Analytical Data
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Gene name
CEACAM4
- Application
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Alternative Names
CEACAM4；CGM7；Carcinoembryonic antigen-related cell adhesion molecule 4
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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
O75871
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Expression Region
36-155aa
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AA Sequence
FTIEALPSSAAEGKDVLLLACNISETIQAYYWHKGKTAEGSPLIAGYITDIQANIPGAAYSGRETVYPNGSLLFQNITLEDAGSYTLRTINASYDSDQATGQLHVHQNNVPGLPVGAVAG
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Molecular Weight
14.7 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
CEACAM4 (Carcinoembryonic Antigen-Related Cell Adhesion Molecule 4) is a member of the CEACAM family, primarily known for its roles in cell adhesion, immune response modulation, and tumor progression. Emerging research highlights CEACAM4's potential in cancer biology, where its expression is often upregulated in various tumors, including colorectal and breast cancers. Its involvement in tumor cell interaction with the immune system has made it a target for therapeutic interventions. Additionally, CEACAM4's role in the pathogenesis of infections and its potential as a biomarker for disease progression further underscores its significance in medical research. Given its dual roles in both normal physiological processes and pathological conditions, the recombinant expression of CEACAM4 protein in model systems is crucial for elucidating its functional mechanisms. This can lead to novel diagnostic and therapeutic strategies, particularly in cancer immunotherapy and infectious disease management. The study of CEACAM4 recombinant proteins allows for detailed analysis of its structural, binding, and functional properties, providing insights necessary for drug development and understanding tumor biology. Overall, CEACAM4 presents a promising avenue for further investigation in translational medicine, highlighting the importance of comprehensive research on its recombinant forms.
