Recombinant Human AMD1 protein, T7-tagged

• Cat.No.: AMD1-122H
• Product Overview: Recombinant human AMD1 fused with T7 Tag at N-terminal was expressed in E. coli.

Specification

• Source: E. coli
• Species: Human
• Tag: T7
• Form: 0.5 mg/ml, sterile-filtered, in 20 mM pH 8.0 Tris-HCl Buffer, with proprietary formulation of NaCl, KCl, EDTA, Sucrose and DTT.
• AA Sequence: MASMTGGQQMGRGEFGSEAAHFFEG TEKLLEVWFSRQQPDANQGSGDLRT IPRSEWDILLKDVQCSIISVTKTDK QEAYVLSESSMFVSKRRFILKTCGT TLLLKALVPLLKLARDYSGFDSIQS FFYSRKNFMKPSHQGYPHRNFQEEI EFLNAIFPNGAAYCMGRMNSDCWYL YTLDFPESRVISQPDQTLEILMSEL DPAVMDQFYMKDGVTAKDVTRESGI RDLIPGSVIDATMFNPCGYSMNGMK SDGTYWTIHITPEPEFSYVSFETNL SQTSYDDLIRKVVEVFKPGKFVTTL FVNQSSKCRTVLASPQKIEGFKRLD CQSAMFNDYNFVFTSFAKKQQQQQS
• Purity: >90% by SDS-PAGE
• Applications: 1. May be used for in vitro human polyamine biosynthesis regulation study.2. May be used as specific substrate protein for kinase and ubiquitin enzymes.3. May be used as cancer biomarker for diagnosis application development.
• Storage: Keep at -80 centigrade for long term storage. Product is stable at 4 centigrade for at least 30 days.

Gene Information

• Gene Name: AMD1 adenosylmethionine decarboxylase 1 [ Homo sapiens ]
• Official Symbol: AMD1
• Synonyms: AMD1; adenosylmethionine decarboxylase 1; S adenosylmethionine decarboxylase 1; S-adenosylmethionine decarboxylase proenzyme; SAMDC; S-adenosylmethionine decarboxylase 1; AMD; ADOMETDC; FLJ26964; DKFZp313L1234
• Gene ID: 262
• mRNA Refseq: NM_001033059
• Protein Refseq: NP_001028231
• MIM: 180980
• UniProt ID: P17707
• Chromosome Location: 6q21
• Pathway: Arginine and proline metabolism, organism-specific biosystem; Arginine and proline metabolism, conserved biosystem; Cysteine and methionine metabolism, organism-specific biosystem; Cysteine and methionine metabolism, conserved biosystem; Metabolic pathways, organism-specific biosystem; Metabolism, organism-specific biosystem; Metabolism of amino acids and derivatives, organism-specific biosystem
• Function: adenosylmethionine decarboxylase activity; adenosylmethionine decarboxylase activity; lyase activity

Reviews

05/06/2019

Compatibility with high-resolution imaging techniques for detailed analysis.

12/29/2018

Accurate measurement of protein turnover rates.

10/03/2017

Reduced non-specific binding in antibody-based assays.

Q&As

How does AMD1 interact with other enzymes or regulatory proteins involved in polyamine metabolism?

AMD1 interacts with other enzymes, such as ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase (SAMDC), in the polyamine biosynthetic pathway, forming a regulatory network.

How does AMD1 expression or activity correlate with disease states, such as cancer, and can it serve as a diagnostic or therapeutic target?

Alterations in AMD1 expression or activity have been observed in various diseases, including cancer, suggesting its potential as a diagnostic marker or therapeutic target for specific conditions.

How is AMD1 expression regulated in different tissues and under various physiological conditions?

AMD1 expression is regulated at the transcriptional level by various factors, including growth factors, hormones, and cellular stressors.

Can AMD1 be targeted pharmacologically to modulate polyamine metabolism and potentially treat diseases?

AMD1 represents a potential pharmacological target for modulating polyamine metabolism, and its inhibition has been explored as a therapeutic strategy in diseases such as cancer.

What is the impact of AMD1 deficiency or inhibition on cell proliferation, differentiation, and survival?

AMD1 deficiency or inhibition can lead to altered polyamine levels and impaired cellular processes, including reduced cell proliferation and compromised cell survival.

How does AMD1 contribute to polyamine biosynthesis and the regulation of intracellular polyamine levels?

AMD1 plays a key role in polyamine biosynthesis, regulating the levels of polyamines such as putrescine, spermidine, and spermine, which are involved in cell growth, proliferation, and differentiation.

What is the enzymatic activity of AMD1 and its role in cellular metabolism?

AMD1 is an enzyme that catalyzes the conversion of S-adenosylmethionine (SAM) to decarboxylated SAM, which is a crucial step in the biosynthesis of polyamines.

What are the structural features of AMD1 that contribute to its catalytic activity and substrate specificity?

The catalytic activity and substrate specificity of AMD1 are determined by its unique protein structure, including active site residues and cofactor binding sites.

What are the downstream signaling pathways or cellular processes influenced by AMD1 activity?

AMD1 activity influences downstream signaling pathways, including mTOR signaling, DNA methylation, and gene expression, which are involved in cell growth and proliferation.

What are the substrates of AMD1 and their functional implications in cellular processes?

The substrates of AMD1 include SAM, the primary methyl donor in cellular methylation reactions, and its decarboxylated product, which serves as a precursor for polyamine synthesis.