lap3

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.

C-X-C chemokine receptor type 4 (CXCR4) is an alpha-chemokine receptor specific for stromal-derived-factor-1 (SDF-1 also called CXCL12), a molecule endowed with potent chemotactic activity for lymphocytes. This receptor is one of several chemokine receptors that HIV isolates can use to infect CD4+ T cells. CXCR4 stands out for its pleiotropic roles in both physiological and pathological conditions and it represents a crucial target in drug development. CXCL12 is the principal CXCR4 specific ligand and that the pro-inflammatory chemokine macrophage migration inhibitory factor (MIF) is also able to bind and activate CXCR4.

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.

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.