Recombinant Human NMNAT2 protein (ab171475)

Overview

  • Product name
    Recombinant Human NMNAT2 protein
  • Protein length
    Full length protein

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • 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
    • Molecular weight
      37 kDa including tags
    • Amino acids
      1 to 307
    • Tags
      His tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab171475 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

  • Purity
    > 85 % SDS-PAGE.
    ab171475 was purified using conventional chromatography techniques
  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.02% DTT, 0.32% Tris HCl, 20% Glycerol, 0.88% Sodium chloride

General Info

  • Alternative names
    • C1orf15
    • KIAA0479
    • MGC2756
    • NaMN adenylyltransferase 2
    • Nicotinamide mononucleotide adenylyltransferase 2
    • Nicotinamide nucleotide adenylyltransferase 2
    • Nicotinate-nucleotide adenylyltransferase 2
    • NMN adenylyltransferase 2
    • NMNA2_HUMAN
    • NMNAT 2
    • Nmnat2
    • PNAT 2
    • PNAT2
    • Pyridine nucleotide adenylyltransferase 2
    see all
  • Function
    Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannnot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+).
  • Tissue specificity
    Highly expressed in brain, in particular in cerebrum, cerebellum, occipital lobe, frontal lobe, temporal lobe and putamen. Also found in the heart, skeletal muscle, pancreas and islets of Langerhans.
  • Pathway
    Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
  • Sequence similarities
    Belongs to the eukaryotic NMN adenylyltransferase family.
  • Cellular localization
    Cytoplasm. Golgi apparatus.
  • Information by UniProt

Images

  • 15% SDS-PAGE analysis of 3µg ab171475.

References

ab171475 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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