Anti-Pleiotrophin/PTN Antibody Picoband® Fluoro647 Conjugated

Pleiotrophin (PTN) also known as heparin-binding brain mitogen (HBBM) or heparin-binding growth factor 8 (HBGF-8) or neurite growth-promoting factor 1 (NEGF1) or heparin affinity regulatory peptide (HARP) or heparin binding growth associated molecule (HB-GAM) is a protein that in humans is encoded by the PTN gene. PTN is the first member of a family of developmentally regulated cytokines. The PTN gene is mapped to 7q33-q34. A mutant PTN that contained only the first N-terminal 40 amino acids was a dominant negative. Pleiotrophin is expressed in the central and peripheral nervous system and also in several non-neural tissues, notably lung, kidney, gut and bone. Pleiotrophin binds to cell-surface nucleolin as a low affinity receptor. This binding can inhibit HIV infection.

Pleiotrophin; PTN; Heparin-binding brain mitogen; HBBM; Heparin-binding growth factor 8; HBGF-8; Heparin-binding growth-associated molecule; HB-GAM; Heparin-binding neurite outgrowth-promoting factor 1; HBNF-1; Osteoblast-specific factor 1; OSF-1; PTN; HBNF1, NEGF1

Cancer, Cytokines, Cytoskeleton/ECM, Extracellular Matrix, Growth and Development, Growth Factors, Immunology, Innate Immunity, Neurology Process, Neuroscience, Signal Transduction, Structures

Secreted growth factor that induces neurite outgrowth and which is mitogenic for fibroblasts, epithelial, and endothelial cells. Binds anaplastic lymphoma kinase (ALK) which induces MAPK pathway activation, an important step in the anti- apoptotic signaling of PTN and regulation of cell proliferation. .

1. Entrez Gene: PTN pleiotrophin (heparin binding growth factor 8, neurite growth-promoting factor 1) . 2. Vanderwinden JM, Mailleux P, Schiffmann SN, Vanderhaeghen JJ (1992) . Cellular distribution of the new growth factor pleiotrophin (HB-GAM) mRNA in developing and adult rat tissues. Anat. Embryol. 186 (4) : 387–406. 3. Said EA, Courty J, Svab J, Delbé J, Krust B, Hovanessian AG (September 2005) . Pleiotrophin inhibits HIV infection by binding the cell surface-expressed nucleolin. FEBS J. 272 (18) : 4646–59.