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Enzymes can be classified systematically according to the difference between reaction and substrate specificity, and the mechanism of action. Oxidoreductases (EC 1.x.x.x) are the first enzyme class in the Enzyme Commission Nomenclature. Oxidoreductases are a large group of enzymes that catalyze the transfer of electrons from one molecule (the oxidant, the hydrogen or the electron donor) to another molecule (the reductant, the hydrogen or electron acceptor). In other words, oxidoreductases catalyze oxidoreduction reactions that occur within the cell, includes oxidase, oxygenase, peroxidase, dehydrogenase, and others. However, it often needs cofactors such as nicotinamide adenine dinucleotides (e.g., NAD+/NADH) and flavines (e.g., FAD/FADH2) in the reactions. Oxidoreductases are a fundamental class of enzymes responsible for the catalysis of oxidation-reduction reactions, crucial in most bioenergetic metabolic pathways.
The G6PD protein is a rate-limiting enzyme in the oxidative pentose phosphate pathway located in the cytosol, which is crucial for the catabolism of carbohydrates in glycolysis. The primary function of G6PD is to provide reducing power in the form of NADPH and generate pentose phosphates, helping the cell resist oxidative stress and regulate metabolic rates. Additionally, the activity of G6PD is associated with cancer progression. The G6PD protein (Human, HEK293, His) is a recombinant G6PD protein expressed in HEK293 cells, with a C-terminal His tag, and consists of 514 amino acids (A2-L515) .
The IDH1 protein catalyzes the oxidative decarboxylation of isocitrate to generate 2-oxoglutarate, which is utilized by enzymes such as phytoacyl-CoA dioxygenase. IDH1 Protein, Human (HEK293, His, Solution) is the recombinant human-derived IDH1 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of IDH1 Protein, Human (HEK293, His, Solution) is 414 a.a., with molecular weight of ~48 kDa.
Peroxiredoxin-2 (PRDX2) is a thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides, which is essential for cellular protection against oxidative stress. It detoxifies peroxide, senses hydrogen peroxide-mediated signaling events, and may participate in signaling cascades initiated by growth factors and tumor necrosis factor-alpha. Peroxiredoxin-2/PRDX2 Protein, Human (sf9, His) is the recombinant human-derived Peroxiredoxin-2/PRDX2 protein, expressed by Sf9 insect cells , with N-His labeled tag. The total length of Peroxiredoxin-2/PRDX2 Protein, Human (sf9, His) is 198 a.a., with molecular weight of ~27 kDa.
Lysyl oxidase homolog 2; Lysyl oxidase-related protein WS9-14; LOXL2
Human
HEK293
LOXL2 protein mediates post-translational oxidative deamination of lysine residues, leading to the formation of allysine. It specifically deaminates H3K4me3, inhibits TFIID-dependent transcription, represses E-cadherin, activates the IRE1-XBP1 pathway, and promotes cross-linking of extracellular matrix proteins. LOXL2 is involved in EMT, tumor progression, angiogenesis regulation, and chondrocyte differentiation. LOXL2 Protein, Human (HEK293, His) is the recombinant human-derived LOXL2 protein, expressed by HEK293 , with C-His labeled tag.
Lysyl oxidase homolog 2; Lysyl oxidase-related protein WS9-14; LOXL2
Human
CHO
LOXL2 protein mediates post-translational oxidative deamination of lysine residues, leading to the formation of allysine. It specifically deaminates H3K4me3, inhibits TFIID-dependent transcription, represses E-cadherin, activates the IRE1-XBP1 pathway, and promotes cross-linking of extracellular matrix proteins. LOXL2 is involved in EMT, tumor progression, angiogenesis regulation, and chondrocyte differentiation. LOXL2 Protein, Human (CHO, His) is the recombinant human-derived LOXL2 protein, expressed by CHO , with C-His labeled tag.
Catalase Protein, Human is an approximately 60.0 kDa human catalase protein expressed in E.coli. Catalase is a key enzyme in metabolism of H2O2 and reactive nitrogen species, and its expression and localization is markedly altered in tumors.
COX-2 protein is involved in the alternative pathway of prostaglandin biosynthesis. COX-2 Protein, Human (sf9, His) is the recombinant human-derived COX-2 protein, expressed by Sf9 insect cells , with C-10*His labeled tag.
15-Lipoxygenase 2 (15-LOX2) is a non-heme iron-containing dioxygenase crucial for peroxidation of polyunsaturated fatty acids (PUFAs). It exhibits peroxidase activity on arachidonate and linoleate, producing bioactive lipid mediators. Oxygenating arachidonyl derivatives, it generates 15-HETE-G, a peroxisome proliferator-activated receptor alpha agonist. 15-LOX2 class-switches pro-inflammatory mediators, participates in DHA oxidations to produce specialized pro-resolving mediators, and may influence cell cycle progression, proliferation, cytokine secretion, and macrophage differentiation. Importantly, it shows substrate specificity by not converting arachidonic acid to (15S)-HPETE. 15 Lipoxygenase 2 Protein, Human (sf9) is the recombinant human-derived 15 Lipoxygenase 2 protein, expressed by Sf9 insect cells , with tag free. and with residual Gly-Pro in N-terminal (not related to functional changes) mutation. The total length of 15 Lipoxygenase 2 Protein, Human (sf9) is 676 a.a., with molecular weight of 62-66 kDa.
rHuMalate dehydrogenase mitochondrial/MDH2, His ; Malate dehydrogenase; mitochondrial; MDH2
Human
HEK293
MDH2 is a key enzyme that undergoes acetylation, leading to an increase in its enzymatic activity. This post-translational modification acts as a regulatory mechanism for MDH2, potentially affecting its function and playing a role in the regulation of cellular metabolic processes. MDH2 Protein, Human (HEK293, His) is the recombinant human-derived MDH2 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MDH2 Protein, Human (HEK293, His) is 314 a.a., with molecular weight of ~34.0 kDa.
HO-1 Protein, an enzyme, plays a critical role in cellular defense against oxidative stress and inflammation. Dysregulation of HO-1 Protein has been implicated in several diseases, including cardiovascular disorders and neuroinflammatory conditions. Targeting HO-1 Protein may offer potential therapeutic interventions by enhancing antioxidant defenses, reducing inflammation, and potentially treating these diseases. HO-1 Protein, Human is the recombinant human-derived HO-1 protein, expressed by E. coli , with tag free. The total length of HO-1 Protein, Human is 261 a.a., with molecular weight of ~30.0 kDa.
SOD1 Protein, an enzyme crucial for cellular defense, operates as a superoxide dismutase, neutralizing radicals to safeguard cells from oxidative stress. Its enzymatic activity underscores the importance of SOD1 in maintaining cellular homeostasis and protecting biological systems from the harmful effects of reactive oxygen species accumulation. SOD1 Protein, Human (His) is the recombinant human-derived SOD1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of SOD1 Protein, Human (His) is 154 a.a., with molecular weight of ~20.0 kDa.
SOD2/Mn-SOD protein is a key enzyme in cellular defense that neutralizes superoxide anion radicals and protects cells from oxidative stress. SOD2, as a manganese-containing superoxide dismutase, plays a key role in breaking down these free radicals and is essential for maintaining cellular homeostasis and protecting biological systems from potential damage caused by the accumulation of reactive oxygen species. SOD2/Mn-SOD Protein, Human (HEK293, His) is the recombinant human-derived SOD2/Mn-SOD protein, expressed by HEK293 , with C-6*His labeled tag. The total length of SOD2/Mn-SOD Protein, Human (HEK293, His) is 198 a.a., with molecular weight of ~25.0 kDa.
As a cell adhesion molecule, AOC3 protein plays a key role in lymphocyte extravasation and recycling by promoting the binding of lymphocytes to peripheral lymph node vascular endothelial cells, independent of L-selectin. In addition to its role in cell adhesion, AOC3 exhibits semicarbazide-sensitive monoamine oxidase activity, contributing to its enzymatic function. AOC3 Protein, Human (HEK293, His) is the recombinant human-derived AOC3 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of AOC3 Protein, Human (HEK293, His) is 736 a.a., with molecular weight of ~95 kDa.
rHu5-demethoxyubiquinone hydroxylase, mitochondrial/COQ7, His; Ubiquinone Biosynthesis Protein COQ7 Homolog; Coenzyme Q Biosynthesis Protein 7 Homolog; Timing Protein Clk-1 Homolog; COQ7
Human
HEK293
The COQ7 protein is a key enzyme in lipid A biosynthesis and catalyzes a key hydrolysis step involving UDP-3-O-myristoyl-N-acetylglucosamine. This activity leads to the formation of UDP-3-O-myristoylglucosamine and acetate, which is a decisive point in lipid A synthesis. COQ7 Protein, Human (HEK293, His) is the recombinant human-derived COQ7 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of COQ7 Protein, Human (HEK293, His) is 181 a.a., with molecular weight of 19-22 kDa.
LDHA protein catalyzes the stereospecific interconversion of pyruvate and lactate, concomitantly exchanging NADH and NAD(+). LDHA Protein, Human (His) is the recombinant human-derived LDHA protein, expressed by E. coli , with N-6*His labeled tag.
LDHA protein catalyzes the simultaneous and stereospecific interconversion of pyruvate and lactate, accompanied by the reciprocal interconversion of NADH and NAD(+).LDHA Protein, Mouse (HEK293, His) is the recombinant mouse-derived LDHA protein, expressed by HEK293 , with C-6*His labeled tag.
rHuL-lactate dehydrogenase B chain/LDH-B, His; L-lactate Dehydrogenase B Chain; LDH-B; LDH Heart Subunit; LDH-H; Renal Carcinoma Antigen NY-REN-46; LDHB
Human
E. coli
The LDHB protein, also known as lactate dehydrogenase B, is an enzyme that plays a crucial role in cellular energy metabolism. References indicate that the LDHB protein effectively catalyzes the simultaneous, stereospecific interconversion of pyruvate and lactate. LDHB Protein, Human (His) is the recombinant human-derived LDHB protein, expressed by E. coli , with N-6*His labeled tag. The total length of LDHB Protein, Human (His) is 334 a.a., with molecular weight of ~37.0 kDa.
GPD1 protein, a glycerol-3-phosphate dehydrogenase, crucially converts glycerol-3-phosphate to dihydroxyacetone phosphate, a key step in glycolysis and gluconeogenesis. Its enzymatic activity regulates cellular energy metabolism and glycerolipid biosynthesis, essential for maintaining cellular homeostasis and energy production. GPD1's role makes it a key player in metabolic processes with implications for various physiological functions. GPD1 Protein, Human (HEK293, His) is the recombinant human-derived GPD1 protein, expressed by HEK293 , with C-6*His labeled tag.
The PRDX5 protein (or Peroxiredoxin-5) plays a critical role as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. This enzyme activity is essential for cells to defend against oxidative stress and detoxify peroxides. PRDX5/Peroxiredoxin-5 Protein, Human (HEK293, His) is the recombinant human-derived PRDX5/Peroxiredoxin-5 protein, expressed by HEK293 , with N-6*His labeled tag.
Ribonucleoside-Diphosphate Reductase Subunit M2; Ribonucleotide Reductase Small Chain; Ribonucleotide Reductase Small Subunit; RRM2; RR2
Human
HEK293
RRM2 Protein, pivotal in DNA synthesis, catalyzes deoxyribonucleotide biosynthesis from ribonucleotide precursors, ensuring vital building blocks for DNA replication. Beyond nucleotide biosynthesis, RRM2 inhibits Wnt signaling, indicating involvement in regulating this crucial cellular pathway. RRM2 Protein, Human (HEK293, His) is the recombinant human-derived RRM2 protein, expressed by HEK293 , with C-6*His labeled tag.
