Recombinant Human NMNAT1/NMNAT Protein (His Tag) | PKSH031118

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SKU:
575-PKSH031118
€1,133.00
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Description

Recombinant Human NMNAT1/NMNAT Protein (His Tag) | PKSH031118 | Gentaur US, UK & Europe Disrtribition

Synonyms: LCA9;NMNAT;PNAT1

Active Protein: N/A

Activity: A DNA sequence encoding the human NMNAT1 (Q9HAN9)( Met 1-Thr279) was expressed with a C-terminal polyhistidine tag.

Protein Construction: A DNA sequence encoding the human NMNAT1 (Q9HAN9)( Met 1-Thr279) was expressed with a C-terminal polyhistidine tag.

Fusion Tag: C-His

Species: Human

Expressed Host: Baculovirus-Insect Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 85 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 33.3 kDa

Formulation: Lyophilized from sterile 20mM Tris, 500mM NaCl, 3mM DTT, 10% glycerol, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: NMNAT, also known as NMNAT1, is a member of the Nicotinamide-nucleotide adenylyltransferases. It is widely expressed with high levels in skeletal muscle, heart, liver and kidney. NMNAT appears to have the ability to protect against axonal degeneration following mechanical or toxic insults. The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation, histone deacetylation, and in some Ca(2+) signaling pathways. NMNAT enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD.

Research Area: Signal Transduction, Neuroscience, Cancer, epigenetics and nuclear signal, metabolism,

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