Analytical Data
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Gene name
WIPF1
- Application
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Alternative Names
PRPL-2; WASPIP; WIP; Wiskott-Aldrich Syndrome Protein Interacting Protein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43516
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Expression Region
Thr24~Asn200
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Molecular Weight
25 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
WIPF1, also known as WASP-interacting protein, plays a crucial role in various cellular processes, including cytoskeletal organization, cell migration, and immune responses. Its involvement in actin filament dynamics positions WIPF1 as a significant player in the regulation of cell shape and movement. Research into WIPF1 has gained momentum due to its potential implications in various diseases, including cancer and autoimmune disorders. Dysregulation of WIPF1 expression or function may contribute to aberrant cell behavior, making it a focus of study for therapeutic intervention. Recent advancements in recombinant protein technology facilitate the study of WIPF1's molecular interactions and functional mechanisms, enabling researchers to produce purified WIPF1 for in vitro assays and structural analyses. Understanding the precise role of WIPF1 in cellular signaling pathways could provide insights into novel drug targets and therapeutic strategies. Furthermore, elucidating its functional dynamics could enhance our comprehension of cell motility and tissue homeostasis, thereby supporting broader applications in regenerative medicine and cancer therapy. Ongoing investigations into WIPF1 are essential for uncovering its biological significance and paving the way for innovative treatments harnessing its properties.
