| Cat# | NATE-1150 |
| Abbr | SAHase, Recombinant |
| Alias | SAHase |
| Description | Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine. |
| Appearance | White powder, lyophilized |
| Product Overview | S-adenosyl-L-homocysteine hydrolase (SAHH, EC 3.3.1.1) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. SAHH is a ubiquitous enzyme which binds and requires NAD+ as a cofactor. AdoHcyase is a highly conserved protein of about 430 to 470 amino acids. The family contains a glycine-rich region in the central part of AdoHcyase; aregion thought to be involved in NAD-binding. This protein may use themorpheein model of allosteric regulation. |
| Form | Freeze dried powder |
| Enzyme Commission Number | EC 3.3.1.1 |
| Activity | 140U/mg |
| Molecular Weight | About 44kDa (SDS-PAGE detection) |
| Purity | >90% (SDS-PAGE test) |
| Isoelectric point | 6.15 |
| pH Stability | 6.0-8.0 |
| Unit Definition | One unit will catalyze 1.0 μmole of S-adenosyl-L-homocysteine to adenosine and Hcy per min at pH 7.4 at 37°C. |
| Storage | Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. |
| Buffer | Tris buffer, pH8.0 |
| Synonyms | Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1 |
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