A9934
Aminopeptidase I from Streptomyces griseus
lyophilized powder, ≥200 units/mg protein
Sinónimos:
Leucine Aminopeptidase IV
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About This Item
Productos recomendados
Formulario
lyophilized powder
Nivel de calidad
actividad específica
≥200 units/mg protein
mol peso
21 kDa by gel filtration
33 kDa by SDS-PAGE
composición
Protein, 40-60% Lowry
temp. de almacenamiento
−20°C
Categorías relacionadas
Descripción general
Aminopeptidase I from Streptomyces griseus is a thermostable enzyme with Glu131 and Tyr246 as key active site residues.
Aplicación
Aminopeptidase I from Streptomyces griseus has been used:
- to test the biochar exposure effect on the enzyme activity
- in circular dichroism (CD) spectroscopy studies
- as a positive control in p-nitroanilide degradation assay
Acciones bioquímicas o fisiológicas
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.
Aminopeptidase I may also be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. In the first stage, the endoprotease cleaves a peptide, such as Z-Y-X-Leu-p-nitroanilide, with the X, Y, and Z residues being chosen according to the specificity of the endoprotease.
Envase
Package size based on protein content.
Definición de unidad
One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0, 25 °C and 3.0 mM substrate concentration.
Forma física
Contains calcium acetate
Nota de preparación
Reconstitute in 20 mM tricine, pH 8.0, with 0.05% bovine serum albumin. Dilute the enzyme with the reconstitution buffer to 0.15-0.3 U/mL for a working concentration. Solutions should be prepared fresh prior to use.
Otras notas
Endopeptidase contaminant: Not more than: 0.01 U/mg protein (as μmole tyrosine equivalent per min released from casein.)
Palabra de señalización
Danger
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Órganos de actuación
Respiratory system
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Acta crystallographica. Section F, Structural biology and crystallization communications, 63(Pt 3), 200-203 (2007-03-03)
The vacuole hydrolase aminopeptidase 1 (Ape1) is a cargo protein transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ape1 is processed into
[Cytoplasm to vacuole targeting pathway in yeast].
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Ionizing radiation, oxidative stress and endogenous DNA-damage processing can result in a variety of single-strand breaks with modified 5' and/or 3' ends. These are thought to be one of the most persistent forms of DNA damage and may threaten cell
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The Journal of biological chemistry, 280(47), 39067-39076 (2005-09-28)
The cytoplasm to vacuole (Cvt) trafficking pathway in S. cerevisiae is a constitutive biosynthetic pathway required for the transport of two vacuolar enzymes, aminopeptidase I (Ape1p) and alpha-mannosidase (Ams1p), to the vacuole. Ape1p and Ams1p bind to their receptor, Atg19p
Jem A Efe et al.
Journal of cell science, 118(Pt 20), 4751-4764 (2005-10-13)
Although the small Arf-like GTPases Arl1-3 are highly conserved eukaryotic proteins, they remain relatively poorly characterized. The yeast and mammalian Arl1 proteins bind to the Golgi complex, where they recruit specific structural proteins such as Golgins. Yeast Arl1p directly interacts
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