PTPRF removes phosphate group from β-catenin, an event that may subsequently facilitate cell-cell adhesion and ensure the stability of the cadherin complex. This phosphatase has also been implicated in various cellular processes such as neurite growth, nerve regeneration, actin remodeling and regulation of insulin function .
Immunogen
synthetic peptide corresponding to an internal region of human PTPRF, conjugated to KLH. The corresponding sequence differs by two amino acids in mouse and rat.
Application
Anti-PTPRF antibody is suitable for use in immunoblot (1:250-1:500 using lysates of HEK-293T cells over-expressing human PTPRF).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The human transmembrane molecule LAR is a protein tyrosine phosphatase (PTPase) with a cell adhesion molecule-like extracellular receptor region. The structure of LAR hinted at its involvement in the regulation of tyrosine phosphorylation through cell-cell or cell-matrix interactions. We show
Biochemistry and cell biology = Biochimie et biologie cellulaire, 82(6), 664-675 (2005-01-28)
The protein tyrosine phosphatases (PTPs) have emerged as critical players in diverse cellular functions. The focus of this review is the leukocyte common antigen-related (LAR) subfamily of receptor PTPs (RPTPs). This subfamily is composed of three vertebrate homologs, LAR, RPTP-sigma
Current topics in medicinal chemistry, 3(7), 809-819 (2003-04-08)
The leukocyte common antigen-related protein, LAR, is a receptor-like protein tyrosine phosphatase (PTP) which has a wide tissue distribution. Post-translational processing cleaves the proprotein into two non-covalently associated subunits, an extracellular subunit resembling a cell adhesion molecule with three immunoglobulin-like
The Journal of biological chemistry, 272(1), 448-457 (1997-01-03)
The receptor-type protein-tyrosine phosphatase LAR (for leukocyte common antigen-related) has been implicated as a physiological regulator of the insulin receptor. To demonstrate a functional interaction between LAR and the insulin receptor, we incubated CHO cells overexpressing the human insulin receptor
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