SLITRK5 (Slit and Trk-like family member 5; also LRR-containing protein 11) is a member of the SLITRK family of proteins.1, 2 This family currently includes six members, all of which contain a slit-like extracellular region and (save for SLITRK1) a Trk-like cytoplasmic region.3 Human SLITRK5 is a type I transmembrane (TM) protein that is 958 amino acids (aa) in length. It contains a putative 40 aa signal sequence, a 624 aa extracellular domain (ECD), a 21 aa TM segment, and a 273 aa cytoplasmic region. The ECD is characterized by the presence of two leucine-rich domains (LRD) that resemble those found in slit. Each LRD (aa # 80-285 plus aa # 384-579) contains seven and eight leucine-rich repeats (LRRs), respectively. The exact function of the LRRs is not known. Based on other LRRs, it might be assumed that they mediate protein-protein-interaction.4 The cytoplasmic region contains two conserved, potential phosphorylation sites at Tyr 833 and Tyr 917, plus a TrkA-like tyrosine phosphorylation site (YLxxL) at Tyr 945. SLITRK5 is expressed on embryonic neurons of the hippocampus (pyramidal layer) and thalamus.3 Based on SLITRK2 studies, SLITRK5 will block neurite extension.3 Human SLITRK5 shares 97% and 98% aa identity with mouse and canine SLITRK5, respectively.||A DNA sequence encoding the extracellular domain of human SLITRK5 (Glu 39-Val 665; Accession # NP_056382) was fused with a 6X histidine tag at the C-terminus. The protein was expressed in a mouse myeloma cell line, NS0.||Calculated molecular mass of ~ 70.8kD. As a result of glycosylation, recombinant human SLITRK5 migrates as an ~ 100-120kD protein in SDS-PAGE under reducing conditions.||Activity: Measured by its ability to induce neurite outgrowth of E13 chick dorsal root ganglia neurons.||Storage and Stability:|Lyophilized powder may be stored at 4°C for short-term only. Reconstitute to nominal volume by adding sterile PBS and store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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