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.