Specification
Description | Recombinant protein from the full-length sequence of Homo sapiens nicotinamide nucleotide adenylyltransferase 2 (NMNAT2), transcript variant 2 (NM_170706). |
Organism | Homo sapiens (Human) |
Expression Host | Human Cells |
Tag Info | His or DYKDDDDK. Please contact us if you need further information or require specific designed tag. |
Purity | Greater than 90% by SDS-PAGE gel |
Uniprot ID | Q9BZQ4 |
Entry Name | NMNA2_HUMAN |
Gene Names | NMNAT2 C1orf15 KIAA0479 |
Alternative Gene Names | C1orf15 KIAA0479 |
Alternative Protein Names | Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2 (NMN/NaMN adenylyltransferase 2) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 2) (NMN adenylyltransferase 2) (Nicotinate-nucleotide adenylyltransferase 2) (NaMN adenylyltransferase 2) |
Application | Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only! |
Buffer | Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives |
Endotoxin | Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg) |
Length | 307 |
Molecular Weight(Da) | 34439 |
Protein Sequence | (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.) MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG |
Background
Function | FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed:16118205, PubMed:17402747). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (PubMed:16118205, PubMed:17402747). Cannot use triazofurin monophosphate (TrMP) as substrate (PubMed:16118205, PubMed:17402747). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (PubMed:16118205, PubMed:17402747). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (PubMed:16118205, PubMed:17402747). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (PubMed:16118205, PubMed:17402747). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). {ECO:0000250|UniProtKB:Q8BNJ3, ECO:0000269|PubMed:16118205, ECO:0000269|PubMed:17402747}. |
Pathway | Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1. Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1. |
Protein Families | Eukaryotic NMN adenylyltransferase family |
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. {ECO:0000269|PubMed:12359228, ECO:0000269|PubMed:14516279, ECO:0000269|PubMed:16118205}. |
QC Data
Note | Please contact us for QC Data |
Product Image (Reference Only) | ![]() |