A9934
Aminopeptidase I from Streptomyces griseus
lyophilized powder, ≥200 units/mg protein
Synonym(s):
Leucine Aminopeptidase IV
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A9934-.1MG
PLN 1,207.00
PLN 1,207.00
List PricePLN 1,420.00Save 15%Please contact Customer Service for Availability
About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-874-6
NACRES:
NA.54
MDL number:
Specific activity:
≥200 units/mg protein
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form
lyophilized powder
Quality Level
specific activity
≥200 units/mg protein
mol wt
21 kDa by gel filtration, 33 kDa by SDS-PAGE
composition
Protein, 40-60% Lowry
storage temp.
−20°C
Related Categories
1 of 4
This Item | |||
|---|---|---|---|
| specific activity ≥200 units/mg protein | specific activity ≥3.5 units/mg solid | specific activity ≥5.0 units/mg protein | specific activity 0.5 units/mg protein |
| form lyophilized powder | form powder | form lyophilized powder | form solution |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 21 kDa by gel filtration, 33 kDa by SDS-PAGE | mol wt - | mol wt 24.072 kDa by amino acid sequence, 28 kDa by SDS-PAGE | mol wt 37 kDa by SDS-PAGE |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| composition Protein, 40-60% Lowry | composition - | composition - | composition - |
General description
Aminopeptidase I from Streptomyces griseus is a thermostable enzyme with Glu131 and Tyr246 as key active site residues.[1]
Application
Biochem/physiol Actions
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.
Packaging
Package size based on protein content.
Physical form
Contains calcium acetate
Preparation Note
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.
Other Notes
Endopeptidase contaminant: Not more than: 0.01 U/mg protein (as μmole tyrosine equivalent per min released from casein.)
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.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Sobhan Sen et al.
Biophysical journal, 89(6), 4129-4138 (2005-10-04)
Synthetic oligonucleotides with a fluorescent coumarin group replacing a basepair have been used in recent time-resolved Stokes-shift experiments to measure DNA dynamics on the femtosecond to nanosecond timescales. Here, we show that the APE1 endonuclease cleaves such a modified oligonucleotide
Claudine Kraft et al.
Nature cell biology, 10(5), 602-610 (2008-04-09)
Eukaryotic cells use autophagy and the ubiquitin-proteasome system (UPS) as their major protein degradation pathways. Whereas the UPS is required for the rapid degradation of proteins when fast adaptation is needed, autophagy pathways selectively remove protein aggregates and damaged or
Paula D B Adamis et al.
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine, 22(2), 243-249 (2008-08-22)
In Saccharomyces cerevisiae, accumulation of cadmium-glutathione complex in cytoplasm inhibits cadmium absorption, glutathione transferase 2 is required for the formation of the complex and the vacuolar gamma-glutamyl transferase participates of the first step of glutathione degradation. Here, we proposed that
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
[Autophagy related genes in yeast, S. cerevisiae].
Yoshinori Ohsumi
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 51(10 Suppl), 1453-1456 (2006-08-23)
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