Enzyme

Cocarboxylase tetrahydrate is a coenzyme form of vitamin B1; cofactor for enzymes involved in carbohydrate catabolism

GLUL Protein, Cricetulus griseus, Recombinant (His) is expressed in E. coli.

Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications.

MER tyrosine kinase (MERTK) encodes a surface receptor localized at the apical membrane of the retinal pigment epithelium.

AlkB Protein, Caulobacter vibrioides, Recombinant (His & Myc) is expressed in E.

Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover.

ALDH1A1 Protein, Mouse, Recombinant (His) is expressed in P. pastoris (Yeast) with N-6xHis. The accession number is P24549.

HK2 Protein, Mouse, Recombinant (His) is expressed in Baculovirus insect cells with His tag.

VIM-15 (β-Lactamase) is an enzyme product, specifically a metallo-beta-lactamase, which is sourced from certain resistant bacterial strains. This enzyme functions by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective. The primary mode of action involves the coordination of zinc ions at its active site, enabling the breakdown of a broad spectrum of beta-lactam antibiotics including penicillins, cephalosporins, and carbapenems. This enzymatic activity significantly contributes to antibiotic resistance, posing a challenge in the treatment of bacterial infections. Its prevalence is noted in healthcare settings, where multidrug-resistant organisms are a concern. VIM-15 is of particular interest in clinical microbiology research and antimicrobial resistance studies, where understanding its structure and function can aid in the development of new inhibitors, potentially restoring the efficacy of beta-lactam antibiotics against resistant strains. Its characterization and study are critical for developing strategies to combat antibiotic-resistant infections effectively.

Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins.

Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis.

Neutral Endopeptidase is an enzymatic product in liquid form, classified as food grade, which is derived from microbial fermentation or animal sources. Its primary mode of action involves the hydrolysis of peptide bonds within proteins, resulting in the breakdown of these macromolecules into smaller peptides and amino acids. This process is facilitated through the enzyme's specificity for neutral pH environments, where it effectively cleaves internal bonds within a protein chain. In the food industry, Neutral Endopeptidase is utilized for its ability to enhance the nutritional and functional properties of protein-rich products. It is commonly applied in the production of hydrolyzed protein products, improving solubility, digestibility, and bioavailability. Additionally, it plays a significant role in flavor development in foods such as cheese and soy sauce by releasing amino acids that contribute to taste and aroma. The enzyme's efficacy at neutral pH levels makes it particularly suitable for incorporation in a wide range of food matrices, facilitating its application across diverse food processing operations.

Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing.

Malate Dehydrogenase, Cytoplasmic (MDH1) is an enzyme which belongs to the MDH Type 2 sub-family of LDH/MDH superfamily.

Lipase 20 recombinantly expressed in P. pastoris comes in a spray-dried formulation. It has its pH optimum at 7-8. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 20 was shown to hydrolyze p-Nitrophenyl esters of butyrate (3 % activity compared to octanoate), octanoate (100 %), laurate (85 %), palmitate (52 %), stearate (29 %), arachidate (22 %) and behenate (8 %).

ATP citrate lyase, also known as Acly or Acl, is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues.

Thioglucosidase (thioglucoside glucohydrolase, Myrosinase, sinigrinase, sinigrase; EC 3.2.1.147) is an enzyme that cleaves thio-linked glucosides:a thioglucoside + H2O ⇌ a sugar + a thiol (the thiol formed is usually unstable and undergoes spontaneous re-arrangement into a isothiocyanate through a loss of a sulfate group)One unit will produce 1.0 μmole glucose per min from sinigrin (a thio-linked glucoside) at pH 6.0 and 25 °C.

NAT2 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.

Involved in the regulation of structural processes in differentiating and mature neuronal cells.