Recombinant Human Nicotinamide Mononucleotide Adenylyltransferase 1 (NMNAT1) Protein (GST)

Name: Recombinant Human Nicotinamide Mononucleotide Adenylyltransferase 1 (NMNAT1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08718P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Nicotinamide Mononucleotide Adenylyltransferase 1 (NMNAT1) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9HAN9
Target Symbol	NMNAT1
Synonyms	EC 2.7.7.1; LCA9; Leber's congenital amaurosis 9; NaMN adenylyltransferase 1; nicotinamide nucleotide adenylyltransferase 1; Nicotinamide-nucleotide adenylyltransferase 1; Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1; nicotinate nucleotide adenylyltransferase 1; Nicotinate-nucleotide adenylyltransferase 1; NMN adenylyltransferase 1; NMN/NaMN adenylyltransferase 1; NMNA1_HUMAN; Nmnat 1; Nmnat1; OTTHUMP00000001731; OTTHUMP00000001732; OTTHUMP00000035892; PNAT 1; PNAT1; pyridine nucleotide adenylyltransferase 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT
Expression Range	1-279aa
Protein Length	Full Length
Mol. Weight	58.9kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less effectively. Involved in the synthesis of ATP in the nucleus, together with PARP1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+). Protects against axonal degeneration following mechanical or toxic insults.
Subcellular Location	Nucleus.
Protein Families	Eukaryotic NMN adenylyltransferase family
Database References	HGNC: 17877 OMIM: 608553 KEGG: hsa:64802 STRING: 9606.ENSP00000366410 UniGene: PMID: 29184169 Results associate a distinct retinal dystrophy phenotype with nicotinamide-nucleotide adenylyltransferase 1 protein (NMNAT1) mutation and suggest coiled-coil domain containing 66 (CCDC66) should not be considered a retinal dystrophy candidate gene. PMID: 28369829 Hidden Genetic Variation in LCA9-Associated Congenital Blindness Explained by 5'UTR Mutations and Copy-Number Variations of NMNAT1. PMID: 26316326 We confirmed a diagnosis of NMNAT1-associated Leber congenital amaurosis in two siblings through identification of the mutation (c.25G>A [p. Val9Met]) in a homozygous state. PMID: 26464178 NMNAT1, which encodes the nicotinamide mononucleotide adenylyltransferase 1, has been recently identified to be one of the LCA-causing genes. Our results expanded the spectrum of mutations in NMNAT1 PMID: 25988908 To study how mutations affect NMNAT1 function and ultimately lead to a retinal degeneration phenotype, we performed detailed analysis of Leber congenital amaurosis 9-associated NMNAT1 mutants. PMID: 26018082 theNMNAT1 p.Glu257Lys variant is a hypomorphic variant that almost without exception causes leber congenital amaurosis (LCA) in combination with more severe NMNAT1 variants. PMID: 24830548 The aim of this study was to determine the occurrence and frequency of NMNAT1 mutations and associated phenotypes in different types of inherited retinal dystrophies. PMID: 24940029 NMNAT1 deletion in tumors may contribute to transformation by increasing ribosomal RNA synthesis. PMID: 23737528 mutations in nicotinamide nucleotide adenylyltransferase 1(NMNAT1) cause Leber congenital amaurosis PMID: 23351689 Mutations in NMNAT1 cause Leber congenital amaurosis with early-onset severe macular and optic atrophy. PMID: 22842229 A new disease mechanism underlying Leber congential amaurosis and the first link between endogenous NMNAT1 dysfunction and a human nervous system disorder. PMID: 22842230 Our studies link the enzymatic activities of NMNAT-1 and PARP-1 to the regulation of a set of common target genes through functional interactions at target gene promoters. PMID: 22334709 Study investigated the importance of NMNAT2's central domain, which are postulated to be dispensable for catalytic activity, instead representing an isozyme-specific control domain within the overall architecture of NMNAT2. PMID: 20954240 nicotinamide mononucleotide adenylyltransferase (Nmnat) protein transduction into transected axons blocks axonal degeneration PMID: 21071441 Neuronal expression of exogenous Nmnat1 protein localized to the cytosol is essential and sufficient to delay Wallerian degeneration; cytosolic Nmnat1 showed greatly enhanced axon protection compared with native (nuclear) Nmnat1. PMID: 19458223 Axonal targeting of transgenic NMNAT activity is both necessary and sufficient to delay Wallerian degeneration; promoting axonal and synaptic delivery greatly enhances NMNAT1 effectiveness. PMID: 20926655 Red blood cells represent the first human cell type with a remarkable predominance of NMNAT3 over NMNAT1; NMNAT2 is absent. PMID: 20457531 analysis of isoform-specific targeting and interaction domains in human nicotinamide mononucleotide adenylyltransferases PMID: 20388704 By using a combination of single isomorphous replacement and density modification techniques, the human NMNAT structure was solved by x-ray crystallography to a 2.5-A resolution, revealing a hexamer that is composed of alpha/beta-topology subunits PMID: 11751893 structure determination and role in activating tiazofurin PMID: 11788603 Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN. PMID: 11959140 structural characterization of this human cytosolic enzyme and implicatons in NAD biosyntheesis PMID: 12574164 NMNAT1 is a nuclear protein, whereas NMNAT2 and -3 are localized to the Golgi complex and the mitochondria PMID: 16118205 depending on its state of phosphorylation, NMNAT-1 binds to activated, automodifying PARP-1 and thereby amplifies poly(ADP-ribosyl)ation PMID: 17360427 ATP binds before NMN with nuclear isozyme NMNAT1. NMNH conversion to NADH by NMNAT1 and NMNAT3 occurs at similar rates, conversion by NMNAT2 is much slower. PMID: 17402747 Nicotinamide mononucleotide adenylyl transferase 1 (Nmnat1) is important for axonal protection, since mutants with reduced enzymatic activity lack axon protective activity. PMID: 19403820

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.