protein

APT-1/LYPLA1 Protein, Human (His)

HY-P7539

10 μg;50 μg

125;350 USD

APT-1/LYPLA1 Protein, Human (His)

proteins

E. coli

10 μg;50 μg

125;350 USD

The APT-1/LYPLA1 protein is an acylprotein thioesterase that hydrolyzes fatty acids from S-acylated cysteine residues in proteins, including G alpha proteins and HRAS. It also depalmitoylates KCNMA1 and potentially ADRB2 while acting as a lysophospholipase, hydrolyzing lysophosphatidylcholine (lyso-PC) and other lysophospholipids (lyso-PE, lyso-PI, lyso-PS). APT-1/LYPLA1 Protein, Human (His) is the recombinant human-derived APT-1/LYPLA1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of APT-1/LYPLA1 Protein, Human (His) is 230 a.a., with molecular weight of ~25.0 kDa.

Human

APT-1/LYPLA1 protein functions as an acyl-protein thioesterase, catalyzing the hydrolysis of fatty acids from S-acylated cysteine residues within proteins, including trimeric G alpha proteins and HRAS. Additionally, it exhibits depalmitoylating activity towards KCNMA1 and potentially ADRB2. Acting as a lysophospholipase, APT-1/LYPLA1 hydrolyzes lysophosphatidylcholine (lyso-PC) and other lysophospholipids such as lyso-PE, lyso-PI, and lyso-PS, with a higher affinity for thioesterase activity. This protein significantly contributes to blood coagulation by recognizing and cleaving plasma phospholipids, generating lysophospholipids that serve as substrates for ENPP2, ultimately producing lysophosphatidic acid (LPA).

rHuAPT-1, His; LYPLA1; APT-1

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

Supplied as a 0.2 μm filter solution of 20 mM Tris-HCl, 100 mM NaCl, 1 Mm DTT, 10% Glycerol, pH 8.0.

Shipping with dry ice.