Enzyme

FKBP3 is a member of FK506-binding proteins (FKBPs).

Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress.

Involved in nuclear export of spliced and unspliced mRNA.

PIN1 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 18.2 kDa and the accession number is Q13526-1.

Putative inactive protein kinase which regulates signaling downstream of immune receptors including IL1R and Toll-like receptors.

CDK1 Protein, Human, Recombinant (GST) is expressed in Baculovirus insect cells with GST tag.

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the

N/A.

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Aconitase 1(ACO1) or IRP1 is one member of the aconitase family that contains a diverse group of iron-sulphur(Fe-S) isomerases and two types of iron regulatory

RAC1 Protein, Human, Recombinant (His) is expressed in yeast with C-6xHis tag.

UGT89C1 Protein, Arabidopsis thaliana, Recombinant (Yeast, His) is expressed in yeast with N-10xHis tag.

The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation.

PDE1C Protein, Rat, Recombinant (His) is expressed in E.

ACK1 (also known as ACK, TNK2, or activated Cdc42 kinase) is a structurally unique non-receptor tyrosine kinase that is expressed in diverse cell types.

COX4I1 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.

Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence.

Cyclophilin A Protein, Human, Recombinant (His) is expressed in E.

PELI1 Protein, Human, Recombinant (E. coli, His) is expressed in E. coli with N-6xHis. The accession number is Q96FA3.

MKK6 Protein, Human, Recombinant is expressed in Baculovirus insect cells. The predicted molecular weight is 37.6 kDa and the accession number is A8K3Y2.

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.

CDC42BPB is a member of the serine / threonine protein kinase family that contains a Cdc42 / Rsc-binding p21 binding domain similar to that of PAK kinase.

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair.

CRELD1 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag.

THOP1, also known as Thimet oligopeptidase 1, Thimet oligopeptidase, EC 3.4.24.15, or EP24.15, is a zinc(II) endopeptidase implicated in the processing of

Plasmodium falciparum lactate dehydrogenase (PfLDH) is a key enzyme for energy generation of malarial parasites and is considered to be a potential antimalarial

DNA helicase that stimulates viral DNA replication and recombination.

PTDSS1 Protein, Human, Recombinant (GST) is expressed in E. coli with N-GST. The accession number is P48651.

Cocarboxylase hydrochloride is a coenzyme derivative, which is primarily sourced from thiamine (vitamin B1). It plays a crucial role in biochemical processes by facilitating the enzymatic decarboxylation of alpha-keto acids within the cellular environment. This action is fundamental in energy production as it aids in the conversion of pyruvate to acetyl-CoA, subsequently entering the citric acid cycle. Cocarboxylase hydrochloride’s involvement in carbohydrate metabolism is especially vital for tissues with high metabolic rates, such as the heart and brain. In scientific applications, cocarboxylase hydrochloride is used to study metabolic pathways and to explore therapeutic interventions for metabolic disorders. Its role in augmenting thiamine activity is significant in research focused on conditions related to oxidative stress and mitochondrial dysfunction. Through its essential contribution to cellular energy production, cocarboxylase hydrochloride is also investigated for its potential in ameliorating symptoms associated with metabolic syndromes and in supporting cardiac function.

CDK7 Protein, Human, Recombinant (His) is expressed in Baculovirus.