Recombinant Human MXRA8/DICAM Protein, CF Summary
His23-Gln341, with a C-terminal 6-his tag
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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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
DICAM, also known as Limitrin and MXRA8, is an approximately 70 kDa transmembrane adhesion protein that is expressed on the endothelium of many tissues (1). In the vascular system, it is found on pericytes, vascular endothelial cells (EC), and the vessel-contacting feet of astrocytes (2). It is up-regulated on EC by VEGF and functions as a negative regulator of angiogenesis (3). It inhibits VEGF-induced signaling, cell migration, capillary tube formation, and in vivo angiogenesis, and promotes EC apoptosis (3). The interaction of DICAM with Integrin alpha V beta 3 enhances cell adhesion and inhibits the differentiation of osteoclasts (1, 4). Mature human DICAM consists of a 322 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and an 80 aa cytoplasmic domain (2). Within the ECD, human DICAM shares 79% aa sequence identity with mouse and rat DICAM. Alternative splicing generates additional isoforms that lack most of the first Ig-like domain or have a substituted signal peptide.
- Jung, Y.K. et al. (2008) J. Cell Physiol. 216:603.
- Yonezawa, T. et al. (2003) Glia 44:190.
- Han, S.-W. et al. (2013) Cardiovasc. Res. 98:73.
- Jung, Y.-K. et al. (2012) J. Bone Mineral Res. 27:2024.
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