Monoglyceride lipase, human recombinant

MLL, HU-K5, HUK5, MAGL, MGL, Lysophospholipase homolog, Lysophospholipase-like

MLL, HU-K5, HUK5, MAGL, MGL, Lysophospholipase homolog, Lysophospholipase-like

MGLL is membrane-associated member of the serine hydrolase superfamily. MGLL functions together with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides. It is most abundantly expressed in skeletal muscle and adipose tissue. Recombinant human MGLL protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.

MGLL

11343

MGLL

Human

Q99685

Yes

E. Coli

N/A

N/A

Measured by its ability to hydrolyze 1.0 umole of p-nitrophenyl butyrate to pnitrophenol per minute at pH 7.5 at 25C.

Specific activity is > 170 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 umole of p-nitrophenyl butyrate to pnitrophenol per minute at pH 7.5 at 25C

>170 units/mg,

36.4 kDa

-20°C

Gel pack

1 year

0.5 mg/ml

Liquid

In 20 mM Tris-HCl Buffer (pH 8.0) containing 10% Glycerol

N/A

Centrifuge the vial prior to opening.

For Research Use Only! Not to be used in humans

Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.

Recombinants or rec. proteins

recombinants