Analytical Data
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Gene name
WFDC2
- Application
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Alternative Names
WFDC2；HE4；WAP four-disulfide core domain Protein 2
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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
Q14508
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Expression Region
31-124aa
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AA Sequence
EKTGVCPELQADQNCTQECVSDSECADNLKCCSAGCATFCSLPNDKEGSC PQVNINFPQLGLCRDQCQVDSQCPGQMKCCRNGCGKVSCVTPNF
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Molecular Weight
11 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
WFDC2, or WAP Four-Disulfide Core Domain 2, is a protein that is part of a larger family known for their role in various biological processes, including immune responses and cell signaling. Research into WFDC2 has gained traction due to its potential implications in cancer biology, where it may influence tumor progression and metastasis. Studies have suggested that WFDC2 is involved in the regulation of extracellular matrix components and has been linked to inflammatory responses, which are critical in various pathological conditions. The recombinant form of WFDC2 is of particular interest for in-depth studies, as it allows for the investigation of its functional properties and interactions with other biomolecules. The recombinant protein can be utilized in various assays to explore its role in cellular processes, providing insights into its mechanisms of action and potential therapeutic applications. Furthermore, understanding the structure-function relationship of WFDC2 through recombinant technology could aid in the development of novel strategies for disease intervention, particularly in cancers where WFDC2 expression levels are altered. Overall, the study of WFDC2 recombinant protein presents a promising avenue for advancing our understanding of its biological functions and therapeutic potential in disease contexts.
