Recombinant Human Wiskott-Aldrich Syndrome Protein (WAS) Protein (His)

Name: Recombinant Human Wiskott-Aldrich Syndrome Protein (WAS) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07576P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Wiskott-Aldrich Syndrome Protein (WAS) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P42768
Target Symbol	WAS
Synonyms	(WASp)
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	SGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD
Expression Range	2-502aa
Protein Length	Full Length of Mature Protein
Mol. Weight	53.6 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Important for efficient actin polymerization. Possible regulator of lymphocyte and platelet function. Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria. In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. Promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular Location	Cytoplasm, cytoskeleton. Nucleus.
Database References	HGNC: 12731 OMIM: 300299 KEGG: hsa:7454 STRING: 9606.ENSP00000365891 UniGene: PMID: 29725003 A novel WASP mutation (I290T) was found in an X-linked neutropenia patient and in his heterozygous mother. This mutation was located in the GTPase-binding domain. PMID: 28956125 In a model of sterile inflammation utilizing TLR4 ligation followed by ATP or nigericin treatment, inflammasome activation is enhanced in monocytes from WAS patients. PMID: 29146903 Despite the lack of typical clinical manifestations of WAS, low expression of WASP could be associated with the pathogenesis of a subtype of inflammatory bowel disease patients. PMID: 29358862 expression of WASP inversely correlates with BCR-ABL1 levels and the progression of the disease in Chronic myeloid leukemia patients. downregulation of WASP contributes to the resistance to apoptosis and to BCR-ABL1-induced tumorigenesis. PMID: 29022901 The coverage and depth of WASP were extremely low. PMID: 28901403 WIP residues 454-456 are the major contributor to WASp affinity, and residues 449-451 were found to have the largest effect upon WASp ubiquitylation and, presumably, degradation. PMID: 29215267 Novel WASP mutations were found in two patients with X-linked thrombocytopenia and their families. PMID: 28641574 High WASP expression is associated with lung cancer invasion. PMID: 28351346 A Treg-specific role for WASP is required for prevention of Th2 effector cell differentiation and allergic sensitization to dietary antigens. PMID: 27643438 WASP and SCAR drive pseudopod formation and are conserved in actin-filled pseudopod-based motility. PMID: 28473602 Authors show that knock-down of WASp or expression of Y102F mutant of WASp decreases colony formation and in vivo tumor growth. Results show that WASp is a novel substrate of ALK and has a critical role in regulating invasiveness and oncogenesis of ALCL. PMID: 27694894 this study describes an Iranian boy with Wiskott-Aldrich syndrome with a novel WASP mutation PMID: 26993433 The inducible recruitment of WASp to the TCR-CD3 complex is partially dependent of tyrosine phosphorylation of Cd3e. PMID: 26342115 retrospectively investigated the outcome of hematopoietic stem cell transplantation in a cohort of 24 patients with the X-linked thrombocytopenia phenotype and mutations in the WAS gene PMID: 25388447 This suggests that N-WASP's failure to compensate for WASP in rescuing chemotaxis could be due to the absence of this I30 region. PMID: 26463123 N-WASP is downregulated in clear cell renal cell carcinoma PMID: 25115631 Studies indicate that mutations in the Wiskott-Aldrich syndrome protein (WASp) gene cause a continuum of clinical symptoms ranging from intermittent X-linked thrombocytopenia to full classical Wiskott-Aldrich syndrome (WAS). PMID: 26159751 Platelet actin nodule formation is dependent on WASp and the ARP2/3 complex. PMID: 26028144 conclude that tyrosine phosphorylation of WIP is a crucial regulator of WASP stability and function as an actin-nucleation-promoting factor PMID: 25413351 WASP, RUNX1, and ANKRD26 genes are important for normal TPO signaling and the network underlying thrombopoiesis. PMID: 26175287 The introduction of functional WASp by GT corrected the alterations of both central and peripheral B cell tolerance checkpoints. WASp plays an important role in the establishment and maintenance of B cell tolerance in humans. PMID: 26368308 We describe two Malay patients with classical Wiskott-Aldrich Syndrome with two different mutations in the WASP gene PMID: 26277674 we identify small ubiquitin-related modifier (SUMO)ylation as a novel posttranslational modification of WASp PMID: 26261240 A total of 60 unique WAS mutations were identified in Chinese patients, including 20 novel mutations and 8 hotspots, from 75 unrelated families with a total of 81 affected members. PMID: 25931402 studies discovered that HMGB1 suppressed phosphorylation, nuclear translocation, and activation of CREB, by inhibiting nuclear translocation of PKA catalytic subunit PMID: 25277185 data suggest that missense mutations WASPRL46P or WASPRA47D affect the activity of WASP in T cell chemotaxis probably by affecting the turnover of the protein. PMID: 25200405 An indispensable relationship between nuclear-WASp- and hSWI/SNF-complexes in gene activation and molecular distinctions in TH cells that might contribute to disease severity in the X-linked thrombocytopenia/Wiskott-Aldrich syndrome clinical spectrum. PMID: 25253772 Data indicate the WASp-interacting protein (WIP)-Wiskott-Aldrich syndrome protein (WASp) interaction in the regulation of actin-dependent processes. PMID: 24962707 WASp and WAVE2 differ in their dynamics and their associated proteins PMID: 25342748 WAS gene mutation is associated with X-linked thrombocytopenia in three males with normal sized platelets. PMID: 25154619 WASP deficiency perturbs the homeostasis of B-cell compartment in humans. PMID: 24369837 Data indicate that mycolactone analogues bind Wiskott-Aldrich syndrome proteins (WASP} with IC50 in the 50-10 muM range. PMID: 25158122 These findings support a contributory role for defective Breg cells in the development of WAS-related autoimmunity PMID: 24945741 study unveils an ARP2/3:VCA-independent function of nuclear-WASp in TH1 gene activation that is uncoupled from its cytoplasmic role in actin polymerization. PMID: 24872192 Pro373Ser mutation reduces Tyr291 phosphorylation and prevents conformational changes required for WASP activity in chemotaxis and T-cell activation. PMID: 24440360 Missense mutation in the WAS gene is associated with intermittent X-linked thrombocytopenia. PMID: 24115682 We conclude that WASp function restricts TGF-b1 secretion in a Cdc42- and Src family kinase-dependent manner and independently of actin assembly PMID: 24133214 We present two cases of WAS in neonates with WAS gene mutations PMID: 23301916 Dedicator of cytokinesis 8 interacts with talin and Wiskott-Aldrich syndrome protein to regulate NK cell cytotoxicity. PMID: 23455509 Data indicate that slit2N alters the localization and binding of Robo1 to WASp and LSP1 in HIV-1-gp120-treated immature dendritic cells (iDCs). PMID: 23119100 Report five previously reported mutations and six novel mutations in WASP gene in Iranian Wiskott-Aldrich patients. PMID: 23264413 this is the first report describing TTP in WAS patients with novel mutation in the WASP gene. PMID: 23237501 Despite mediating enhanced actin polymerization, EVH1 missense-mutated human proteins did not function fully in mouse cells, even when overexpressed. Mutant protein retention in podosomes was impaired & associated with low WASp Tyr phosphorylation. PMID: 23160469 study describes that both N-WASp and WASp participate in the inhibition of NK-cell chemotaxis in response to NKG2D WASp engagement, and that this effect is not dependent on the regulation of F-actin dynamics PMID: 22585739 WASP-deficient T cells migrated in a normal proportion towards CXCL12, CCL19 and CCL21, but displayed an increased adhesion and elongation on ICAM-1 PMID: 22804504 data suggest that regulated degradation of activated WASp might be an efficient strategy by which the duration and localization of actin rearrangement and the intensity of T-cell activation are controlled. PMID: 22665495 The wild-type WASp, but not the mutant restored adhesion capacity, spreading morphology, and cytoskeletal reorganization. PMID: 22311461 Mutation in WASP gene is associated with Wiskott-Aldrich syndrome and X-linked thrombocytopenia. PMID: 22038941 the c.273+11dup change within the WAS gene was observed in patients showing symptoms consistent with the Wiskott-Aldrich syndrome; concluded that the presence of the additional C in the WAS gene is a functionally neutral polymorphism PMID: 21711396

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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Recombinant Human Wiskott-Aldrich Syndrome Protein (WAS) Protein (His)

Recombinant Human Wiskott-Aldrich Syndrome Protein (WAS) Protein (His)

Product Overview

Target Details

FAQs