Human CRTAM Recombinant Protein His Tag Lyophilized from Innovative Research has been recombinantly produced in HEK293 cells. This is a Lyophilized protein buffered in PBS, pH7.4 with a purity of >90% as determined by SDS-PAGE..

More Details:

• Species: Human
• Target: CRTAM
• Purity: >90% as determined by SDS-PAGE.
• Source: HEK293 cells
• Storage Conditions: Lyophilized Protein should be stored at -20°C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20°C or -70°C. Avoid repeated freeze-thaw cycles.

Additional Information:

Class I-restricted T cell-associated molecule (CRTAM), a member of nectin family and the immunoglobulin superfamily, is also known as cytotoxic and regulatory T-cell molecule, which is expressed by activated CD8+ and NK T cells. CRTAM is found in spleen, thymus, small intestine, peripheral blood, and surprisingly, in brain where it is highly expressed by Purkinje cells of the cerebellum. The high affinity of CRTAM/IGSF4 adhesion allows CRTAM to disrupt IGSF4 homotypic interactions (3 - 5). IGSF4 and T cell receptor co-engagement of CRTAM-expressing CD8+ cells induces increased IFN-gamma or IL-22 production (3, 4). Furthermore, a role in cancer surveillance through NK cell-mediated rejection of IGSF4-expressing tumors has been proposed.

This protein carries a polyhistidine Tag at the C-terminal. The protein has a calculated MW of 31.9 kDa. The protein migrates as 45-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.. At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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