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Proteinase-activated receptor-4 (extracellular) polyclonal antibody

 
BML-SA652-0050 50 µl 334.00 USD
 
BML-SA652-0200 200 µl 504.00 USD
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Product Specification

Alternative Name:PAR-4
 
Host:Rabbit
 
Immunogen:Synthetic peptide corresponding to aa 136-150 (with a C149S replacement) of human PAR-4 (proteinase-activated receptor-4).
 
UniProt ID:Q96RI0
 
Species reactivity:Human, Rat
 
Applications:Flow Cytometry, ICC, IHC, WB
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Scientific Background:PAR-4 belongs to a four member family of G protein-coupled receptors (PAR-1 to -4) that are activated as a result of proteolytic cleavage by certain serine proteases, hence their name. In this modality of activation, a specific proteinase cleaves the PAR receptor within a defined sequence in its extracellular N-terminal domain. This cleavage results in the creation of a new N-terminal sequence (tethered ligand), which subsequently binds to a site in the second extracellular loop of the same receptor. This binding results in the coupling of the receptor to G proteins and in the activation of several signal transduction pathways1-3 Different PARs are activated by different proteinases. PAR-4 is activated by both thrombin and trypsin whereas PAR-1 and PAR-3 are activated by thrombin and PAR-2 is activated by trypsin1-3. PAR-4 can be also cleaved and activated by other proteinases such as cathepsin G. The intracellular signaling mechanisms mediated by PAR-4 activation are not completely elucidated but they may involve calcium mobilization downstream of phospholipase C through the Gαq pathway1-3 Tissue distribution of PAR-4 is very broad with the highest expression levels found in lung, testis, pancreas and small intestine. In addition, PAR-4 expression was observed in platelets, megakaryocytes and leukocytes. Studies with platelets derived form PAR-4 knockout mice have established an essential role for PAR-4 in thrombin-induced platelet activation.PAR-4 is likely involved in other physiological functions such as regulation of gastrointestinal motility and regulation of vascular endothelial cell function1-3.
 

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