Recombinant Human LRRC4 Protein, CF Summary
Ala39-Lys527, with a C-terminal 6-His tag
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 400 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.
LRRC4 (Leucine rich repeat/LRR-containing protein 4), also called NGL-2 (netrin-G ligand-2) or NAG14 (nasopharyngeal carcinoma-associated gene 14) is a 55 kDa (predicted) type I transmembrane protein that is a member of the NGL family of synaptic LRR adhesion molecules (1, 2). Human LRRC4 cDNA encodes 653 amino acids (aa) that include a 38 aa signal sequence, a 489 aa extracellular domain (ECD), a 21 aa transmembrane domain, and a 105 aa cytoplasmic domain. The ECD contains nine LRRs (aa 74 ‑ 288), a C2 type Ig like domain (aa 354 ‑ 440), and a Thr-rich segment (aa 455 ‑ 526). Within the ECD, human LRRC4 shares 98% aa identity with mouse and rat, 99% aa identity with canine and bovine, and 99.6% aa identity with equine LRRC4. It also shares 54 ‑ 55% aa identity with family members LRRC4C/NGL-1 and LRRC4B/NGL-3, but each recognizes different ligands (1). LRRC4 is predominantly expressed in the brain on neurons and astrocytes as a ligand for netrin-G2 on the dendritic surface of synaptic neurons (2 - 4). It is proposed to regulate the formation of excitatory synapses via recruitment of PSD-95 to the cytoplasmic domain after aggregation of LRRC4 at the surface (3, 5). It suppresses proliferation by downregulating cell signaling pathways, resulting in altered expression of cell cycle regulating proteins and delay at the late G1 phase (1, 2, 6 - 8). It is thus considered a tumor suppressor protein and is often downregulated in brain tumors, particularly gliomas (1, 2, 6). Forced expression of LRRC4 in tumor cells slows proliferation and promotes differentiation (1, 4, 9). Addition of soluable LRRC4 to cultured neurons reduces excitatory synapse formation (3).
- Woo, J. et al. (2009) Mol. Cell. Neurosci. 42:1.
- Zhang, Q. et al. (2005) FEBS Lett. 579:3674.
- Kim, S. et al. (2006) Nat. Neurosci. 9:1294.
- Wu, M. et al. (2007) Acta Biochim Biophys Sin (Shanghai) 39:731.
- Nishimura-Akiyoshi, S. et al. (2007) Proc. Natl. Acad. Sci. USA 104:14801.
- Wu, M. et al. (2006) Mol. Biol. Cell 17:3534.
- Wu, M. et al. (2008) J. Cell. Biochem. 103:245.
- Wu, M. et al. (2008) J. Cell. Physiol. 214:65.
- Zhang, W. et al. (2008) Genes Brain Behav. 7:385.
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