Recombinant Human CEACAM-1/CD66a Protein, CF

Recombinant Human CEACAM-1/CD66a Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: CEACAM-1/CD66a

Carcinoembryonic antigen (CEA)-related cell adhesion molecule 1 (CEACAM-1; also BGP) is a 160 kDa member of the CEACAM branch of the CEA gene family of the immunoglobulin superfamily (1 - 3). It is one of seven human CEACAM subfamily genes that are essentially divided equally between type I transmembrane proteins (CEACAM-1, 3 & 4) and GPI-linked molecules (CEACAM-5-8). There is no CEACAM-2 in human. The gene for human CEACAM-1 codes for a 526 amino acid (aa) type I transmembrane protein that contains a 34 aa signal sequence, a 394 aa extracellular domain (ECD), a 24 aa transmembrane segment, and a 74 aa cytoplasmic region (4, 5). The ECD contains one N-terminal V-type Ig-like domain, followed by three C2-type Ig-like domains. It shows considerable glycosylation, including high mannose residues and (sialyl) Lewis^X (1). The cytoplasmic region shows one ITIM motif and a calmodulin binding site (1 - 3). In addition to the full length form, ten alternate splice forms have been reported (1, 4, 6, 7, 8). There are three soluble and seven transmembrane isoforms, with variations occurring in both the ECD and cytoplasmic region. All ten alternate splice forms contain the V-type Ig-like domain (aa’s 35 - 142). The three soluble forms also contain the first two C2-type Ig-like domains (aa’s 145 - 317), with differences coming in the third C2-type Ig-like domain (6). The seven transmembrane isoforms are highly divergent. Five of the seven contain the V-type plus the first two C2-type domains and then diverge considerably both in the ECD and cytoplasmic region. The remaining two contain only the V-type Ig-like domain, the transmembrane region, and either a full-length or truncated cytoplasmic tail (1, 8). The actual functions of the isoforms are unclear.
Full-length mouse and rat CEACAM-1 are approximately 57% aa identical to human CEACAM-1; in the V-type Ig-like domain, they are 58% and 56% aa identical, respectively. The full-length molecule is found on neutrophils, bile duct epithelium, activated NK cells, colonic columnar epithelium and endothelium. It is known to act as an intercellular adhesion molecule, forming both homotypic, and heterotypic bonds with CEA and CEACAM-6/NCA (3, 9). On neutrophils, CEACAM-1 also binds to dendritic cell CD-SIGN via its Le^X moiety, inducing dendritic cell maturation and a subsequent Th1-type response (10,11).

Related Research Areas

• Adhesion Molecules in Angiogenesis
• Cancer Biomarkers
• Epithelial Cell Markers and Intracellular Molecules
• Granulocyte Markers
• Immunoglobulin Superfamily CAMs
• ITIM/ITAM Immunoreceptors and Related Molecules
• Myeloid Lineage Markers
• Platelet Adhesion Molecules
• Search Immune Checkpoint Targets
• Surface Ectodermal Cells