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A9934

Aminopeptidase I from Streptomyces griseus

lyophilized powder, ≥200 units/mg protein

Synonym(s):

Leucine Aminopeptidase IV

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0.1 MG

$287.30

$287.30

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About This Item

CAS Number:
EC 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

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P5147P6236M6435
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

Aminopeptidase I from Streptomyces griseus has been used:
  • to test the biochar exposure effect on the enzyme activity
  • in circular dichroism (CD) spectroscopy studies[2]
  • as a positive control in p-nitroanilide degradation assay[3]

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.

pictograms

Health hazardExclamation mark

signalword

Danger

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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Jason L Parsons et al.
The FEBS journal, 272(22), 5753-5763 (2005-11-11)
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
Bonnie K Baxter et al.
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
[Cytoplasm to vacuole targeting pathway in yeast].
Takahiro Shintani
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 51(10 Suppl), 1480-1483 (2006-08-23)
Wakana Adachi et al.
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
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

Global Trade Item Number

SKUGTIN
A9934-.1MG04061832699615

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