCR to WASP activation
- PSTPIP1 acts downstream of CD2/CD2AP to link CD2 engagement to the WASp-evoked actin polymerization required for synapse formation and T cell activation.
- X-linked thrombocytopenia caused by a mutation in the WAS gene that disrupts interaction with the (WASP)-interacting protein (WIP).
- Results describe somatic mosaicism in two brothers affected with Wiskott-Aldrich syndrome (WAS) due to a second-site mutation in the WAS protein (WASP) gene.
- Phosphorylation plays a critical role in WASP function as a regulator of arp-2- and arp-3-mediated actin polymerization.
- WAS protein expression is a useful tool for predicting long-term prognosis for patients with Wiskott-Aldrich syndrome.
- Differentiation and survival of B lymphocytes is minimally dependent on WAS protein.
- the interaction of the betaPIX.WASP.SPIN90 complex with Nck is crucial for stable cell adhesion and can be dynamically modulated by SPIN90 phosphorylation that is dependent on cell adhesion and ERK activation
- WASp undergoes tyrosine phosphorylation upon CD16 or beta2-integrin engagement on NK cells.
- WASp is either not involved in or is redundant in the rapid dynamics of lymphocyte microvilli.
- interactions of WASP and WIP are affected by two novel mutations that change the conformation of WASP and disrupt hydrogen bonding
- Mutations identified included p.R13X, p.R41X, p.S82P, IVS1-1 G --> C, p.L342TFsX493, and a large deletion.
- The Wiskott-Aldrich WASP protein is an important component for integration of signals leading to nuclear translocation of transcription factors NFAT2 and NF-kappa B RelA during cell-cell contact and natural cytotoxicity receptor NKp46-dependent signaling
- Results describe a quantitative model of allosteric regulation of the Wiskott-Aldrich syndrome protein (WASP) by the Rho GTPase Cdc42.
- The selective advantage of WASP+ natural killer cells was also demonstrated for carrier females
- Knowledge of the molecular effect of WAS protein mutations provides a logical basis for correlating genotype and clinical phenotype of Wiskott-Aldrich syndrome
- The process is a prerequisite for WASp activation and a critical step in temporal regulation and integration of WASp-mediated cellular responses.
- TRAP and WASp, but not other unrelated aldolase binders, compete for the binding to the enzyme in vitro.
- NMR investigation and cross-linking studies of the interaction of the Arp2/3 complex with VCA peptides of Wiskott-Aldrich syndrome protein
- WASP and N-WASP are activated and phosphorylated by protein-tyrosine kinase and GTPase signals
- A partial down-regulation of WASP is sufficient to inhibit podosome formation in dendritic cells.
- A novel Wiskott-Aldrich syndrome protein (WASP) complex mutation identified in a WAS patient results in an aberrant product at the C-terminus from two transcripts with unusual polyA signals.
- Human WASP suppresses the growth defect of Saccharomyces cerevisiae las17Delta strain, only in the presence of WASP-interacting protein (WIP).
- The results strongly suggest that the smaller WASP is translated from the second ATG downstream of the original mutation, and not only T cells but also NK cells carrying the second mutation acquired a growth advantage over WASP negative counterparts.
- In addition to chemotaxis, the WASP-verprolin complex is involved in both podosome formation and phagocytosis.
- activating mutations in the Wiskott-Aldrich syndrome protein result in congenital neutropenia
- impaired beta2 integrin function in WASp-deficient neutrophil may contribute substantially to the clinical immunodeficiency suffered by WAS patients
- investigated family members of the patients originally described by Wiskott in 1937 and identified a new frame shift mutation in exon 1 of WAS
- the WASp/SNX9/p85/CD28 complex enables a unique interface of endocytic, actin polymerizing, and signal transduction pathways required for CD28-mediated T cell costimulation
- Thus, WASP appears to play an important role in the activation and suppressor function of nTreg cells, and a dysfunction or incorrect localization of nTreg cells may contribute to the development of autoimmunity in WAS patients.
- Two novel mutations of the WASP gene in two Spanish families with patients clinically diagnosed as havingX-linked thrombocytopenia and Wiskott-Aldrich syndrome, were identified.
- study found 28 novel WAS mutations in Wiskott-Aldrich syndrome and X-linked thrombocytopenia (7 missense, 1 nonsense, 1 nonstop change, 5 splice site mutations and 14 deletions or insertions)
- Chinese Wiskott-Aldrich Syndrome (WAS) patients had mutations involving exon 1 of the Wiskott-Aldrich syndrome protein (WASP) gene and none had the X-linked thrombocytopenia phenotype.
- the WIP-WASP complex plays an important role in WASP stabilization and NFAT activation
- Study provides a strategy that allows a strong suppression of WASp in CD34(+) cells and will facilitate future studies on the role of WASp in human cells.
- These findings reveal a novel mechanism for inhibition of myelopoiesis through defective mitosis and cytokinesis due to hyperactivation and mislocalization of actin polymerization.
- that WASP and WASP-interacting protein (WIP) form a complex at the phagocytic cup and that the WASP.WIP complex plays a critical role in the phagocytic cup formation.
- The discovery of unique functional domains of Wiskott-Aldrich syndrome protein has been instrumental in defining mechanisms that control activation of Wiskott-Aldrich syndrome protein. Review.
- Genotypic analysis of allospecific T-cell clones revealed a remarkable diversity of deletions and base substitutions resulting in at least 34 different revertant genotypes that restored expression of WASp
- One gene with unknown function to be differentially expressed in UC but not Crohn's disease by RT-PCR. Due to its predicted protein architecture, we call this gene Wiskott-Aldrich syndrome protein.
- the presence of truncated WASP confers an extreme disadvantage in early developing thymocytes, beyond that of absence of full-length WASP, and the disadvantage likely occurs through dominant negative competition of WASP Delta VCA with N-WASP
- Robo4 binding to a Wiskott-Aldrich syndrome protein (WASP)
- Dimerization act in hierarchical fashion, enabling WASP/WAVE proteins to integrate different classes of inputs to produce a wide range of cellular actin responses in Wiskoo Aldrich syndrome.