Enzimas en Proteínas Recombinantes

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Glutaminyl cyclase, also known as QPCT, can promote the N-terminal cyclization reaction of N-terminal pyroglutamate(pGlu).

SUCLA2 Protein, Human, Recombinant (His & Myc) is expressed in E. coli with N-10xHis, C-Myc. The accession number is Q9P2R7.

TrkA Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Muscle, skeletal receptor tyrosine-protein kinase, also known as Muscle-specific tyrosine-protein kinase receptor, Muscle-specific kinase receptor, and MUSK, is

Phospholipase D 040, concentrated (100 U/mg), spray-dried, recombinant, of prokaryotic origin, is an enzyme preparation designed for advanced biochemical applications. This enzyme is derived from a prokaryotic source through recombinant DNA technology, allowing for high purity and activity. Phospholipase D functions by catalyzing the hydrolysis of phospholipids to produce phosphatidic acid and free head groups, which is a crucial reaction in both lipid signaling and membrane dynamics. Its robust enzymatic activity and defined kinetic properties make it an essential tool for researchers studying cell signaling, membrane composition, and lipid metabolism. The spray-dried form ensures stability and ease of use in various experimental setups, from in vitro assays to more complex in vivo systems. Recognized for its significance in biochemical pathways, Phospholipase D 040 plays a critical role in elucidating mechanisms of cellular communication and function. Its applications extend to the development of novel therapeutic approaches targeting lipid-associated disorders and contribute to advancements in molecular biology and biochemistry research.

Carbonic Anhydrase 9 Protein, Human, Recombinant (hFc & Avi), Biotinylated is expressed in HEK293 mammalian cells with hFc and Avi tag.

D-Ribulose 1,5-diphosphate carboxylase, commonly known as RuBisCO, is an essential enzyme that catalyzes the first major step of carbon fixation, a process by which inorganic carbon from the atmosphere is converted into organic molecules. This enzyme is derived from spinach, a common model organism used in plant biology research due to its accessibility and well-characterized photosynthetic pathways. RuBisCO operates by catalyzing the reaction of carbon dioxide with ribulose-1,5-bisphosphate (RuBP) to form two molecules of 3-phosphoglycerate. This reaction constitutes a crucial part of the Calvin cycle, which takes place in the chloroplasts of plant cells. As the most abundant protein on Earth, RuBisCO plays a critical role in the conversion of carbon dioxide into organic compounds, ultimately supporting the food chain through its foundational role in photosynthesis. Given its pivotal role, RuBisCO is of great interest in studies involving photosynthetic efficiency, plant biochemistry, and strategies to enhance crop yield. Researchers often explore its structural properties, kinetics, and potential for genetic engineering to improve its catalytic efficiency to meet global food demands and address climate change challenges.

Protocatechuate 3,4-dioxygenase is a bacterial enzyme, which is sourced from Pseudomonas sp. This enzyme operates by catalyzing the cleavage of aromatic rings in protocatechuate, a derivative of catechol. Its mode of action involves the incorporation of oxygen into protocatechuate, resulting in the formation of beta-carboxy-cis,cis-muconate. This reaction is crucial for the microbial degradation of aromatic compounds, thereby playing a significant role in the biodegradation pathways of lignin-derived aromatic pollutants. Widely studied for its significance in environmental bioremediation, protocatechuate 3,4-dioxygenase is key to breaking down complex organic materials in soil and water ecosystems. Its applications extend to industrial processes where the enzymatic transformation of aromatic compounds is required, such as in the synthesis of bio-based chemicals. Researchers also investigate its potential in metabolic engineering to enhance microbial strains for efficient degradation of environmental pollutants. Understanding and utilizing this enzyme can significantly contribute to advances in biotechnology and ecological sustainability.

The p38 mitogen-activated protein kinase (MAPK) pathway plays an important role in cellular responses to inflammatory stimuli and environmental stress.

ACYP1, also known as Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1 and

Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D-alanyl carrier protein (Dcp)

GUCY2C Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-6xHis-Avi tag.

Factor XI (FXI) is the zymogen of a plasma protease (FXIa) that contributes to hemostasis by activating factor IX (FIX).

Has pectate lyase activity.

VEGFR3/FLT4 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Alkaline phosphatase can be considered "our favorite enzyme" for reasons apparent to those who diagnose and treat metabolic bone diseases or who study skeletal

SMAD Family Member 1 (SMAD1) is a member of the dwarfin/SMAD family.

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin.

N/A.

Carbonic Anhydrase 1 Protein, Human, Recombinant (Active, His) is expressed in E. coli with C-6xHis. The accession number is P00915.

ABCB1 Protein, Human, Recombinant (His) is expressed in E. coli.

IL-1R1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Kallikrein-4, also known as Enamel matrix serine proteinase 1, Kallikrein-like protein 1, KLK-L1, Serine protease 17, KLK4, PRSS17, and EMSP1, is a secreted

Coagulation Factor II Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

RAF1 Protein, Human, Recombinant (His & SUMO) is expressed in E.

Ribonuclease T1 is an endonuclease enzyme, which is derived from the fungus Aspergillus oryzae. It specifically cleaves single-stranded RNA at the 3' end of guanosine residues, which involves hydrolyzing the phosphodiester bond to produce 3′-phosphomononucleotides and 5′-hydroxylated oligonucleotides. This enzyme’s high specificity and catalytic efficiency make it valuable for various applications. Ribonuclease T1 is widely used in molecular biology for RNA sequencing, structural studies, and RNA mapping. It facilitates the investigation of RNA secondary structures and has been instrumental in determining the primary structure of numerous RNAs. Its specificity for guanosine residues makes it an ideal tool for studying RNA sequences with a known or hypothesized abundance of guanine. In enzymology and structural studies, Ribonuclease T1 helps decipher the role of RNA in protein synthesis and cellular regulation. Additionally, it contributes to advancements in biotechnological applications where RNA processing and manipulation are critical. Such applications highlight the enzyme’s importance in both basic research and applied sciences.

Ricin Protein, Ricinus communis, Recombinant (His) is expressed in E.

Carboxypeptidase B1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

SDS Protein, Human, Recombinant (His & Myc) is expressed in E. coli.

MRAS Protein, Human, Recombinant (His & Myc) is expressed in E. coli with N-10xHis, C-Myc. The accession number is O14807.

Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan

ErbB4 Protein, Human, Rhesus, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag.

Hydrolyzes carbapenems, penicillins, cephalosporins and aztreonam with varying efficiency.

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.

BACE2, also known as beta secretase 2, belongs to the peptidase A1 family.

The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in

SMARCA4 Protein, Human, Recombinant (His) is expressed in E.

Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.

Kallikrein-2 (KLK2) is a secreted serine protease that belongs to the peptidase S1 family of Kallikrein subfamily.

Heat-Responsive Protein 12 (HRSP12) is an endoribonuclease that belongs to the Rut family.

Phosphomannomutase 1 (PMM1) blongs to the eukaryotic PMM family.

Iron-storage protein.

RAN Protein, Human, Recombinant (GST) is expressed in E.

Carbonic Anhydrase 12 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.

Acetyl-CoA carboxylase Protein, Candida albicans, Recombinant (His) is expressed in E.

Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily.

PAK1 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.

Sulfatase from Helix pomatia is a highly potent enzyme that is capable of hydrolyzing sulfated compounds and sulfate esters. It has been widely used in various applications such as glucosinolate analysis, genistein extraction preparation, and regiospecificity studies. With a concentration of ≥10,000 units per gram of solid, this sulfatase offers exceptional enzymatic activity for sulfatase assays. It effectively catalyzes the hydrolysis of sulfated substrates, including p-nitrocatechol sulfate, naphthyl sulfate and phenyl sulfates.The enzyme can be incubated with the desired sample to facilitate the release of sulfate groups from sulfated compounds. Sulfatase from Helix pomatia is a valuable tool for researchers and scientists working in diverse fields requiring efficient and reliable enzymatic hydrolysis capabilities. Additionally the enzyme has been found to have industrial applications, such as in the bioconversion of industrial chemicals, where it can be used as a catalyst.  One unit will hydrolyze 1.0 μmole of p-nitrocatechol sulfate per hour at pH 5.0 at 37 °C (30 min assay).