Analytical Data
-
Gene name
WFDC1
- Application
-
Alternative Names
WFDC1；PS20；WAP four-disulfide core domain Protein 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9HC57
-
Expression Region
32-220aa
-
AA Sequence
KNIWKRALP ARLAEKSRAE EAGAPGGPRQ PRADRCPPPP RTLPPGACQA ARCQADSECP RHRRCCYNGC AYACLEAVPP PPVLDWLVQP KPRWLGGNGW LLDGPEEVLQ AEACSTTEDG AEPLLCPSGY ECHILSPGDV AEGIPNRGQC VKQRRQADGR ILRHKLYKEY PEGDSKNVAE PGRGQQKHFQ
-
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
WFDC1, or WAP four-disulfide core domain protein 1, is a member of the WFDC protein family that plays a vital role in various biological processes, including immune response, inflammation, and tissue remodeling. Originally identified as a gene expressed in the epididymis, WFDC1 has garnered attention due to its potential involvement in cancer progression and metastasis, particularly in epithelial-derived tumors. It is believed to act as a suppressor of cancer cell invasion and migration, making it a target of interest for therapeutic strategies. Furthermore, its unique structural features, characterized by a four-disulfide core, suggest it could have distinct inhibitory functions on proteases, thereby impacting the extracellular matrix and cellular signaling pathways. Recent studies indicate that WFDC1 may also be implicated in the modulation of the tumor microenvironment, which further cements its relevance in cancer biology. Consequently, the recombinant expression of WFDC1 has become an essential focus for understanding its biological functions and therapeutic potential. Scientists aim to produce high-quality recombinant WFDC1 proteins to study their interactions and mechanisms of action in cellular models. This research not only enhances our understanding of WFDC1's role in tumor dynamics but also opens new avenues for developing targeted cancer therapies that exploit the protein's regulatory properties. Through these investigations, the aim is to delineate the relevance of WFDC1 in clinical contexts, potentially offering novel biomarkers or therapeutic targets for cancer diagnosis and treatment. Thus, studying the recombinant form of WFDC1 is crucial for uncovering its functions and developing innovative approaches in cancer therapeutics.
