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anti-Human PTPRF Antibodies:
anti-Mouse (Murine) PTPRF Antibodies:
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Human Monoclonal PTPRF Primary Antibody for IF, IP - ABIN967916
Arnott, Sale, Miller, Sale: Use of an antisense strategy to dissect the signaling role of protein-tyrosine phosphatase alpha. in The Journal of biological chemistry 1999
Show all 4 Pubmed References
Human Monoclonal PTPRF Primary Antibody for IF, IP - ABIN967915
Tao, Malbon, Wang: Galpha(i2) enhances insulin signaling via suppression of protein-tyrosine phosphatase 1B. in The Journal of biological chemistry 2001
Show all 3 Pubmed References
Mammalian Monoclonal PTPRF Primary Antibody for ISt, IHC - ABIN1304788
Liu, Peng, Tobin: A new 12-gene diagnostic biomarker signature of melanoma revealed by integrated microarray analysis. in PeerJ 2013
Show all 2 Pubmed References
PTPRF may have value as a predictive marker to identify which patients can obtain the greatest benefit from erlotinib in the post-first-line setting.
Homozygous truncating PTPRF mutation causes athelia.
PTPRF is down-regulated in hepatocellular carcinoma-facilitated tumor development.
Interaction between the tripartite NGL-1 (show LRRC4C Antibodies), netrin-G1 (show NTNG1 Antibodies) and LAR adhesion complex promotes development of excitatory synapses.
LAR functions as a negative regulator of adipogenesis.
Trans-synaptic adhesions between netrin-G ligand-3 (NGL-3 (show LRRC4B Antibodies)) and receptor tyrosine phosphatases LAR, protein-tyrosine phosphatase delta (show PTPRD Antibodies) (PTPdelta), and PTPsigma (show PTPRS Antibodies) via specific domains regulate excitatory synapse formation.
regulation of expression by cell density through functional E-cadherin (show CDH1 Antibodies) complexes
interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs (show PTPRS Antibodies)
LAR PTPase domains play distinct functional roles in phosphorylation and dephosphorylation
LAR as a crucial regulator of the sensitivity of two key insulin (show INS Antibodies) signalling pathways to insulin (show INS Antibodies)
loss of LAR activity resulted in reduced activity of CDK1 (show CDK1 Antibodies).
Study has identified LAR as a regulator of key signaling pathways, including mTOR (show FRAP1 Antibodies) and JNK (show MAPK8 Antibodies), and has significantly expanded the number of proteins regulated downstream of LAR phosphatase activity.
Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR and RPTPsigma (show PTPRS Antibodies) and Modulation of the Rho/ROCK Pathway.
This study demonstrates the crucial role of LAR in restricting regrowth of injured CNS axons
Ptprs (show PTPRS Antibodies) and Ptprf deficiency affects mandibular cell proliferation.
Inhibition of LAR attenuates palmitate-induced insulin (show INS Antibodies) resistance in myotubes.
Deletion of LAR in knock-out mice or blockade of LAR with sequence-selective peptides significantly overcomes neurite growth restrictions of chondroitin sulfate proteoglycan (show Vcan Antibodies) in neuronal cultures.
the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type IIa receptor Dlar and its mouse homolog LAR were reported.
LAR reduces the basal c-Abl activity thereby allowing for platelet derived growth factor beta receptor kinase activation
LAR deficiency affected the differentiation & expansion of immature thymocytes, positive & negative selection, & a lower Ca2+ response. LAR is an important modulator of TCR signaling that controls thymocyte differentiation.
Presynaptic PTPsigma (show PTPRS Antibodies) controls the number of olfactory sensory neuron and mitral cell synapses by suppressing excessive increase of axon terminals.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains three Ig-like domains, and nine non-Ig like domains similar to that of neural-cell adhesion molecule. This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherents junctions, as well as in the control of beta-catenin signaling. An increased expression level of this protein was found in the insulin-responsive tissue of obese, insulin-resistant individuals, and may contribute to the pathogenesis of insulin resistance. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.
, leukocyte antigen-related (LAR) PTP receptor
, leukocyte antigen-related tyrosine phosphatase
, leukocyte common antigen related
, protein tyrosine phosphatase, receptor type, F polypeptide
, receptor-linked protein-tyrosine phosphatase LAR
, receptor-type tyrosine-protein phosphatase F
, protein tyrosine phosphatase receptor-type F