Analytical Data
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Gene name
SVEP1
- Application
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Alternative Names
SVEP1；C9orf13；CCP22；SELOB；Sushi. von Willebrand factor type A. EGF and pentraxin 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
Q4LDE5
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Expression Region
736-827aa
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AA Sequence
GDFICTPDNTGVNCTLTCLEGYDFTEGSTDKYYCAYEDGVWKPTYTTEWPDCAKKRFANHGFKSFEMFYKAARCDDTDLMKKFSEAFETTLG
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Molecular Weight
17.6 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
SVEP1 (Sushi, von Willebrand factor A, EGF, and Pentraxin domain-containing protein 1) is a relatively new protein that has gained attention in recent biomedical research due to its potential roles in various physiological and pathological processes. It is primarily expressed in vascular tissues and is implicated in cell adhesion, immune responses, and the regulation of angiogenesis. Recent studies suggest that SVEP1 could play a significant role in the development of certain cardiovascular diseases and cancers. Additionally, its involvement in the extracellular matrix dynamics and interactions with other cellular components position SVEP1 as a key player in tissue repair and remodeling. The recombinant expression of SVEP1 has enabled researchers to investigate its functional properties further and explore its potential as a biomarker for disease states or as a therapeutic target. Given the complexity of its interactions and functions, ongoing studies are focusing on elucidating the precise mechanisms by which SVEP1 contributes to health and disease, which could provide insights into novel treatment strategies and enhance our understanding of various pathological conditions.
