Recombinant Human MAdCAM-1 Fc Chimera Avi-tag Protein, CF

Recombinant Human MAdCAM-1 Fc Chimera Avi-tag 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: MAdCAM-1

Mucosal addressin cell adhesion molecule-1 (MAdCAM-1) is an approximately 60 kDa type 1 transmembrane glycoprotein. It is an endothelial cell adhesion molecule that belongs to the immunoglobulin (Ig) superfamily of proteins (1). Human MAdCAM-1 is synthesized as a 382 amino acid (aa) precursor that contains an 18 aa signal sequence, a 299 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 44 aa cytoplasmic tail. Within the ECD there is one potential site for N-linked glycosylation (2). The ECD comprises two Ig-like domains of 90 aa and 119 aa, respectively, each possessing invariant cysteine residues that stabilize the Ig loop (2). There is also a Ser-Thr-Pro-rich (71%) mucin-like 48 aa domain that is (aa 206 ‑ 317) formed by six tandem repeats of an eight aa sequence having the general consensus DTTSPEP/SP. This mucin domain contains 19 potential sites for O-linked glycosylation (2, 3). A splicing variant in which a single Ala residue is substituted for aa 223 ‑ 334 in isoform 1 produces a second isoform. Human mature MAdCAM-1 shares only 44% aa sequence identity with mature mouse MAdCAM-1. The integrin alpha (4)  beta (7), which is expressed on lymphocytes, functions as the MAdCAM-1 receptor (1). The Ig domains of MAdCAM-1 are critical to alpha (4)  beta (7)  binding, and the mucin domain has activity in L‑Selectin binding. MAdCAM-1 expression is up-regulated by TNF-alpha  and IL‑1 beta. MAdCAM-1 is expressed on the surface of high endothelial venules (HEV) in the gut and in Peyer's patches, on endothelial cells of the mesenteric lymph nodes, lamina propria of the small and large intestine, and the mammary gland during lactation, and on brain endothelial cells (1). MAdCAM‑1 has also been reported to be expressed in the liver portal region in autoimmune hepatitis (1), and in bone marrow following allogenic (genetically non-identical) hematopoietic stem cell transplantation, where it recruits donor T cells, which may lead to graft versus host disease (3, 4). MAdCAM‑1 functions as a homing receptor, and plays a central role in leukocyte migration into HEVs and Peyer's patch (5). In addition to its normal role in lymphocyte trafficking to mucosal tissue, MAdCAM‑1 expression is also dramatically increased in chronic inflammatory and disease states (1, 6), including inflammatory bowel disease (Crohn's disease and ulcerative colitis) (7), sclerosing cholangitis (8), and diabetes (9), and may play an important role in these conditions. Our Avi-tag Biotinylated human MAdCAM‑1 Fc Chimera 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
• Immunoglobulin Superfamily CAMs
• Regulatory T Cells (Tregs)