Analytical Data
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Gene name
vWA1
- Application
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Alternative Names
vWA1；von Willebrand factor A domain-containing Protein 1
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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
Q6PCB0
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Expression Region
23-445aa
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AA Sequence
ERGPPASA PRGDLMFLLD SSASVSHYEF SRVREFVGQL VAPLPLGTGA LRASLVHVGS RPYTEFPFGQ HSSGEAAQDA VRASAQRMGD THTGLALVYA KEQLFAEASG ARPGVPKVLV WVTDGGSSDP VGPPMQELKD LGVTVFIVST GRGNFLELSA AASAPAEKHL HFVDVDDLHI IVQELRGSIL DAMRPQQLHA TEITSSGFRL AWPPLLTADS GYYVLELVPS AQPGAARRQQ LPGNATDWIW AGLDPDTDYD VALVPESNVR LLRPQILRVR TRPGEAGPGA SGPESGAGPA PTQLAALPAP EEAGPERIVI SHARPRSLRV SWAPALGSAA ALGYHVQFGP LRGGEAQRVE VPAGRNCTTL QGLAPGTAYL VTVTAAFRSG RESALSAKAC TPDGPRPRPR PVPRAPTPGT ASREP
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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
Related Products
Protein Description
The vWA1 protein, a member of the von Willebrand factor A (vWA) domain-containing proteins, has gained significant attention in recent years due to its potential roles in various biological processes, particularly in cell adhesion and signaling. Its structure, characterized by the presence of vWA domains, suggests a capacity for mediating interactions with other proteins, which is critical in physiological and pathological conditions. Research has indicated that vWA1 may be implicated in the regulation of cell proliferation, migration, and differentiation, making it a candidate for studies in cancer biology and tissue development. Moreover, preliminary findings suggest that vWA1 could play a role in immune responses, potentially influencing inflammatory processes. As a recombinant protein, vWA1 can be produced and purified for functional assays, enabling the exploration of its biochemical properties and interactions. Investigating the mechanisms by which vWA1 operates in cellular contexts not only provides insights into fundamental biological mechanisms but also highlights potential therapeutic applications for diseases where these processes are disrupted. Given its multifaceted roles, the continued study of vWA1 may uncover novel targets for intervention in various diseases, reinforcing the importance of understanding protein-protein interactions and the significance of post-translational modifications in modulating protein function. Overall, research on vWA1 underscores the intricate and dynamic nature of protein functions within cellular environments and their implications for health and disease.
