Analytical Data
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Gene name
DERF2
- Application
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Alternative Names
DERF2；MD1；Lymphocyte antigen 86
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Species
E.coli
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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
Q00855
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Expression Region
18-146aa
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AA Sequence
DQVDVKDCANNEIKKVMVDGCHGSDPCIIHRGKPFTLEALFDANQNTKTAKIEIKASLDGLEIDVPGIDTNACHFMKCPLVKGQQYDIKYTWNVPKIAPKSENVVVTVKLIGDNGVLACAIATHGKIRD
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Molecular Weight
16.1 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
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Protein Description
DERF2, a member of the epidermal growth factor receptor (EGFR) family, has emerged as a significant player in the regulation of cellular processes such as growth, differentiation, and survival. Research indicates that DERF2 is actively involved in various signaling pathways that contribute to cancer progression, making it a potential target for therapeutic interventions. Given its structural and functional similarities to other EGFR family members, studies focusing on the recombinant expression of DERF2 protein have gained traction. The generation of DERF2 recombinant protein allows for better understanding of its biological role and interactions within cellular environments. Such studies can elucidate the mechanisms through which DERF2 influences tumorigenesis and identify potential biomarkers for cancer diagnosis and prognosis. Moreover, the recombinant DERF2 protein can serve as a valuable tool in drug development and validation, providing insights into the design of targeted therapies aimed at mitigating DERF2-related pathologies. As research advances, the exploration of DERF2’s structure-function relationships and its role in specific diseases continues to reveal promising avenues for therapeutic applications, underscoring the importance of DERF2 as a focal point in cancer biology and pharmacology.
