Recombinant Human CEACAM-1/CD66a Fc Chimera Avi Protein, CF

Recombinant Human CEACAM-1/CD66a Fc Chimera Avi 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-related cell adhesion molecule 1 (CEACAM-1), also known as cluster of differentiation 66a (CD66a) and biliary glycoprotein (BGP), is a member of the CEACAM subfamily of glycoproteins in the immunoglobulin (Ig) superfamily. The CEACAM family is involved in diverse cellular functions from cell adhesion and differentiation to proliferation, and survival and are utilized by several bacterial pathogens to bind and invade host cells (1-3). Mature human CEACAM-1 consists of an extracellular domain (ECD) with 1 V-type Ig-like domain and 3 C2-type Ig-like domains, a transmembrane domain, and a cytoplasmic region shows one ITIM motif and a calmodulin binding site (4). CEACAM-1 is unique among the CEACAM family as it is the only family member to contain the inhibitory ITIM domains. The ECD of human CEACAM-1 shares 54% and 52% amino acid sequence identity with mouse and rat CEACAM-1, respectively. Several alternative splice variants of CEACAM-1 have been reported with alterations occurring in both the ECD and cytoplasmic region, though the function of the isoforms remain poorly understood (5). CEACAM-1 can be expressed in human epithelial, endothelial, and hematopoietic cells and is involved in morphogenesis, apoptosis, angiogenesis, and cell proliferation as well as playing a role in innate and adaptive immunity (6,7). CEACAM-1 functions through either homophilic interactions with CEACAM-1 variants or binds in a heterophilic manner to other CEACAMs, including CEACAM-5, CEACAM-6, and CEACAM-8 (7). Several pathogens from Escherichia coli and Neisseria gonorrhoeae to N. meningitidis use CEACAM-1 as a ligand as a step in bacterial invasion of the host (8). CEACAM-1 signaling is associated with inhibition of proliferation and misregulation of its expression is often reported in cancer (5,9,10). As such, CEACAM-1 is being studied as a clinical biomarker and/or promising therapeutic target for several cancer types including: non-small cell lung cancer, pancreatic, colorectal, bladder, and melanomas (5,9,10). Our Avi-tag Biotinylated CEACAM-1 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.

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