Analytical Data
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Gene name
WAS
- Application
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Alternative Names
WAS；IMD2；Actin nucleation-promoting factor WAS
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P42768
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Expression Region
2-502aa
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AA Sequence
SGGPMGGRPGGRGAPAVQQNIPSTLLQDHENQRLFEMLGRKCLTLATAVVQLYLALPPGAEHWTKEHCGAVCFVKDNPQKSYFIRLYGLQAGRLLWEQELYSQLVYSTPTPFFHTFAGDDCQAGLNFADEDEAQAFRALVQEKIQKRNQRQSGDRRQLPPPPTPANEERRGGLPPLPLHPGGDQGGPPVGPLSLGLATVDIQNPDITSSRYRGLPAPGPSPADKKRSGKKKISKADIGAPSGFKHVSHVGWDPQNGFDVNNLDPDLRSLFSRAGISEAQLTDAETSKLIYDFIEDQGGLEAVRQEMRRQEPLPPPPPPSRGGNQLPRPPIVGGNKGRSGPLPPVPLGIAPPPPTPRGPPPPGRGGPPPPPPPATGRSGPLPPPPPGAGGPPMPPPPPPPPPPPSSGNGPAPPPLPPALVPAGGLAPGGGRGALLDQIRQGIQLNKTPGAPESSALQPPPQSSEGLVGALMHVMQKRSRAIHSSDEGEDQAGDEDEDDEWDD
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Molecular Weight
53.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
WASP (Wiskott-Aldrich Syndrome Protein) is a crucial actin-regulating protein that plays a significant role in the immune system and cell motility. Mutations in the WAS gene can lead to Wiskott-Aldrich Syndrome, which is characterized by immunodeficiency, eczema, and thrombocytopenia. Given its essential function in cytoskeletal dynamics, research into WAS protein has garnered attention for its potential implications in immunology, cell biology, and therapeutic applications. Recent studies have focused on the recombinant expression of WASP to explore its structural properties and functional mechanisms. The generation of WASP recombinant proteins allows researchers to investigate the protein's interactions with other cellular components, such as actin and various signaling molecules, providing insights into its role in regulating the cytoskeleton during immune responses. Additionally, understanding the nuances of WASP function can lead to the development of novel therapeutic strategies for conditions related to WAS deficiency and other cytoskeletal disorders. The application of advanced techniques in protein engineering and characterization has further opened avenues for designing WASP-based interventions that could restore normal immune function in affected individuals. This background sets the stage for an in-depth exploration of recombinant WASP, its biological significance, and its potential as a target for innovative treatments in related diseases.
