saccharomyces cerevisiae

SUC2 Protein, Saccharomyces cerevisiae, Recombinant (His) is expressed in yeast with His tag. The predicted molecular weight is 60 kDa and the accession number is P00724-1.

DNMT2, also known as tRNA (cytosine-5-)-methyltransferase, DNA methyltransferase homolog HsaIIP, and TRDMT1, is a member of the DNA methyltransferase family of enzymes. DNMT2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases. It contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide, and its structure is very similar to prokaryotic DNA methyltransferases. DNMT2 has close homologs in plants, insects and Schizosaccharomyces pombe, but no related sequence can be found in the genomes of Saccharomyces cerevisiae or Caenorhabditis elegans. While the biological function of DNMT2 is not yet known, the strong binding to DNA suggests that DNMT2 may mark specific sequences in the genome by binding to DNA through the specific target-recognizing motif. However, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.

Cdh1 is one of the substrate adaptor protein of the anaphase-promoting complex (APC) in the budding yeast Saccharomyces cerevisiae. Functioning as an activator of the APC C, Cdh1 regulates the activity and substrate specificity of this ubiquitin E3-ligase.

Ubiquitin-conjugating enzyme E2 A (also known as HHR6A or UBE2A), encoded by human DNA repair genes HHR6A, belongs to the ubiquitin-conjugating enzymes (E2 enzymes) family and is likely to be involved in postreplication repair and induced mutagenesis. UBE2A is described as a CDK2 substrate. It is the human homologue of the product of the Saccharomyces cerevisiae RAD6 UBC2 gene, a member of the family of ubiquitin-conjugating enzymes. In vivo, HHR6A phosphorylation peaks during the G2 M phase of cell cycle transition, with a concomitant increase in histone H2B ubiquitylation. Mutation of Ser120 to threonine or alanine abolished UBE2A activity, while mutation to aspartate to mimic phosphorylated serine increased UBE2A activity 3-fold. A mutation of UBE2A is considered as the cause of a novel X-linked mental retardation (XLMR) syndrome that affects three males in a two-generation family.

SUMO protease, also known as Ulp, is a highly specific enzyme that removes small ubiquitin-like modifier (SUMO) from recombinant SUMO fusion proteins. Unlike proteases such as enterokinase or TEV, which recognize linear amino acid sequences, SUMO protease recognizes the native tertiary structure of SUMO, allowing precise cleavage without leaving extra residues at the cleavage site. This recombinant SUMO protease is derived from Saccharomyces cerevisiae, expressed in E. coli, and purified to obtain high yields of active enzyme under animal-free conditions. It is well suited for applications in drug and vaccine development, protein manufacturing, and other research uses. A C-terminal 6×His tag is included to enable easy removal of the protease following cleavage via Ni²⁺ affinity purification.

Expression system: E. coli
Length: 32-265, Partial
Activity: Not Tested

Expression system: E. coli
Length: 1-181, Full Length
Activity: Not Tested