Recombinant Human POMGNT1

Instruction Manual!

Product name:	Recombinant Human POMGNT1
Source:	Human Cells
Purity:	Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:	Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl, 10% Glycerol, pH 8.5.
Applications:	Applications:SDS-PAGE; WB; ELISA; IP.
Storage:	Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:	100ug/50ug/200ug/1mg/1g

Source	Human Cells
Description	Recombinant Human POMGNT1 is produced by our Mammalian expression system and the target gene encoding Leu59-Thr660 is expressed with a 6His tag at the C-terminus.
Names	Protein O-Linked-Mannose Beta-1,2-N-Acetylglucosaminyltransferase 1, POMGnT1, UDP-GlcNAc:Alpha-D-Mannoside Beta-1,2-N-Acetylglucosaminyltransferase I.2, GnT I.2, POMGNT1, MGAT1.2
Accession #	Q8WZA1
Formulation	Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 150mM NaCl, 10% Glycerol, pH 8.5.
Shipping	The product is shipped on dry ice/ice packs.
Storage	Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.
Purity	Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin	Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence	LDTRRAISEANEDPEPEQDYDEALGRLEPPRRRGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDE AREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDT AKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAVEAE CHWADTELNRRRRRFCSKVEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRM LRSLLSAQGVSPQMITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLF PEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPG LGWVLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGYFH EAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAF IRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLVVGVPASPYSVKKPPSVTPIF LEPPPKEEGAPGAPEQTVDHHHHHH
Background	Protein O-Linked-Mannose β-1 2-N-Acetylglucosaminyltransferase 1 (POMGNT1) belongs to the Glycosyltransferase 13 family. Amino acid residues between 299-311 are important for both protein expression and enzymatic activity. The minimal catalytic domain is located between positions 299-651. It is suggested that the stem domain of the soluble form is unnecessary for activity, but that some amino acids play a crucial role in the membrane-bound form. Defects in POMGNT1 are the cause of muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies type A3 (MDDGA3).