Analytical Data
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Gene name
VWA5B2
- Application
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Alternative Names
VWA5B2；von Willebrand factor A domain-containing Protein 5B2
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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
Q8N398
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Expression Region
781-862aa
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AA Sequence
PRKPSLGAILDGPSPEPGQQLGQGLDDSGNLLSPAPMDWDMLMEPPFLFTAVPPSGELAPPAVPPQAPRCHVVIRGLCGEQP
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Molecular Weight
24.6 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
Related Products
Protein Description
The VWA5B2 protein, a member of the von Willebrand factor A (VWA) domain-containing proteins, has garnered significant attention in recent years due to its potential role in various biological processes and disease mechanisms. Initially identified as a gene linked to specific developmental and physiological functions, VWA5B2 has been implicated in cellular adhesion, migration, and signaling pathways. Research indicates that alterations in VWA5B2 expression may be associated with certain pathological conditions, including cancer progression and neurological disorders. The protein’s unique structural features, including its VWA domain, suggest a complex interaction network with other cellular components. As a result, recombinant expressions of VWA5B2 have been pursued to facilitate detailed studies on its functional roles and therapeutic potentials. Advances in recombinant DNA technology have enabled the production of this protein in various expression systems, allowing for biochemical characterization, functional assays, and structural analyses. Understanding VWA5B2’s mechanism of action could provide valuable insights into its role in health and disease, paving the way for potential therapeutic strategies targeting its functions. Enhanced knowledge about VWA5B2 may eventually contribute to the development of biomarkers for disease diagnosis and prognosis, as well as novel treatments for related disorders.
