Mouse Anti-F2R Recombinant Antibody (CBYC-P064) (CBMAB-P0329-YC)

Mouse

Human

CBYC-P064

IgG2b

FC

E. coli-derived Recombinant human PAR1, Arg27-Thr102, Ser375-Thr425

Human

IgG2b

Monoclonal

The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Saline solution containing BSA and sodium azide

Store at 4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Coagulation Factor II Thrombin Receptor

Coagulation factor II receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member.

CF2R; TR; HTR; PAR-1; PAR1

High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development.

Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
Activation of MAPKK activity Source: UniProtKB
Anatomical structure morphogenesis Source: ProtInc
Cell-cell junction maintenance Source: UniProtKB
Connective tissue replacement involved in inflammatory response wound healing Source: BHF-UCL
Establishment of synaptic specificity at neuromuscular junction Source: UniProtKB
G protein-coupled receptor signaling pathway Source: UniProtKB
Homeostasis of number of cells within a tissue Source: UniProtKB
Inflammatory response Source: UniProtKB
Negative regulation of cell population proliferation Source: BHF-UCL
Negative regulation of glomerular filtration Source: UniProtKB
Negative regulation of neuron apoptotic process Source: UniProtKB
Negative regulation of renin secretion into blood stream Source: UniProtKB
Phospholipase C-activating G protein-coupled receptor signaling pathway Source: BHF-UCL
Platelet activation Source: BHF-UCL
Platelet dense granule organization Source: BHF-UCL
Positive regulation of blood coagulation Source: BHF-UCL
Positive regulation of calcium ion transport Source: UniProtKB
Positive regulation of cell migration Source: BHF-UCL
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of collagen biosynthetic process Source: BHF-UCL
Positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
Positive regulation of cytosolic calcium ion concentration Source: UniProtKB
Positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling Pathway Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
Positive regulation of GTPase activity Source: UniProtKB
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of interleukin-6 production Source: UniProtKB
Positive regulation of interleukin-8 production Source: UniProtKB
Positive regulation of MAPK cascade Source: BHF-UCL
Positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
Positive regulation of receptor signaling pathway via JAK-STAT Source: BHF-UCL
Positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
Positive regulation of Rho protein signal transduction Source: UniProtKB
Positive regulation of smooth muscle contraction Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: BHF-UCL
Positive regulation of vasoconstriction Source: UniProtKB
Protein kinase C-activating G protein-coupled receptor signaling pathway Source: UniProtKB
Regulation of blood coagulation Source: BHF-UCL
Regulation of interleukin-1 beta production Source: UniProtKB
Regulation of sensory perception of pain Source: UniProtKB
Release of sequestered calcium ion into cytosol Source: UniProtKB
Response to lipopolysaccharide Source: UniProtKB
Response to wounding Source: BHF-UCL
Trans-synaptic signaling by endocannabinoid, modulating synaptic transmission Source: Ensembl

Cell membrane

Extracellular: 42-102
Helical: 103-128
Cytoplasmic: 129-137
Helical: 138-157
Extracellular: 158-176
Helical: 177-198
Cytoplasmic: 199-218
Helical: 219-239
Extracellular: 240-268
Helical: 269-288
Cytoplasmic: 289-311
Helical: 312-334
Extracellular: 335-350
Helical: 351-374
Cytoplasmic: 375-425

A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Phosphorylated in the C-terminal tail; probably mediating desensitization prior to the uncoupling and internalization of the receptor.