protein

RKIP/PEBP1 Protein, Human

HY-P77179

2 μg;10 μg;50 μg

35;70;200 USD

RKIP/PEBP1 Protein, Human

proteins

E. coli

2 μg;10 μg;50 μg

35;70;200 USD

The RKIP/PEBP1 protein has diverse binding capabilities and can interact with ATP, opioids, and phosphatidylethanolamine. It acts as a serine protease inhibitor, effectively inhibiting thrombin, neuroproteases, and chymotrypsin. RKIP/PEBP1 Protein, Human is the recombinant human-derived RKIP/PEBP1 protein, expressed by E. coli , with tag free. The total length of RKIP/PEBP1 Protein, Human is 187 a.a., with molecular weight of ~21.1 KDa.

Human

The RKIP/PEBP1 protein exhibits versatile binding capabilities, interacting with ATP, opioids, and phosphatidylethanolamine, while displaying lower affinity for phosphatidylinositol and phosphatidylcholine. This protein serves as a serine protease inhibitor, effectively inhibiting thrombin, neuropsin, and chymotrypsin, albeit not trypsin, tissue-type plasminogen activator, and elastase. Notably, RKIP/PEBP1 plays a pivotal role in modulating the kinase activity of RAF1 by impeding its activation, dissociating the RAF1/MEK complex, and acting as a competitive inhibitor of MEK phosphorylation. Additionally, it is implicated in the function of presynaptic cholinergic neurons in the central nervous system, enhancing the production of choline acetyltransferase without affecting acetylcholinesterase. This regulatory function appears to be mediated by a specific receptor.

Phosphatidylethanolamine-binding protein 1; HCNPpp; Neuropolypeptide h3; HCNP; PBP; PEBP

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4, 10% Glycerol.

Room temperature in continental US; may vary elsewhere.