Recombinant Human LAR Protein Summary
Ala27-Glu1251 with a C-terminal 6-His tag, and its proteolyzed forms Ala27-Arg1169 and Gln1170-Glu1251 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||Supplied as a 0.2 μm filtered solution in PBS.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
PTPRF (Receptor-type tyrosine-protein phosphatase F), also called LAR (Leukocyte common antigen related), is a 212 kDa single-pass type I membrane protein that is a member of the protein tyrosine phosphatase (PTP) family and the receptor class 2A subfamily (1). Human LAR cDNA encodes 1,907 amino acids (aa) including a 29 aa signal sequence, a 1234 aa extracellular region with six potential N-glycosylation sites, a 21 aa transmembrane sequence, and a 623 aa cytoplasmic domain (1). An 1,898 aa isoform appears from alternative splicing; it is missing aa 772 to 780 (1). Human LAR shares a 95% aa sequence identity with mouse and rat LAR. LARs have been shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling (2). An increased expression level of LARs have been found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance (3). LARs have been identified as novel ligands of SALM5/LRFN-5 that mediates SALM5/LRFN-5 dependent presynaptic differentiation in a splicing- dependent manner. SALM5/LRFN-5 interacts directly with the Ig domain of LAR family receptor protein tyrosine phosphatases. The postsynaptic SALM5/LRFN-5 promotes synapse development by trans-synaptically interacting with presynaptic LARs which is important for the regulation of excitatory synaptic strength (4). Clinically, LAR has been shown down-regulated in cancers and its up-regulation is associated with better clinical outcomes (5).
- SwissProt Accession # P10586.
- Um J.W. et al. (2013) Trends Cell Biol. 23:465.
- Mander A. et al. (2005) FEBS Lett. 579:3024.
- Choi, Y. et al. (2016) Sci Rep. 6:26676.
- Bera, R. et al. (2014) Hepatology. 59:2238.
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