Human S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Protein
234€ (1 µg)
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name
Human S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx073971
tested applications
SDS-PAGE
Description
Adenosylmethionine Decarboxylase 1 is a recombinant enzyme.
Documents del producto
Instrucciones
Data sheet
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | S-Adenosylmethionine Decarboxylase ProProtein (AMD1) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 80% (SDS-PAGE) |
| Size 1 | 1 µg |
| Size 2 | 5 µg |
| Size 3 | 50 µg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Storage | Store at 4 °C if the entire vial will be used within 2-4 weeks. Store at -20 °C for long term storage. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P17707 |
| Alias | AMD,SAMDC,ADOMETDC |
| Background | Protein AMD1 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Adenosylmethionine Decarboxylase 1 (AMD1) is a key regulatory enzyme in polyamine biosynthesis, catalyzing the decarboxylation of S-adenosylmethionine (SAM) to form S-adenosylmethioninamine (dcSAM). This reaction provides the aminopropyl group for the synthesis of polyamines such as spermidine and spermine, which are essential for cell proliferation, differentiation, and DNA stabilization. AMD1 activity is tightly regulated at multiple levels, including transcription, translation, and post-translational modifications, to meet cellular demands for polyamine production. Dysregulation of AMD1 has been linked to various pathological conditions, including cancer, where increased polyamine synthesis supports tumor growth and survival. Inhibiting AMD1 is being explored as a potential therapeutic strategy for cancer treatment, targeting the overactive polyamine biosynthesis pathway to suppress cell proliferation. AMD1 also plays a role in cellular responses to oxidative stress and metabolic regulation, making it an important enzyme in maintaining cellular homeostasis.
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