recombinant
expressed in E. coli
Quality Level
grade
Proteomics Grade
form
powder
specific activity
50-100 U/mg
shelf life
2 yr
shipped in
wet ice
storage temp.
−20°C
Other Notes
One unit will hydrolyze 1.0 micromole of Leucine P-Nitroanilide to L-Leucine and P-Nitroaniline per minute at pH 8.0 at 25°C.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
存储类别
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
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C Schalk et al.
Archives of biochemistry and biophysics, 294(1), 91-97 (1992-04-01)
The heat-stable aminopeptidase from Aeromonas proteolytica has been purified using two new procedures, with the aim of preparing large single crystals for X-ray analysis. In a first procedure, we tried to avoid any drastic conditions capable of inducing microheterogeneities in
William T Desmarais et al.
Structure (London, England : 1993), 10(8), 1063-1072 (2002-08-15)
The aminopeptidase from Aeromonas proteolytica (AAP) is a bridged bimetallic enzyme that removes the N-terminal amino acid from a peptide chain. To fully understand the metal roles in the reaction pathway of AAP we have solved the 1.20 A resolution
Mariam Hartley et al.
Protein expression and purification, 66(1), 91-101 (2009-02-24)
Metalloaminopeptidases (mAPs) are enzymes that are involved in HIV infectivity, tumor growth and metastasis, angiogenesis, and bacterial infection. Investigation of structure-function relationships in mAPs is a prerequisite to rational design of anti-mAP chemotherapeutics. The most intensively studied member of the
全球贸易项目编号
| 货号 | GTIN |
|---|---|
| A4987-100UN | 04061832699554 |
| A4987-250UN | 04061832699561 |