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AdipoGen Life Sciences
NAD Synthetase (M. tuberculosis) (rec.) (His)
As low as
480
CHF
CHF 480.00
In stock
Only %1 left
AG-40T-0108-C05050 µgCHF 480.00
Specifications / Handling
| Product Details | |
|---|---|
| Synonyms | NADE; Glutamine-dependent NAD(+) Synthetase; EC 6.3.5.1 |
| Product Type | Protein |
| Properties | |
| Source/Host | E. coli |
| Sequence | NAD synthetase (Mycobacterium tuberculosis) (with mutation S444A) is fused at the N-terminus to a His-tag. |
| Biological Activity | ~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. |
| MW | ~75.0kDa |
| Purity | ≥98% (SDS-PAGE) |
| Endotoxin Content | N/A |
| Concentration | 0.5mg/ml (Lot specific) |
| Formulation | Liquid. In 20mM TRIS-HCl, pH 7.8. |
| Other Product Data | UniProt link P0A5L6: NAD Synthetase (M. tuberculosis) |
| Shipping and Handling | |
| Shipping | DRY ICE |
| Short Term Storage | -20°C |
| Long Term Storage | -80°C |
| Handling Advice |
After opening, prepare aliquots and store at -80°C. Avoid freeze/thaw cycles. |
| Use/Stability | Stable for at least 6 months after receipt when stored at -80°C. |
| Documents | |
| MSDS |
 Download PDF |
| Product Specification Sheet | |
| Datasheet |
Download PDF |
Scientific Background Information
Product Description
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
Catalytic activity: ATP + deamido-NAD+ + L-glutamine + H2O = AMP + diphosphate + NAD+ + L-glutamate
Product-specific References
- Heterologous expression, purification, and enzymatic activity of Mycobacterium tuberculosis NAD(+) synthetase: M. Bellinzoni, et al.; Protein Expr. Purif. 25, 547 (2002)