Anti-CD45/PTPRC Antibody Picoband® Fluoro488 Conjugated

CD45 (Cluster of Differentiation 45), also known as PTPRC, LCA or CD45R, is an enzyme that, in humans, is encoded by the PTPRC gene. CD45 is a member of the protein tyrosine phosphatase (PTP) family. CD45 is a major high molecular mass leukocyte cell surface molecule which is also an integral membrane protein tyrosine phosphatase. The cytogenetic location of CD45 is 1q31.3-q32.1. CD45 is especially a prototype for transmembrane protein-tyrosine phosphatase (PTP) . Targeted disruption of the CD45 gene leads to enhanced cytokine and interferon receptor-mediated activation of JAKs and STAT proteins. In vitro, CD45 ly dephosphorylates and binds to JAKs. Functionally, CD45 negatively regulates interleukin-3-mediated cellular proliferation, erythropoietin-dependent hematopoiesis, and antiviral responses in vitro and in vivo. CD45 has been best studied in T cells, where it determines T cell receptor signaling thresholds. CD45 is moved into or out of the immunological synapse (IS) membrane microdomain depending on the relative influence of interaction with the extracellular galectin lattice or the intracellular actin cytoskeleton. Galectin interaction can be finetuned by varying usage of the heavily Oglycosylated spliced regions and sialylation of Nlinked carbohydrates.

Isoform 1: Detected in thymocytes. Isoform 2: Detected in thymocytes. Isoform 3: Detected in thymocytes. Isoform 4: Not detected in thymocytes. Isoform 5: Detected in thymocytes. Isoform 6: Not detected in thymocytes. Isoform 7: Detected in thymocytes. Isoform 8: Not detected in thymocytes.

Cancer, Cancer Metabolism, Carbohydrate Metabolism, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Pathways and Processes, Signal Transduction

Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity. (Microbial infection) Acts as a receptor for human cytomegalovirus protein UL11 and mediates binding of UL11 to T-cells, leading to reduced induction of tyrosine phosphorylation of multiple signaling proteins upon T-cell receptor stimulation and impaired T-cell proliferation.

1. Anderson, J.N. et al. (2004) FASEB J. 18:8. 2. Akao, Y., Utsumi, K. R., Naito, K., Ueda, R., Takahashi, T., Yamada, K. Chromosomal assignments of genes coding for human leukocyte common antigen, T-200, and lymphocyte function-associated antigen 1, LFA-1 beta subunit. Somat. Cell Molec. Genet. 13: 273-278, 1987. 3. Falahti, R. and D. Leitenberg (2008) J. Immunol. 181:6082.