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Leucineaminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucineaminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: LeucineAminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. LeucineAminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879.
Native Porcine LeucineAminopeptidase, microsomal
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli (E. coli) LAP (also known as PepA or XerB), and the solanaceous-specific acidic LAP (LAP-A) in tomato (Solanum lycopersicum). Group: Enzymes. Synonyms: LeucineAminopeptidase, microsomal; 9054-63-1; leucineaminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL prot. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9054-63-1. LAP. Activity: Type VI-S, > 12 units/mg protein (biuret); Type IV-S, 10-40 units/mg protein (Bradford). Form: Type VI-S, lyophilized powder; Type IV-S, ammonium sulfate suspension. Source: Porcine kidney. Species: Porcine. LeucineAminopeptidase, microsomal; 9054-63-1; leucineaminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-0378.
Actinonin
Actinonin ((-)-Actinonin) is a naturally occurring antibacterial agent produced by Actinomyces. Actinonin inhibits aminopeptidase M , aminopeptidase N and leucineaminopeptidase. Actinonin is a potent reversible peptide deformylase (PDF) inhibitor with a K i of 0.28 nM. Actinonin also inhibits MMP-1 , MMP-3 , MMP-8 , MMP-9 , and hmeprin α with K i values of 300 nM, 1,700 nM, 190 nM, 330 nM, and 20 nM, respectively. Actinonin is an apoptosis inducer. Actinonin has antiproliferative and antitumor activities [1] [2] [3] [4] [5]. Uses: Scientific research. Group: Natural products. Alternative Names: (-)-Actinonin. CAS No. 13434-13-4. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-113952.
Adamantanine
Adamantanine (2-Aminoadamantane-2-carboxylic acid) inhibits the transport of methionine ( K i is 0.76 mM) and leucine into Ehrlich ascites carcinoma cells. Adamantanine inhibits proliferation of P388 lymphocytic leukemia cells with an IC 50 of >1 mM. Adamantanine inhibits the leucineaminopeptidase with an I/S 0.5 of 10.5 [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 2-Aminoadamantane-2-carboxylic acid. CAS No. 42381-05-5. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-121123.
Amastatin hydrochloride
Amastatin, also known as 3-amino-2-hydroxy-5-methylhexanoyl-L-valyl-L-valyl-L-aspartic acid, is a naturally occurring, competitive and reversible aminopeptidase inhibitor. Amastatin has originally been isolated from the culture filtrate of Streptomyces sp. ME98-M3 and is a competitive inhibitor of human serum aminopeptidase A (Ki = 1.1 · 10?? M) and of pig kidney leucineaminopeptidase (Ki = 1.6 · 10?? M). Amastatin hydrochloride has been shown to slightly decrease the conversion of angiontensin II to angiotensin III, but significantly increases the potency of angiotensin III and des(Asp1)angiotensin I. Synonyms: BIMI-1803; J-000280; ZX-AFC000547; Amastatin HCl. Grades: ≥95%. CAS No. 100938-10-1. Molecular formula: C21H39ClN4O8. Mole weight: 511.01.
Amastatin hydrochloride
Amastatin hydrochloride is a slow, tight binding, competitive aminopeptidase (AP) inhibitor with K i values of 0.26 nM, 30 nM, 52 nM for Aeromonas aminopeptidase, cytosolic leucineaminopeptidase, microsomal aminopeptidase [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 100938-10-1. Pack Sizes: 1 mg; 5 mg. Product ID: HY-115194.
aminopeptidase I
A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucineaminopeptidase IV; yeast aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. 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-4019; aminopeptidase I; EC 3.4.11.22; 9031-94-1; aminopeptidase III; aminopeptidase yscI; leucineaminopeptidase IV; yeast aminopeptidase I. Cat No: EXWM-4019.
Bestatin hydrochloride
Bestatin hydrochloride is a competitive aminopeptidase inhibitor, which is studied for use in the treatment of acute myelocytic leukemia. It has become a useful tool in elucidating the physiological role of some mammalian exopeptidases in the regulation of the immune system, in the growth of tumors and their invasion of surrounding tissues, and in the degradation of cellular proteins. Synonyms: Aminopeptidase inhibitor; leucineaminopeptidase; aminopeptidase B; NK-421. Grades: >98%. CAS No. 65391-42-6. Molecular formula: C16H24N2O4.HCl. Mole weight: 344.83.
Bu-2743E
Bu-2743E is a leucineaminopeptidase (LAP) inhibitor originally isolated from Bacillus circulans J725-B93. It inhibits the LAP with an IC50 of 0.51 μg/mL. Synonyms: (2,3-Dihydroxybenzoyl)-L-alanyl-L-threonine. CAS No. 88167-28-6. Molecular formula: C14H18N2O7. Mole weight: 326.30.
Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant
Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucineaminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981.
Gly-Leu-OH
Substrate for aminopeptidases. Synonyms: Glycyl-L-leucine; N-Glycyl-L-leucine. Grades: ≥ 98.5% (HPLC). CAS No. 869-19-2. Molecular formula: C8H16N2O3. Mole weight: 188.23.
L-Leucine 7-Amido-4-methylcoumarin Hydrochloride is a fluorogenic substrate for LAP3 (leucineaminopeptidase). Upon enzyme activity, a bright blue fluorescent dye, 7-amino-4-methylcoumarin, is released. Group: Biochemicals. Alternative Names: L-Ala-AMC·HCl. Grades: Highly Purified. CAS No. 62480-44-8. Pack Sizes: 100mg, 250mg, 1g. Molecular Formula: C13H14N2O3·HCl, Molecular Weight: 282.6. US Biological Life Sciences.
Worldwide
Leu-AMC HCl
L-Leucine 7-Amido-4-methylcoumarin Hydrochloride is a fluorogenic substrate for LAP3 (leucineaminopeptidase). Upon enzyme activity, a bright blue fluorescent dye, 7-amino-4-methylcoumarin, is released. Synonyms: L-Leucine-AMC.HCl. Grades: ≥ 99% (HPLC). CAS No. 62480-44-8. Molecular formula: C16H21ClN2O3. Mole weight: 324.80.
leucyl aminopeptidase
A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Group: Enzymes. Synonyms: leucineaminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9001-61-0. LAP. 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-4007; leucyl aminopeptidase; EC 3.4.11.1; 9001-61-0; leucineaminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucineaminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Cat No: EXWM-4007.
L-Leucine 4-nitroanilide
A substrate for the colorimetric determination of leucineaminopeptidase. Synonyms: L-Leu-pNA; L-Leucine-p-nitroanilide. Grades: ≥ 99% (HPLC). CAS No. 4178-93-2. Molecular formula: C12H17N3O3. Mole weight: 251.30.
L-Leucine 7-amido-4-methylcoumarin
Sensitive fluorogenic A substrate for leucineaminopeptidase and aminopeptidase M. Synonyms: L-Leu-AMC; L-leucine 4-methylcoumaryl-7-amide; 7-Leucylamido-4-methylcoumarin; (S)-2-amino-4-methyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)valeramide. Grades: ≥ 99.5% (HPLC). CAS No. 66447-31-2. Molecular formula: C16H20N2O3. Mole weight: 288.37.
L-Leucine-7-amido-4-methylcoumarin hydrochloride
L-Leucine-7-amido-4-methylcoumarin (Leu-AMC) hydrochloride is a bright blue fluorogenic peptidyl substrate for LAP3 (leucineaminopeptidase). L-Leucine-7-amido-4-methylcoumarin hydrochloride can be used for leucineaminopeptidase inhibition assays in vitro [1]. Uses: Scientific research. Group: Fluorescent dye. Alternative Names: Leu-AMC hydrochloride. CAS No. 62480-44-8. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-137844.
L-Leucine β-naphthylamide hydrochloride
A substrate for the assay of leucine-aminopeptidase. Synonyms: L-Leu-βNA HCl; (2S)-2-amino-4-methyl-N-naphthalen-2-ylpentanamide hydrochloride; L-Leucine alpha-naphthylamide hydrochloride. Grades: ≥ 99% (TLC). CAS No. 893-36-7. Molecular formula: C16H20N2O·HCl. Mole weight: 292.90.
membrane alanyl aminopeptidase
A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1. Group: Enzymes. Synonyms: microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucineaminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. 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-4016; membrane alanyl aminopeptidase; EC 3.4.11.2; 9054-63-1; microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucineaminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Cat No: EXWM-4016.
Native Arthrobacter sp. Tyramine Oxidase
Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 <-> RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Native tyramine oxidase (ec 1.4.3.4) was purified from arthrobacter sp. Applications: Useful for enzymatic determiantion of leucineaminopeptidase. Group: Enzymes. Synonyms: Tyramine Oxidase; TOD; EC 1.4.3.6. Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Tyramine Oxidase. Activity: > 3 U/mg. Appearance: White to light brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter sp. Tyramine Oxidase; TOD; EC 1.4.3.6. Cat No: DIA-158.
Native Crotalus atrox L-Amino Acid Oxidase
In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase is used to convert l-amino acids to their corresponding α-keto acids. this product is from crotalus atrox. one unit will oxidatively deaminate 1.0 μmole of l-phenylalanine per min at ph 6.5 at 37°c. l-amino acid oxidase, from creative enzymes, has been used in leucineaminopeptidase (lap) activity assays. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxido. Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: > 0.10 unit/mg solid. Storage: -20°C. Form: dried venom. Source: Crotalus atrox (Western Diamondback Rattlesnake). L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Cat No: NATE-0367.
In enzymology, an L-amino acid oxidase (LAAO) (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction:an L-amino acid + H2O + O2<-> a 2-oxo acid + NH3 + H2O2. The enzyme was first described in 1944 by A. Zeller and A. Maritz. Not only are LAAOs quite variable in terms of molecular mass, they also vary widely regarding stability. In a similar vein, this enzyme performs in a myriad of biological activities including apoptosis-induction, edema-induction, hemorrhaging, and inhibition or induction of platelet aggregation. Applications: L-amino acid oxidase (laao) is used to convert l-amino acids to their corresponding α-keto acids. this product is from crotalus durissus venom. l-amino acid oxidase, from creative enzymes, has been used in leucineaminopeptidase (lap) activity assays. Group: Enzymes. Synonyms: L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:ox. Enzyme Commission Number: EC 1.4.3.2. CAS No. 9000-89-9. LAAO. Activity: 3-8 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH approx. 6. Source: Crotalus durissus venom. L-amino acid oxidase; LAAO; L-AAO; EC 1.4.3.2; 9000-89-9; ophio-amino-acid oxidase; L-amino-acid:oxygen oxidoreductase (deaminating). Pack: Package size based on protein content. Cat No: NATE-0368.
Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucineaminopeptidase and urea...ating); EC 1.4.1.2; GLDH. Enzyme Commission Number: EC 1.4.1.2. CAS No. 9001-46-1. Mole weight: approx. 260 kDa. Activity: 100 U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Microorganism. Glutamate Dehydrogenase; glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD: gluta
Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucineaminopeptidase and urea...lutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Enzyme Commission Number: EC 1.4.1.4. Mole weight: approx. 300 kDa. Activity: 300U/mg-protein or more (9,000U/ml or more). Appearance: Solution with 50mM Tris-HCl buffer containing 0.05% NaN3 and 5.0mM EDTA, pH 7.8. Form: Freeze dried powder. Source: Proteus sp. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: DIA-196.
L-glutamic dehydrogenase catalyzes the conversion of glutamate to α-ketoglutarate. Applications: This enzyme is useful for enzymatic determination of nh3, α-ketoglutaric acid and l-glutamic acid, and for assay of leucineaminopeptidase and urease. this enzyme is also used for enzymatic determination of urea when coupled with urease (urh-201) in clinical analysis. Group: Enzymes. Synonyms: L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate de. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Mole weight: mol wt ~300 kDa. Activity: > 400 units/mg protein (biuret). Storage: 2-8°C. Form: buffered aqueous solution; Solution in 50 mM Tris HCl, pH 7.8, 5 mM Na2EDTA containing 0.05% sodium azide. Source: Proteus sp. L-Glutamic Dehydrogenase; EC 1.4.1.4; 9029-11-2; glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD (P)-glutamate dehydrogenase; NAD (P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP). Cat No: NATE-0395.
Native Streptomyces griseus Aminopeptidase I
Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucineaminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucineaminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070.
Ubenimex
Ubenimex (INN), also known more commonly as bestatin, is a competitive, reversible protease inhibitor. It is an inhibitor of arginyl aminopeptidase (aminopeptidase B), leukotriene A4 hydrolase (a zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities), alanyl aminopeptidase (aminopeptidase M/N), leucyl/cystinyl aminopeptidase (oxytocinase/vasopressinase), and membrane dipeptidase (leukotriene D4 hydrolase). It is being studied for use in the treatment of acute myelocytic leukemia. It is derived from Streptomyces olivoreticuli. Ubenimex has been found to inhibit the enzymatic degradation of oxytocin, vasopressin, enkephalins, and various other peptides and compounds. Alternative Names: 3-(r)-amino-2-(s)-hydroxy-4-phenylbutanoyl-(s)-leucine;n-(3-amino-2-hydroxy-1-oxo-4-phenylbutyl)-,(s-(r*,s*))-l-leucin;nk421;UBENIMEX;N-[(2S,3R)-3-AMINO-2-HYDROXY-1-OXO-4-PHENYLBUTYL]-L-LEUCINE;N-((2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTYRYL)-L-LEUCINE;[(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTYRYL]-L-LEUCINE;[(2S,3R)-3-AMINO-2-HYDROXY-4-PHENYLBUTANOYL]-LEU. CAS No. 58970-76-6. Molecular formula: C16H24N2O4. Mole weight: 308.37. Appearance: White crystalline powder. Purity: 0.99. IUPACName: (2S)-2-[[(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoyl]amino]-4-methylpentanoicacid. Canonical SMILES: CC (C)CC (C (=O)O)NC (=O)C (C (CC1=CC=CC=C1)N)O. Density: 1.197 g/cm³. ECNumber: 261-529-2. Catalog: ACM58970766.
L-Leucine α-naphthylamide
A substrate for a histochemical assay of aminopeptidase M. Synonyms: L-Leu-αNA; (2S)-2-amino-4-methyl-N-naphthalen-1-ylpentanamide. Grades: ≥ 98% (TLC). CAS No. 203793-55-9. Molecular formula: C16H20N2O. Mole weight: 256.35.
L-Leucinol
A reversible inhibitor of protein synthesis and starting material for the synthesis of aminopeptidase N and phospholipase A2 inhibitors. Synonyms: (S)-(+)-Leucinol; H-Leucinol; L-(+)-Leucinol; (2S)-2-amino-4-methylpentan-1-ol. CAS No. 7533-40-6. Molecular formula: C6H15NO. Mole weight: 117.2.
L-Leucinol
L-Leucinol ((+)-Leucinol) is a competitive aminopeptidase inhibitor with K i value of 17 μM [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: (+)-Leucinol. CAS No. 7533-40-6. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg; 500 mg; 1 g; 5 g. Product ID: HY-W015876.
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