Exchange Inhibitor Peptide, Rat (XIP) (Control Peptide)

Catalog No : USB-E9004-50
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Product name Exchange Inhibitor Peptide, Rat (XIP) (Control Peptide)
Catalog No USB-E9004-50
Supplier’s Catalog No E9004-50
Supplier US Biologicals
Source antigen Rat synthetic peptide
Reactivity
Cross reactivity Fr Human, Mouse, Rabbit, Rat
Applications
Molecular weight
Storage -20°C
Other names
Grade Highly Purified
Purity Highly purified
Form Supplied as a liquid in PBS, pH 7.4.
Reactivity life 12 months
Note For reserch purpose only
Purity Highly purified
Description The 20aa Peptide (designated XIP11-P; control peptide) corresponding to rat XIP. The 20 AA rat is 100% conserved in mouse, rat, human, rabbit, frog NCX1. Ca2+ plays a critical role in intracellular signaling. Intracellular Ca2+ levels are tightly controlled by continuos removal of Ca2+ via ATP-driven Ca2+ pump in the endoplasmic reticulum and plasma membrane, and Ca2+ transport system, the Na+/Ca2+ exchangers (NCX), in the plasma membrane. NCX can move Ca2+ either into or out of cells, depending on the net Na+, Ca2+, and K+ gradient across the membrane. In most cells, 3 Na+ are exchanged for 1 Ca2+. In mammals, at least 5 distinct genes code for the exchangers: Three NCX (NCX1, NCX2, and NCX3), and two in the NCKX family (NCKX1 and NCKX2). NCX share significant sequence homology (~70%), display 11 TM domains, a large central, intracellular hydrophilic regulatory loop between TM5 and 6, extracellular N-terminus and cytoplasmic C-terminus. The N-terminal signal peptide is cleaved off from the mature exchanger protein. NCX contains a highly basic region in the large hydrophilic, intracellular loop called XIP (Exchange inhibitory peptide; RRLLFYKYVYKRYRAGKQRG 20 aa), that inhibits Na-Ca+ exchange in cardiac sarcolemmal vesicles and in other cells. Little or no sequence identity is found between the NCX and the Ca-pump. However, XIP also inhibits the Ca pumps with more or less same efficiency as C28R2 peptide sequence (LRRGQILWFRGLNRIQTQIRVVKAFRSS, 28 aa) corresponding to the autoinhibitory domain of the Ca-pump.