S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Antibody (Biotin)
169€ (20 µg)
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Name
S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Antibody (Biotin)
Category
Primary Antibodies
Provider
Abbexa
Reference
abx315580
Tested Applications
ELISA
Description
AMD1 Antibody (Biotin) is a Rabbit Polyclonal against AMD1 conjugated to Biotin.
Documentos del producto
Instrucciones
Data sheet
Especificaciones del producto
| Category | Primary Antibodies |
| Immunogen Target | Target: S-Adenosylmethionine Decarboxylase Proenzyme (AMD1) Immunogen: Recombinant Human S-adenosylmethionine decarboxylase proenzyme protein (167-264AA). |
| Host | Rabbit |
| Reactivity | Human |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Clonality | Polyclonal |
| Conjugation | Biotin |
| Isotype | IgG |
| Purity | > 95% |
| Purification | Purified by Protein G. |
| Size 1 | 20 µg |
| Size 2 | 50 µg |
| Size 3 | 100 µg |
| Size 4 | 200 µg |
| Size 5 | 1 mg |
| Form | Liquid |
| Tested Applications | ELISA |
| Buffer | 0.01 M PBS, pH 7.4, 0.03% Proclin-300 and 50% Glycerol. |
| Availability | Shipped within 5-10 working days. |
| Storage | Aliquot and store at -20°C. Avoid exposure to light. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P17707 |
| Gene ID | 262 |
| NCBI Accession | NP_001625.2, NM_001634.5 |
| OMIM | 180980 |
| Alias | AMD,SAMDC,ADOMETDC |
| Background | Antibody anti-AMD1 |
| Status | RUO |
| Note | THIS PRODUCT IS FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC, THERAPEUTIC OR COSMETIC PROCEDURES. NOT FOR HUMAN OR ANIMAL CONSUMPTION. |
Background
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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