Analytical Data
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Gene name
VWC2
- Application
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Alternative Names
VWC2；Brorin
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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
Q2TAL6
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Expression Region
1-325aa
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AA Sequence
MPSSTAMAVG ALSSSLLVTC CLMVALCSPS IPLEKLAQAP EQPGQEKREH ASRDGPGRVN ELGRPARDEG GSGRDWKSKS GRGLAGREPW SKLKQAWVSQ GGGAKAGDLQ VRPRGDTPQA EALAAAAQDA IGPELAPTPE PPEEYVYPDY RGKGCVDESG FVYAIGEKFA PGPSACPCLC TEEGPLCAQP ECPRLHPRCI HVDTSQCCPQ CKERKNYCEF RGKTYQTLEE FVVSPCERCR CEANGEVLCT VSACPQTECV DPVYEPDQCC PICKNGPNCF AETAVIPAGR EVKTDECTIC HCTYEEGTWR IERQAMCTRH ECRQM
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Molecular Weight
34 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 research on VWC2 recombinant protein primarily stems from its potential significance in cellular processes and implications in various diseases. VWC2, a member of the Von Willebrand factor type C domain-containing protein family, is believed to play a crucial role in the regulation of cellular interactions and signaling pathways. Its structure features a von Willebrand factor type C domain, which is associated with protein-protein interactions, making it a subject of interest in understanding its biological functions. Initial studies indicated that VWC2 may be involved in neuronal development and function, as well as vascular biology, highlighting its potential involvement in neurodegenerative disorders and vascular diseases. Recombinant protein techniques allow for the detailed study of VWC2 in vitro, aiding in elucidating its function, interactions, and potential therapeutic targets. By producing and analyzing VWC2, researchers aim to uncover its role in cytoskeletal organization, cell adhesion, and signaling, which could lead to the development of novel strategies for treating related disorders. This investigation is crucial given the growing interest in the interplay between protein function and disease pathogenesis, emphasizing the need for deeper insights into the molecular mechanisms involving VWC2. Overall, the study of VWC2 recombinant protein is positioned at the intersection of basic research and clinical application, promising future advancements in biomedical science.
