Recombinant Human DSCAM Protein, CF

Recombinant Human DSCAM 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: DSCAM

Down syndrome cell adhesion molecule (DSCAM) is a 220 kDa type I transmembrane glycoprotein and member of the immunoglobulin superfamily (1). Human DSCAM, which maps to a Down syndrome region of chromosome 21q22.2-22.3, is synthesized as a 2012 amino acid (aa) precursor that contains a 17 aa signal sequence, a 1578 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 396 aa cytoplasmic tail (SwissProt #: O60469). The ECD contains ten Ig-like C2-type domains, six fibronectin type-III domains, and 16 potential sites for N-linked glycosylation. Splicing variants lead to a second, shorter isoform, which has a ten aa substitution for aa 1562 - 1571 in the longer isoform, and a deletion of residues corresponding to aa 1572 - 2012 in the longer isoform. Human mature DSCAM is 98% aa identical to mature mouse and rat DSCAM. Studies on mice have shown that DSCAM is expressed widely in the developing nervous system (1 - 2). More recent studies indicate that DSCAM plays an important role in neurite arborization, cell body spacing, and lamina-specific synaptic targeting in vertebrate retina (2 - 4). DSCAM signaling in vertebrates is not well understood, but it has been shown that DSCAM directly binds to Pak1 and stimulates Pak1 phosphorylation and activity (5). In addition, DSCAM activates both JNK and p38 MAP kinases, and expression of the cytoplasmic domain of DSCAM induces a morphological change in cultured cells that is JNK-dependent (5). Thus, it appears that DSCAM signals through Pak1 and functions in axon guidance. Furthermore, DSCAM, in collaboration with DCC, interacts with netrin-1, and is a receptor required for netrin-dependent commissural axon outgrowth and pathfinding (2, 6).

Related Research Areas

• Adhesion Molecules in Angiogenesis
• Immunoglobulin Superfamily CAMs
• Netrins and Receptors
• Synaptic Adhesion Molecules