Anti-PTPN12 Antibody Picoband® Fluoro594 Conjugated

Tyrosine-protein phosphatase non-receptor type 12 is an enzyme that in humans is encoded by the PTPN12 gene. The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may regulate protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of the oncogene c-ABL and thus may play a role in oncogenesis. This PTP was also shown to interact with, and dephosphorylate, various products related to cytoskeletal structure and cell adhesion, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin. This suggests it has a regulatory role in controlling cell shape and mobility. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

Platelet basic protein; PBP; C-X-C motif chemokine 7; Leukocyte-derived growth factor; LDGF; Macrophage-derived growth factor; MDGF; Small-inducible cytokine B7; PPBP; CTAP3; CXCL7; SCYB7; TGB1; THBGB1; NAP-2

LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2 (73), NAP-2 (74), NAP-2 (1-66), and most potent NAP-2 (1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III (1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation.

1. Charest, A., Wagner, J., Muise, E. S., Heng, H. H. Q., Tremblay, M. L. Structure of the murine MPTP-PEST gene: genomic organization and chromosomal mapping. Genomics 28: 501-507, 1995. 2. Cong, F., Spencer, S., Cote, J.-F., Wu, Y., Tremblay, M. L., Lasky, L. A., Goff, S. P. Cytoskeletal protein PSTPIP1 s the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Molec. Cell 6: 1413-1423, 2000. 3. Spencer, S., Dowbenko, D., Cheng, J., Li, W., Brush, J., Utzig, S., Simanis, V., Lasky, L. A. PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for PEST tyrosine phosphatase. J. Cell Biol. 138: 845-860, 1997.