AMD1
AMD1 (adenosylmethionine decarboxylase 1, also known as SAMDC) is a decarboxylase that supports biosynthesis of the polyamines spermidine and spermine. It is encoded by the human AMD1 gene and was previously named S-adenosylmethionine decarboxylase 1. Browse Assay Genie's current range of AMD1 research reagents below, or read on for the biology behind the target.
AMD1 is an important intermediate enzyme in polyamine biosynthesis and is essential for the production of the polyamines spermidine and spermine. Polyamines, which include spermine, spermidine and putrescine, are low-molecular-weight aliphatic amines that are essential for cellular proliferation and tumour promotion. As a decarboxylase (EC 4.1.1.50), AMD1 sits at a control point in this pathway, which is why it is studied in both cell growth and cancer biology.
Beyond its role in polyamine synthesis, AMD1 promotes the maintenance and self-renewal of embryonic stem cells by maintaining spermine levels. This links a core metabolic enzyme directly to stem cell state. The protein is made as a proenzyme, reflected in its UniProt name, S-adenosylmethionine decarboxylase proenzyme, and belongs to the eukaryotic AdoMetDC family.
The human AMD1 gene is a member of the HGNC decarboxylases gene group. Multiple alternatively spliced transcript variants have been identified, and pseudogenes of the gene are found on chromosomes 5, 6, 10, X and Y, which is worth bearing in mind when designing nucleic acid assays. The mouse and rat orthologs are both named Amd1, allowing comparative work in common model organisms. Researchers studying the AMD1 protein often use an AMD1 antibody or AMD1 ELISA kit-based approaches to follow expression alongside polyamine levels.
AMD1 is essential for biosynthesis of spermidine and spermine, making it a key enzyme for studying polyamine pathway regulation.
Polyamines are essential for cellular proliferation and tumour promotion, placing AMD1 within research on proliferative control and tumour growth.
AMD1 promotes maintenance and self-renewal of embryonic stem cells by maintaining spermine levels, linking metabolism to pluripotency.
The AMD1 gene produces multiple alternatively spliced transcript variants, and has pseudogenes on several chromosomes, relevant to transcript analysis.
AMD1 is essential for biosynthesis of the polyamines spermidine and spermine, acting as an important intermediate enzyme in the pathway. It also promotes maintenance and self-renewal of embryonic stem cells by maintaining spermine levels.
AMD1 is also known as SAMDC, and its previous HGNC name was S-adenosylmethionine decarboxylase 1. UniProt lists the protein as S-adenosylmethionine decarboxylase proenzyme. Multiple alternatively spliced transcript variants of the gene have been identified.
Yes. Mouse and rat both have an ortholog named Amd1. The human gene also has pseudogenes on chromosomes 5, 6, 10, X and Y. Check the datasheet of any product for its validated reactivity.
Other enzymes and metabolic targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P17707; product specifications from Assay Genie datasheets.