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The enzyme is a ribozyme. Two non-equivlant ribonucleoprotein subunits operate in non-concerted fashion in peptide elongation. The small subunit forms the mRNA-binding machinery and decoding center, the large subunit performs the main ribosomal catalytic function in the peptidyl-transferase center. Group: Enzymes. Synonyms: transpeptidase; ribosomal peptidyltransferase. Enzyme Commission Number: EC 2.3.2.12. CAS No. 9059-29-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2285; peptidyltransferase; EC 2.3.2.12; 9059-29-4; transpeptidase; ribosomal peptidyltransferase. Cat No: EXWM-2285.
23S rRNA (guanosine2251-2'-O)-methyltransferase
The enzyme catalyses the methylation of guanosine2251, a modification conserved in the peptidyltransferase domain of 23S rRNA. Group: Enzymes. Synonyms: rlmB (gene name); yifH (gene name). Enzyme Commission Number: EC 2.1.1.185. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1784; 23S rRNA (guanosine2251-2'-O)-methyltransferase; EC 2.1.1.185; rlmB (gene name); yifH (gene name). Cat No: EXWM-1784.
Chloramphenicol
Chloramphenicol is a chlorine-containing antibiotic produced by Streptomyces venezuelae. It has a wide spectrum of activity against gram-positive and gram-negative cocci and bacilli (including anaerobes), Rickettsia, Mycoplasma, and Chlamydia. It inhibits prokaryotic protein synthesis by attaching to the 50S ribosomal subunit. This inhibits peptidyltransferase, thereby preventing the formation of peptide bonds. It also inhibits protein synthesis in mitochondria which accounts for its toxic effects that cause aplastic anemia. Chloramphenicol has other adverse effects such as bone marrow depression, and gray baby syndrome. Its use is limited to serious infections such as those where resistance to other antibiotics occurs. It is still widely used in the treatment of typhoid fever, meningitis and eye infections. Group: Biochemicals. Alternative Names: 2, 2-Dichloro-N-[ (1R, 2R) -2-hydroxy-1- (hydroxymethyl) -2- (4-nitrophenyl) ethyl]Acetamide; D-threo-N-Dichloroacetyl-1-p-nitrophenyl-2-amino-1,3-propanediol; Anacetin; Aquamycetin; Chlorocid; Chloroptic; Fenicol; Pantovernil; Paraxin; Chloromycetin. Grades: Molecular Biology Grade. CAS No. 56-75-7. Pack Sizes: 25g, 100g, 250g, 500g, 1Kg. Molecular Formula: C11H12Cl2N2O5, Molecular Weight: 323.13. US Biological Life Sciences.
Worldwide
Chloramphenicol succinate sodium salt
Chloramphenicol is a chlorine-containing antibiotic produced by Streptomyces venezuelae. It has a wide spectrum of activity against gram-positive and gram-negative cocci and bacilli (including anaerobes), Rickettsia, Mycoplasma, and Chlamydia. It inhibits prokaryotic protein synthesis by attaching to the 50S ribosomal subunit. This inhibits peptidyltransferase, thereby preventing the formation of peptide bonds. It also inhibits protein synthesis in mitochondria which accounts for its toxic effects that cause aplastic anemia. Chloramphenicol has other adverse effects such as bone marrow depression, and gray baby syndrome. Its use is limited to serious infections such as those where resistance to other antibiotics occurs. It is still widely used in the treatment of typhoid fever, meningitis and eye infections. Group: Biochemicals. Alternative Names: Chloramphenicol alpha-succinate. Grades: Molecular Biology Grade. CAS No. 982-57-0. Pack Sizes: 5g, 25g. US Biological Life Sciences.
Worldwide
Florfenicol amine hydrochloride
Florfenicol amine hydrochloride is a metabolite of Florfenicol (HY-B1374). Florfenicol inhibits bacterial protein synthesis by binding to 50S and 70S subunits in the ribosome to abolish the activity of peptidyltransferase. Florfenicol, is a veterinary antibiotic, can be used in aquaculture to control susceptible bacterial diseases [1] [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 108656-33-3. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg. Product ID: HY-118099.
γ-glutamyltransferase
The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. Group: Enzymes. Synonyms: glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2293; γ-glutamyltransferase; EC 2.3.2.2; 9046-27-9; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-2293.
Native Bovine Gamma-Glutamyl Transferase
γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular.transferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. Purity: Purified. γ-GT. Activity: > 30 U/mg (Dimension Clinical Chemistry System). Appearance: Tan Powder. Storage: -20°C. Form: Lyophilized. Source: Bovine Kidney. Species: Bovine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0790.
Native Equine γ-Glutamyltranspeptidase
γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 5-12 units/mg solid. Storage: -20°C. Source: Equine kidney. Species: Equine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0791.
Native Human Gamma-Glutamyl Transferase
γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular pathophysiology. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl tr. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: >50 U/mg. Storage: 4°C. Source: Human Liver. Species: Human. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0792.
Native Porcine γ-Glutamyltranspeptidase
γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellul.ase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: 2.0-6.0 units/mg solid. Storage: -20°C. Source: Porcine kidney. Species: Porcine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0793.
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