S adenosylhomocysteine hydrolase (AHCY) (NM_000687) Human Recombinant Protein
Specifications
| Product Data | |
| Species | Human |
|---|---|
| Expression Host | HEK293 |
| Expression cDNA Clone or AA Sequence | |
| Tag | C-Myc/DDK |
| Predicted MW | 47.5 kDa |
| Concentration | >0.05 µg/µL as determined by microplate BCA method |
| Purity | > 80% as determined by SDS-PAGE and Coomassie blue staining |
| Buffer | 25 mM Tris-HCl, 100 mM glycine, pH 7.3, 10% glycerol |
| Preparation | Recombinant protein was captured through anti-DDK affinity column followed by conventional chromatography steps. |
| Note | For testing in cell culture applications, please filter before use. Note that you may experience some loss of protein during the filtration process. |
| Storage | Store at -80°C. |
| Stability | Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles. |
| Shipping | Dry Ice |
| Reference Data | |
| RefSeq | NP_000678 |
| Locus ID | 191 |
| UniProt ID | P23526 |
| Cytogenetics | 20q11.22 |
| RefSeq Size | 2211 |
| RefSeq ORF | 1296 |
| Synonyms | adoHcyase; SAHH |
| Summary | S-adenosylhomocysteine hydrolase belongs to the adenosylhomocysteinase family. It catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). Thus, it regulates the intracellular S-adenosylhomocysteine (SAH) concentration thought to be important for transmethylation reactions. Deficiency in this protein is one of the different causes of hypermethioninemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. provided by RefSeq, Jun 2009 |
| Protein Categories | Intracellular Proteins |
| Protein Families | Druggable Genome |
| Protein Pathways | Cysteine and methionine metabolism, Metabolic pathways, Selenoamino acid metabolism |
Reviews
Documents
| FAQs |
| SDS |
Resources
| Recombinant Protein Resources |
Citations
Rex, Kasmala, Bond et al
PLoS ONE (2016) 11 (6), e0157411 DOI: 10.1371/journal.pone.0157411
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