DGAT1 Protein, Human (Cell-Free, His, Myc)

The DGAT1 protein catalyzes triacylglycerol synthesis using diacylglycerol and fatty acyl CoA as substrates. The DGAT1 protein has acyltransferase activity. DGAT1 Protein, Human (Cell-Free, His, Myc) is the recombinant human-derived DGAT1 protein, expressed by E. coli Cell-free , with N-10*His, C-Myc labeled tag. The total length of DGAT1 Protein, Human (Cell-Free, His, Myc) is 249 a.a., with molecular weight of 37.1 kDa.

DGAT1 protein functions as the catalyst for the terminal and exclusive step in triacylglycerol synthesis, employing diacylglycerol and fatty acyl CoA as substrates. Highly expressed in the epithelial cells of the small intestine, DGAT1 is crucial for the absorption of dietary fats. In the liver, it plays a role in esterifying exogenous fatty acids to glycerol, contributing to fat storage. Additionally, DGAT1 is present in female mammary glands, where it participates in the production of fat in the milk. The protein may be involved in very low-density lipoprotein (VLDL) assembly. Unlike DGAT2, DGAT1 is not essential for survival. In the skin, DGAT1 serves as the major acyl-CoA retinol acyltransferase (ARAT), maintaining retinoid homeostasis and preventing retinoid toxicity, thereby averting skin and hair disorders. Beyond its primary role, DGAT1 exhibits diverse acyltransferase activities, including acyl-CoA:monoacylglycerol acyltransferase (MGAT), wax monoester, and wax diester synthases. Furthermore, it demonstrates the capability to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG).

Human

E. coli Cell-free

N-10*His;C-Myc

O75907 (T240-A488)

8694

TVSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWMVPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREFYRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVSVPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLNYEAPAAEA

37.1 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.