Recombinant Human LAR Protein Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human LRFN5 Fc Chimera
(Catalog #
9385-SA)
is used at 1 μg/mL, the concentration of Recombinant
Human LAR that produces 50% optimal binding response is 1.5-9 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived human LAR protein 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 |
Accession # |
|
N-terminal Sequence |
Ala27 and Gln1170 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
136 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
114-146 kDa and 14 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after opening.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
Buffer |
Supplied as a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human LAR Protein
Background
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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