Analytical Data
-
Gene name
vWA2
- Application
-
Alternative Names
AMACO; VWFA2; CCSP-2; A Domain-Containing Protein Similar To Matrilin And Collagen; Colon cancer secreted protein 2
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5GFL6
-
Expression Region
Ser457~Gly708
-
Molecular Weight
30&28kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 study of vWA2 recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. vWA2, a protein containing von Willebrand factor A (vWA) domains, is part of a class of proteins known for their roles in cell adhesion and interaction with extracellular matrices. Research into vWA2 has highlighted its involvement in various biological processes, such as wound healing and tissue repair, while also revealing its implications in pathological conditions like cancer metastasis and cardiovascular diseases. The ability to produce vWA2 as a recombinant protein allows for detailed studies into its structure-function relationships, facilitating the exploration of its biochemical properties and its interactions with other cellular components. Additionally, the development of vWA2 recombinant proteins opens avenues for innovative therapeutic strategies, including targeted drug delivery systems and regenerative medicine approaches. By generating and characterizing vWA2 proteins in a controlled laboratory environment, researchers aim to unravel the mechanisms underlying its functions and evaluate its potential as a biomarker or therapeutic target. Overall, the exploration of vWA2 recombinant proteins stands at the intersection of molecular biology and clinical research, promising advancements in our understanding of complex biological systems and their manipulation for therapeutic benefit.
