NAD Synthetase protein (His tag)
Origin: Mycobacterium tuberculosis
Host: Escherichia coli (E. coli)
Recombinant
>98 % (SDS-PAGE)
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- Target
- NAD Synthetase
- Protein Type
- Recombinant
- Origin
- Mycobacterium tuberculosis
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- His tag
- Purpose
- NAD Synthetase (M. tuberculosis) (rec.) (His)
- Specificity
- NAD synthetase (Mycobacterium tuberculosis) (with mutation S444A) is fused at the N-terminus to a His-tag.
- Characteristics
- NAD synthetase (Mycobacterium tuberculosis) (with mutation S444A) is fused at the N-terminus to a His-tag.
- Purity
- >98 % (SDS-PAGE)
- Biological Activity Comment
- ~0.1 U/mg protein. (Ammonium or glutamine as nitrogen source). One unit is defined as the amount of enzyme that synthesizes 1μmol NAD per min.
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- Restrictions
- For Research Use only
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- Format
- Liquid
- Reconstitution
- 0.5 mg/mL (Lot specific)
- Concentration
- Lot specific
- Buffer
- In 20 mM TRIS-HCl, pH 7.8.
- Handling Advice
- After opening, prepare aliquots and store at -80 °C.Avoid freeze/thaw cycles.
- Storage
- -20 °C,-80 °C
- Storage Comment
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Short Term Storage: -20°C
Long Term Storage: -80°C
Use & Stability: Stable for at least 6 months after receipt when stored at -80°C.
- Expiry Date
- 6 months
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- Target
- NAD Synthetase
- Background
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NADE, Glutamine-dependent NAD(+) Synthetase, EC 6.3.5.1
NAD synthetase is an essential enzyme involved in both the de novo biosynthesis and salvage of NAD+, catalyzing the final step of both pathways. Since NAD has a vital role in cell metabolism, the enzyme represents a valid target for the development of new antimycobacterial agents. It can use both glutamine or ammonia as a nitrogen source. Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate
- Molecular Weight
- ~75.0kDa
- UniProt
- P0A5L6
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