Enzimi nelle Proteine Ricombinanti
Gli enzimi accelerano le reazioni chimiche, agendo come catalizzatori biologici, agendo sui substrati e convertendoli in diverse molecole chiamate prodotti. Queste proteine sono indispensabili nei processi biochimici e nelle applicazioni industriali, facilitando le reazioni in condizioni miti con alta specificità ed efficienza. Da CymitQuimica, offriamo un'ampia selezione di enzimi di alta qualità per supportare le vostre applicazioni di ricerca, industriali e cliniche.
Trovati 3320 prodotti di " Enzimi nelle Proteine Ricombinanti"
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Tyrosinase, from mushroom
CAS:Purezza:≥ 1000U/mgColore e forma:Freeze-dried materialPeso molecolare:-Peroxidase, from horseradish, approx. 200 U/mg
CAS:Purezza:≥ 150U/mgColore e forma:Beige to light-brown, reddish brown or dark brown lyophilised powderPeso molecolare:-L-Asparaginase
CAS:Formula:C1377H2208N382O442S17Purezza:≥ 100U/mgColore e forma:White to almost white powderPeso molecolare:31731.9Tris(benzyltriazolylmethyl)amine
CAS:Tris(benzyltriazolylmethyl)amine (TBTA) is a tertiary amine. It complexes with, and stabilizes, copper(I) to accelerate azide-alkyne cycloadditions.Formula:C30H30N10Purezza:99.58% - 99.82%Colore e forma:SolidPeso molecolare:530.63ENPP3 Protein, Canine, Recombinant (His)
Ectonucleotide pyrophosphatase-phosphodiesterase 3 (ENPP3), a protein detected in the human uterus, has been found to play an important role in the developmentColore e forma:Lyophilized PowderPeso molecolare:96.19 kDa (predicted). Due to glycosylation, the protein migrates to 110-130 kDa based on Tris-Bis PAGE result.PfLDH Protein, P. falciparum, Recombinant (His)
Plasmodium falciparum lactate dehydrogenase (PfLDH) is a key enzyme for energy generation of malarial parasites and is considered to be a potential antimalarialPurezza:96.1%Colore e forma:Lyophilized PowderPeso molecolare:34.9 kDa (predicted)Urokinase/uPA Protein, Rat, Recombinant (His)
Urokinase/uPA Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Purezza:> 95 % as determined by SDS-PAGE - > 95 % as determined by SDS-PAGEColore e forma:Lyophilized PowderPeso molecolare:47.3 kDa (predicted)HER3/ERBB3 Protein, Human, Recombinant (His)
HER3/ERBB3 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag.Purezza:SDS-PAGE: 98.5%; SEC-HPLC: 97.6%Colore e forma:Lyophilized PowderPeso molecolare:70.2 kDa (predicted); 100-110 kDa (reducing condition, due to glycosylation)CDK2 Protein, Human, Recombinant (His)
CDK2 is a member of the Ser/Thr protein kinase family.Colore e forma:Lyophilized PowderPeso molecolare:35 kDa (predicted); 33 kDa (reducing conditions)Ref: TM-TMPY-04542
5µg95,00€10µg153,00€20µg245,00€50µg486,00€100µg837,00€200µg1.468,00€500µg3.037,00€COX-2 Protein, Human, Recombinant (His)
PTGS2, also known as COX-2, is s component of Prostaglandin-endoperoxide synthase (PTGS).Purezza:92.1% - > 90 % as determined by SDS-PAGEColore e forma:Lyophilized PowderPeso molecolare:68.5 kDa (predicted); 66 kDa (reducing conditions)Ref: TM-TMPY-01736
5µg162,00€10µg250,00€20µg400,00€50µg743,00€100µg1.190,00€200µg1.848,00€500µg3.518,00€TPSAB1 protein, Cynomolgus, Recombinant (His)
TPSAB1, namely tryptase alpha/beta-1, is a serine protease with trypsinlike activity.Colore e forma:Lyophilized PowderPeso molecolare:28.57kDa (predicted). The protein migrates to 30-33kDa based on Tris-Bis PAGE result.Necrostatin-1
CAS:Prodotto controllatoApplications Necroptosis is a regulated caspase-independent cell death mechanism that results in morphological features resembling necrosis. Necrostatin-1 is an inhibitor of RIP1 kinase that prevents the death of TNF-α-treated FADD-deficient Jurkat cells. Necrostatin-1 has been used to investigate the pathological importance of necroptosis in ischemic brain injury and myocardial infarction.
References Foresti, R., et al: J. Biol. Chem., 272, 18411 (1997); Cardenas, A., et al.: J. Neurochem., 74, 2041 (2000); Degterev, et al.: Nat. Chem. Biol., 1, 112 (2005); Hitomi, J., et al.: Cell, 135, 1311 (2008);Formula:C13H13N3OSColore e forma:NeatPeso molecolare:259.33Penase (Penicillinase)
CAS:Penase is an enzyme, specifically a type of beta-lactamase, which is derived from bacterial sources. Its mode of action involves the hydrolysis of the beta-lactam ring present in penicillin molecules. This enzymatic activity renders penicillin inactive by breaking its critical structural component that is essential for its antibacterial activity.Luciferase - from Photinus pyralis (firefly)
CAS:Luciferase enzyme from Photinus pyralis (firefly), which catalyzes the oxidation of firefly luciferin. This reaction depends on the presence of oxygen and ATP and causes the bioluminescence seen in firefliesPurezza:(Gel Electrophoresis) Min. 98%Colore e forma:PowderSPM-1 (β-Lactamase)
CAS:SPM-1 (β-Lactamase) is an enzyme, which is a type of metallo-beta-lactamase enzyme, derived from bacterial origins, specifically from pathogens associated with nosocomial infections. This enzyme acts by hydrolyzing the amide bond in the beta-lactam ring of antibiotics, rendering β-lactam antibiotics ineffective. SPM-1 participates in antibiotic resistance by facilitating the degradation of a wide range of β-lactam antibiotics, including penicillins and cephalosporins, thereby nullifying their therapeutic effects.
OXA-11 (β-Lactamase)
CAS:OXA-11 is a β-lactamase enzyme, which is a type of protein produced by certain bacteria. These enzymes are derived from the bacterial source and are responsible for antibiotic resistance. The primary mode of action of OXA-11 is the hydrolysis of the β-lactam ring found in various antibiotics, such as penicillins and cephalosporins, rendering them ineffective. This enzymatic activity allows bacteria to survive exposure to these antimicrobial agents, posing a significant challenge in clinical settings.KPC-1 (β-Lactamase)
CAS:KPC-1 (β-Lactamase) is an enzyme that breaks down β-lactam antibiotics, rendering them ineffective. It originates from strains of bacteria, particularly Klebsiella pneumoniae, which are significant sources of hospital-acquired infections. The mode of action involves hydrolyzing the β-lactam ring found in antibiotics such as penicillins and cephalosporins, neutralizing their antibacterial effects.EUCODIS® Peroxidase 13, from bacterial, fungal and plant origin, recombinant - EP013
Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.VIM-15 (β-Lactamase)
CAS:VIM-15 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from bacterial sources, particularly Gram-negative bacteria. Its mode of action involves the hydrolysis of β-lactam antibiotics, facilitating bacterial resistance. This enzyme employs zinc ions as cofactors to break the β-lactam ring, rendering these antibiotics ineffective against the bacteria that produce the enzyme. The hydrolysis process disrupts the antibiotic's structural integrity, crucial for its antibacterial activity, thereby nullifying its therapeutic effects.LacBuster™-L bulk (β-lactamase)
CAS:Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.Proteinase K, high-quality, liquid, recombinant
CAS:Proteinase K, high-quality, liquid, recombinant is an advanced enzymatic product, which is a serine protease derived through recombinant DNA technology. It cleaves peptide bonds to facilitate protein digestion with broad substrate specificity. Its robust proteolytic activity is optimal under various conditions, including a wide range of temperatures and pH levels, making it incredibly versatile.Carboxypeptidase G from pseudomonas sp.
CAS:Carboxypeptidase G (EC 3.4.17.11, alternative name γ-Glutamyl hydrolase) is a protease that cuts γ-glutamyl bonds with high specificity. One unit of Carboxypeptidase G will hydrolyze (+)amethopterin to generate 1.0 μmole of L-glutamic acid.Purezza:Min. 95%Carboxypeptidase B, >170 units/mg
CAS:Carboxypeptidase B is an enzyme responsible for the cleavage of arginine and lysine from a peptide's C-terminus
Colore e forma:PowderEUCODIS® Lipase 003, screening grade, recombinant, from microbial sources - EL003
Lipase 03 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 20-50°C. 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 03 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (90 %), laurate (28 %), palmitate (14 %), stearate (9 %), arachidate (2 %) and behenate (3 %).NMCA (β-Lactamase)
CAS:NMCA (β-Lactamase) is an enzyme, specifically acclaimed for its role in conferring antibiotic resistance. It is derived from bacterial sources, where it naturally occurs as part of the bacterial defense mechanism against β-lactam antibiotics. NMCA (β-Lactamase) functions by hydrolyzing the β-lactam ring present in these antibiotics, effectively rendering them inactive. This mode of action disrupts the antibiotic's ability to inhibit cell wall synthesis within bacteria, thereby permitting bacterial survival and proliferation.Colore e forma:PowderKPC-1 (β-Lactamase)
CAS:KPC-1 (β-Lactamase) is a specialized enzyme, which is produced by certain Gram-negative bacteria, notably Klebsiella pneumoniae. It functions by hydrolyzing the β-lactam ring found in a wide range of β-lactam antibiotics, such as penicillins and cephalosporins. This enzymatic action effectively neutralizes the antibiotic's antimicrobial properties, rendering the drugs ineffective against bacteria that produce KPC-1.SPM-1 (β-Lactamase)
CAS:SPM-1 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from certain Gram-negative bacteria, such as Pseudomonas aeruginosa. This enzyme is characterized by its ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, due to the presence of a zinc ion in its active site. The zinc ion plays a crucial role in the catalytic mechanism by facilitating the cleavage of the β-lactam ring, rendering the antibiotic ineffective against bacterial cell wall synthesis.OXA-11 (β-Lactamase)
CAS:OXA-11 (β-Lactamase) is an enzyme of the β-lactamase class, which is primarily derived from Gram-negative bacteria. This enzyme is characterized by its ability to hydrolyze β-lactam antibiotics, rendering them ineffective by breaking the β-lactam ring, a crucial component of these antibiotics. OXA-11 is a notable member of the oxacillinase group within class D β-lactamases, known for its resistance to penicillins and cephalosporins.Glucosyltransferase211-freeze dried
CAS:Glucosyltransferase211-freeze dried is an enzyme preparation which is derived from microbial fermentation. This enzyme functions by catalyzing the transfer of glucosyl groups from activated donor molecules to specific acceptor substrates. Its mechanism of action involves the formation of glycosidic bonds, facilitating the synthesis of various oligosaccharides and polysaccharides.Glucosyltransferase204-freeze dried
CAS:Glucosyltransferase204-freeze dried is an enzyme preparation, derived from specific strains of Streptococcus bacteria, which plays a crucial role in catalyzing the transfer of glucosyl units from donor molecules to acceptor carbohydrates, predominantly in the formation of glucans. This enzymatic activity results in complex carbohydrate structures essential for various biological processes.
Glucosyltransferase205-freeze dried
CAS:Glucosyltransferase205-freeze dried is an enzyme preparation that is commonly used in biochemical and molecular biology research. It is derived from microbial sources, often from bacteria or fungi that are known for producing extracellular enzymes. The primary mode of action of Glucosyltransferase205 involves catalyzing the transfer of glucose residues from donor molecules, such as UDP-glucose, to acceptor molecules, forming glycosidic bonds. This enzymatic activity is crucial in the biosynthesis of polysaccharides, which are essential components in various biological structures and processes.
Glucosyltransferase210-freeze dried
CAS:Glucosyltransferase210-freeze dried is an enzyme preparation that catalyzes the transfer of glucose molecules. Derived from specific microorganisms, it facilitates biochemical reactions by adding glucose residues to various substrates, thereby modifying their structure and function. The enzyme functions through the glucosylation process, which is essential in synthesizing different polysaccharides and glycoconjugates.Carboxypeptidase P
CAS:Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.Formula:C8H17N2O5PPeso molecolare:252.2 g/molGlucosyltransferase206-freeze dried
CAS:Glucosyltransferase206-freeze dried is an enzymatic preparation designed for specific biochemical applications. It is derived from microbial sources, where it is produced and purified through advanced biotechnological processes. The enzyme functions by catalyzing the transfer of glucosyl units from donor molecules to specific acceptors, thereby forming glycosidic bonds. This mode of action is crucial in various biosynthetic pathways, particularly in the production of polysaccharides and structural carbohydrates.Lipase 017
CAS: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.Glucosyltransferase203-freeze dried
CAS:Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.
