Adenosylhomocysteinase Human Recombinant
Adenosylhomocysteinase Human Recombinant, Sf9
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
Adenosylhomocysteinase Mouse Recombinant
AHCY Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 456 amino acids (1-432 a.a) and having a molecular mass of 50.2kDa.
AHCY is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Sterile filtered colorless solution.
Adenosylhomocysteinase (AHCY), also known as S-adenosyl-L-homocysteine hydrolase (SAHH), is a protein-coding gene. It belongs to the adenosylhomocysteinase family and catalyzes the reversible hydrolysis of S-adenosylhomocysteine (SAH) to adenosine and L-homocysteine . This enzyme plays a crucial role in regulating intracellular SAH concentration, which is important for transmethylation reactions .
AHCY is one of the most conserved enzymes across various species, including bacteria, nematodes, yeast, plants, insects, and vertebrates . It is the only enzyme in mammals capable of catalyzing the reversible hydrolysis of SAH . AHCY is recruited to chromatin during replication and active transcription, correlating with increasing demands for DNA, RNA, and histone methylation . The enzyme is expressed in various tissues, with significant roles in metabolic processes .
AHCY acts within the one-carbon metabolic cycle, a universal metabolic process that enables the transfer of one-carbon units for biosynthetic processes, amino acid homeostasis, redox cellular control, and epigenetic regulation . It is essential for the breakdown of methionine and the regulation of methylation levels . AHCY deficiency is associated with hypermethioninemia, developmental delays, and potentially fatal outcomes .
AHCY catalyzes the hydrolysis of SAH to adenosine and L-homocysteine, thus regulating the methylation potential within cells . It interacts with various molecules and is involved in the regulation of DNA methylation throughout the day by interacting with circadian rhythm genes . AHCY’s activity is crucial for maintaining the balance of SAM (S-adenosylmethionine) and SAH, which is vital for numerous cellular processes .
The expression and activity of AHCY are regulated at multiple levels. Transcriptional regulation involves various factors that control the gene’s expression . Post-translational modifications, such as acetylation, can significantly impact AHCY’s catalytic activity . Additionally, AHCY’s subcellular localization is controlled to facilitate local transmethylation reactions .
AHCY has several applications in biomedical research. Antibodies targeting AHCY are used in various scientific applications, including Western Blot, ELISA, Immunohistochemistry, Immunocytochemistry, and Immunoprecipitation . AHCY’s role in regulating methylation makes it a potential target for therapeutic strategies aimed at diseases related to methylation imbalances .
AHCY plays a critical role throughout the life cycle. It is essential for embryonic development, as its deletion is embryonic lethal in many organisms . AHCY’s regulation of methylation and metabolic processes is crucial for maintaining cellular homeostasis from development to aging . Dysregulation of AHCY activity is associated with various diseases, including cancer .