Analytical Data
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Gene name
vwc2l
- Application
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Alternative Names
vwc2l；von Willebrand factor C domain-containing Protein 2-like
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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
B2RUY7
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Expression Region
22-222aa
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AA Sequence
AAISHEDYP ADEGDQISSN DNLIFDDYRG KGCVDDSGFV YKLGERFFPG HSNCPCVCAL DGPVCDQPEC PKIHPKCTKV EHNGCCPECK EVKNFCEYHG KNYKILEEFK PSPCEWCRCE PSNEVHCVVA DCAVPECVNP VYEPEQCCPV CKNGPNCFAG TTIIPAGIEV KVDECNICHC HNGDWWKPAQ CSKRECQGKQ TV
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Molecular Weight
24.5 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
VWC2L, or von Willebrand factor C domain containing 2-like protein, is a member of the von Willebrand factor family, which plays a critical role in various biological processes, including cell adhesion, signaling, and ligation. Its unique structure, characterized by the presence of von Willebrand factor C domains, suggests potential functions in cardiovascular biology and hemostasis. Recent studies have indicated that VWC2L may be involved in the modulation of vascular permeability and inflammation, making it a compelling target for research in cardiovascular diseases and disorders related to coagulation. Recombinant VWC2L proteins have been produced to facilitate in vitro studies aimed at uncovering its functional roles and interactions with other biological molecules. Understanding VWC2L's mechanisms may provide insights into its potential as a biomarker or therapeutic target in diseases such as thrombosis and atherosclerosis. Given the increasing prevalence of these conditions in the global population, ongoing research into VWC2L and its properties could pave the way for novel interventions and improvements in patient outcomes. Thus, the study of VWC2L recombinant proteins is essential in advancing our understanding of vascular biology and developing innovative strategies for disease management.
