Anti-Protease activated receptor 2 Antibody, Non-Fucosylated (BioBet-853ZP) (CAT#: BioBet-853ZP) Datasheet

F2RL1

coagulation factor II (thrombin) receptor-like 1

Coagulation factor II (thrombin) receptor-like 1 (F2RL1) is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL1 is also a member of the protease-activated receptor family. It is activated by trypsin, but not by thrombin. It is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. The F2RL1 gene contains two exons and is widely expressed in human tissues. The predicted protein sequence is 83% identical to the mouse receptor sequence.

F2RL1; coagulation factor II (thrombin) receptor-like 1; PAR2; GPR11; proteinase-activated receptor 2; thrombin receptor-like 1; G-protein coupled receptor 11; protease-activated receptor 2; coagulation factor II receptor-like 1

Plasma membrane

Diseases associated with F2RL1 include Pulmonary Vein Stenosis and Granulomatous Orchitis.

Its related pathways are RET signaling and Signaling by GPCR.

Receptors for trypsin and trypsin-like enzymes coupled to G protein. Its function is mediated through the activation of multiple signaling pathways, including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho. It can also be activated by cracked F2R/PAR1. Participate in the regulation of inflammatory response, innate immunity and adaptive immunity, and act as a sensor to produce proteolytic enzymes in infection. Usually promote inflammation. In the inflammatory response, there may be TLR2 cooperative signals with TLR4 to regulate TLR3 signals. It has a protective effect on the establishment of the endothelial barrier; coagulation factor x regulates the integrity of the endothelial cell barrier in the process of neutrophil extravasation, which may occur under the proteolysis of PRTN3. It is believed to have a bronchial protective effect in the airway epithelium, but it has also been shown to disrupt the airway epithelial barrier by interrupting E-cadherin adhesion. Participate in the regulation of vascular tension; activation leads to hypotension, which may be mediated by vasodilation. Participate in cell migration. Participate in cytoskeleton rearrangement and scaffold chemotaxis promoted by -arrestin; this function is independent of GNAQ and GNA11, including promotion of cofilin dephosphorylation and actin filament cutting. Inducing the redistribution of COPS5 from the plasma membrane to the cytoplasm, the activation of the JNK cascade is mediated by COPS5. Participating in the recruitment of leukocytes to inflammation sites, it is the main PAR receptor that can regulate the functions of eosinophils, such as the secretion of pro-inflammatory cytokines, the production of superoxide and degranulation. Inflammation promotes the maturation of dendritic cells, metastasis to lymph nodes and subsequent activation of T cells. Participate in the antibacterial response of natural immune cells; activation can enhance the phagocytosis of Gram-positive bacteria and the killing effect of Gram-negative bacteria. Synergize with interferon to enhance antiviral response. Involved in many acute and chronic inflammatory diseases, such as joints, lungs, brain, gastrointestinal tract, periodontal, skin and vascular system, and autoimmune diseases.

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand. Activating serine proteases include trypsin, mast cell tryptase, coagulation factors VII and Xa, myeloblastin/PRTN3 and membrane-type serine protease 1/ST14. Proposed subsequent cleaveage by serine proteases is leading to receptor deactivation and include neutrophil elastase and cathepsin G. At least in part, implicated proteases are also shown to activate the receptor; the glycosylation status of the receptor is thought to contribute to the difference. In addition to conventional trypsin-like proteases is proposed to be activated by other proteases and glycosidases derived from bacteria, fungi and insects: serine protease allergens such as dust mite Der p3 and Der p9 and mold Pen c13, Porphyromonas gingivalis arginine-specific (trypsin-like) cysteine proteinases called gingipains, Streptomyces griseus exogenous chitinase, and an Alternaria alternata aspartate protease. Cleavage by the Alternaria alternata aspartate protease generates non-conventional processed forms. N-glycosylated and sialylated. Multiple phosphorylated on serine and threonine residues in the cytoplasmic region upon receptor activation; required for receptor desensitization. Monoubiquitinated by CBL at the plasma membrane and in early endosomes; not required for receptor endocytosis but for translocation to late endosomes or lysosomes. Deubiquitination involves STAMBP and USP8; required for lysosomal trafficking and receptor degradation.

Protein Based Therapies
Monoclonal antibody (mAb)

IgG

BioBet-853ZP

Human

Human

The anti-PAR-2 antibody can be used for treatment of pain, including post-operative incision pain, neuropathic pain, fracture pain, osteroporotic fracture pain, bone cancer pain or gout joint pain; inflammatory pain associated with irritable bowel syndrome; and inflammation related to rheumatoid arthritis or osteoarthritis.

Inflammatory Diseases

Inflammatory Diseases