NMNAT2 Human

Nicotinamide Nucleotide Adenylyltransferase 2 Human Recombinant

Cat. No.

BT11421

Source

Escherichia Coli.

Synonyms

Nicotinamide Nucleotide Adenylyltransferase 2, C1orf15, Nicotinate-Nucleotide Adenylyltransferase 2, NaMN Adenylyltransferase 2, NMN Adenylyltransferase 2, PNAT2, KIAA0479, Chromosome 1 Open Reading Frame 15, Nicotinamide Mononucleotide Adenylyltransferase 2, Pyridine Nucleotide Adenylyltransferase 2, EC 2.7.7.1, EC 2.7.7.18.

Appearance

Sterile Filtered clear solution.

Purity

Greater than 85.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

NMNAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (1-307 a.a) and having a molecular mass of 36.6kDa.

NMNAT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

Nicotinamide Nucleotide Adenylyltransferase 2, also called NMNAT2, is part of the nicotinamide mononucleotide adenylyltransferase (NMNAT) enzyme family. These enzymes play a crucial role in the creation of NAD (NADP). Unlike its counterpart found in the nucleus and present throughout the body, NMNAT2 is primarily located in the cytoplasm and found mainly in the brain. There are two known forms of NMNAT2, each produced by different transcripts. NMNAT2 has been linked to diseases like tauopathy and systemic lupus erythematosus.

Description

Recombinant human NMNAT2, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 327 amino acids (specifically, amino acids 1 to 307) and has a molecular weight of 36.6 kDa. A 20 amino acid His-tag is fused to the N-terminus of NMNAT2. The protein is then purified using specialized chromatographic techniques.

Physical Appearance

A clear solution that has been sterilized by filtration.

Formulation

The NMNAT2 protein solution has a concentration of 0.25 mg/ml. It is prepared in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 20% glycerol, and 1 mM DTT.

Stability

For short-term storage (up to 2-4 weeks), the solution should be kept at 4°C. For longer storage, it should be frozen at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is recommended for extended storage. It's important to avoid repeatedly freezing and thawing the solution.

Purity

Determined by SDS-PAGE analysis, the purity is greater than 85%.

Biological Activity

The specific activity of the enzyme is measured as greater than 500 pmol of beta-NADH converted to beta-NAD per minute per microgram of protein. This measurement is conducted at a pH of 8.0 and a temperature of 37°C. One unit of enzyme activity is defined as the amount needed to convert 1.0 pmole of beta-NADH to beta-NAD every minute under these conditions.

Synonyms

Source

Escherichia Coli.

Amino Acid 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

Product Science Overview

Structure and Function

NMNAT2 catalyzes the conversion of nicotinamide mononucleotide (NMN) and ATP to NAD+ and pyrophosphate. This reaction is essential for maintaining cellular NAD+ levels, which are critical for energy metabolism, DNA repair, and cell signaling . Unlike NMNAT1, which is localized in the nucleus, NMNAT2 is predominantly found in the cytoplasm and is highly expressed in the brain.

Isoforms and Localization

NMNAT1: Widespread expression, primarily localized in the nucleus.
NMNAT2: Predominantly expressed in the brain, localized in the cytoplasm.
NMNAT3: Highest expression in the liver, heart, skeletal muscle, and erythrocytes, localized in the mitochondrion or cytoplasm .

Biological Significance

NMNAT2 is critical for neuronal health. It acts as an axon maintenance factor, delaying Wallerian degeneration, a process that leads to the loss of damaged axons. This enzyme’s role in maintaining NAD+ levels is vital for neuronal survival and function. Loss of NMNAT2 is associated with neurodegenerative conditions, highlighting its importance in neuroprotection.

Clinical Implications

While mutations in the NMNAT1 gene are known to cause Leber congenital amaurosis, a severe retinal dystrophy, mutations in NMNAT2 or NMNAT3 genes have not been linked to any specific human diseases. However, chronic inflammation due to obesity and other factors can reduce NMNAT and NAD+ levels in various tissues, potentially impacting overall health.

Research and Therapeutic Potential

Research into NMNAT2 has revealed its potential as a therapeutic target for neurodegenerative diseases. By boosting NAD+ levels, it may be possible to enhance neuronal survival and function, offering new avenues for treating conditions like Alzheimer’s disease and other forms of dementia.

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NMNAT2 Human

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