A9934
Aminopeptidase I from Streptomyces griseus
lyophilized powder, ≥200 units/mg protein
Synonym(e):
Leucine Aminopeptidase IV
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(1)
About This Item
Empfohlene Produkte
Form
lyophilized powder
Qualitätsniveau
Spezifische Aktivität
≥200 units/mg protein
Mol-Gew.
21 kDa by gel filtration
33 kDa by SDS-PAGE
Zusammensetzung
Protein, 40-60% Lowry
Lagertemp.
−20°C
Allgemeine Beschreibung
Aminopeptidase I from Streptomyces griseus is a thermostable enzyme with Glu131 and Tyr246 as key active site residues.
Anwendung
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
Biochem./physiol. Wirkung
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.
Verpackung
Package size based on protein content.
Einheitendefinition
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.
Physikalische Form
Contains calcium acetate
Angaben zur Herstellung
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.
Sonstige Hinweise
Endopeptidase contaminant: Not more than: 0.01 U/mg protein (as μmole tyrosine equivalent per min released from casein.)
Signalwort
Danger
H-Sätze
Gefahreneinstufungen
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Zielorgane
Respiratory system
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Analysenzertifikate (COA)
Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.
Besitzen Sie dieses Produkt bereits?
In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.
Kunden haben sich ebenfalls angesehen
[Autophagy related genes in yeast, S. cerevisiae].
Yoshinori Ohsumi
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 51(10 Suppl), 1453-1456 (2006-08-23)
Indig, F.E., et al.
Febs Letters, 225, 237-237 (1989)
Taras Y Nazarko et al.
Autophagy, 1(1), 37-45 (2006-07-29)
Yarrowia lipolytica was recently introduced as a new model organism to study peroxisome degradation in yeasts. Transfer of Y. lipolytica cells from oleate/ethylamine to glucose/ammonium chloride medium leads to selective macroautophagy of peroxisomes. To decipher the molecular mechanisms of macropexophagy
A Spungin et al.
European journal of biochemistry, 183(2), 471-477 (1989-08-01)
A heat-stable aminopeptidase with an N-terminal Ala-Pro-Asp-Ile-Pro-Leu sequence has been purified from Streptomyces griseus by heat treatment followed by gel-exclusion and anion-exchange chromatographic procedures. The enzyme is a monomeric zinc metalloenzyme showing an apparent molecular mass of 33 kDa by
Congcong He et al.
Molecular biology of the cell, 19(12), 5506-5516 (2008-10-03)
Autophagy is the degradation of a cell's own components within lysosomes (or the analogous yeast vacuole), and its malfunction contributes to a variety of human diseases. Atg9 is the sole integral membrane protein required in formation of the initial sequestering
Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..
Setzen Sie sich mit dem technischen Dienst in Verbindung.