lap 3

LAP3 (Leucine Aminopeptidase 3) is a Protein Coding gene. 2 alternative initiation human isoforms have been reported. LAP3, belonging to the peptidase M17 family, has been proved to catalyze the hydrolysis of leucine residues. It catalyzes the removal of unsubstituted N-terminal amino acids from various peptides and is presumably involved in the processing and regular turnover of intracellular proteins. Leucine aminopeptidases are involved in many pathological disorders and regulate cell proliferation, invasion, and or angiogenesis of tumors. A recent study showed that LAP3 is highly expressed in several malignant and affects tumor angiogenesis. LAP3 is widely expressed in the appendix, lymph node, and other tissues. Diseases associated with LAP3 include Bacterial Vaginosis and Trichomoniasis.

CXCR4 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 39.75 kDa and the accession number is P61073-1.

Transforming growth factor beta 3(TGFB3) is a member of a TGF -β superfamily which is defined by theirstructural and functional similarities. TGFB3 is secreted as a complex with LAP. This latent form of TGFB3becomes active upon cleavage by plasmin, matrix metalloproteases, thrombospondin -1, and a subset ofintegrins. It binds with high affinity to TGF- β RII, a type II serine threonine kinase receptor. TGFB3 is involved incell differentiation, embryogenesis and development.It is believed to regulate molecules involved in cellularadhesion and extracellular matrix (ECM) formation during the process of palate development. Without TGF-β3,mammals develop a deformity known as a cleft palate.

Thrombospondin-1 (TSP-1) is a 150-180kDa calcium-sensitive protein that is secreted as a disulfide-linked homotrimer. TSP-1 regulates a wide range of cellular functions including their interactions with other cells and with the extracellular matrix (ECM). TSP-1 contains an N-terminal Laminin G-like globular domain, an extended central region with one vWFC domain, 3 TSP type 1domains, 2 EGF-like domains, and 8 TSP type3 domains, and a globular TSP C-terminal domain. Distinct regions of TSP-1 have been associated with binding to particular ECM or cellular molecules. TSP-1 counteracts the angiogenic, hypotensive, and antithrombotic effects of nitric oxide (NO). It binds and neutralizes VEGF, blocks VEGF R2 signaling on vascular endothelial cells(EC), and destabilizes adhesive contacts between EC. TSP-1 also plays an important role in wound repair and tissue fibrosis by binding latent TGF-beta and inducing release of the active cytokine from the latency associated peptide (LAP).