|Calculated MW||36.6 kDa (327 aa, 1-307 aa + His Tag)|
|Other Names||Nicotinamide mononucleotide Adenylyltransferase 2, C1orf15, PNAT2|
|Results||Specific activity: > 500 pmol/min/ µg|
|Sequence||MGSSHHHHHH SSGLVPRGSH MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP SMTPVIGQPQ NETPQPIYQN SNVATKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ LYINASG|
|Storage||-20°C; 0.25 mg/ml solution 20 mM Tris-HCl buffer (pH 8.0), 20% glycerol, 150 mM NaCl and 1 mM DTT.|
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Provided below are standard protocols that you may find useful for product applications.
NMNAT2 belongs to the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family, members of which catalyze an essential step in NAD (NADP) biosynthetic pathway. Unlike the other human family member, which is localized to the nucleus, and is ubiquitously expressed; this enzyme is cytoplasmic, and is predominantly expressed in the brain. Two transcript variants encoding different isoforms have been found for this gene. Recombinant human NMNAT2 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques.
Sood R.,et al.Genomics 73:211-222(2001).
Seki N.,et al.DNA Res. 4:345-349(1997).
Gregory S.G.,et al.Nature 441:315-321(2006).
Raffaelli N.,et al.Biochem. Biophys. Res. Commun. 297:835-840(2002).
Yalowitz J.A.,et al.Biochem. J. 377:317-326(2004).
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