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此商品 | P5147 | P6236 | P6911 |
|---|---|---|---|
| form lyophilized powder | form powder | form lyophilized powder | form powder |
| 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 monomer ~20 kDa |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
| composition Protein, 40-60% Lowry | composition - | composition - | composition - |
一般描述
Aminopeptidase I from Streptomyces griseus is a thermostable enzyme with Glu131 and Tyr246 as key active site residues.[1]
应用
生化/生理作用
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.
包装
Package size based on protein content.
单位定义
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.
外形
Contains calcium acetate
制备说明
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.
其他说明
Endopeptidase contaminant: Not more than: 0.01 U/mg protein (as μmole tyrosine equivalent per min released from casein.)
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
储存分类代码
11 - Combustible Solids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Tomohiro Yorimitsu et al.
Molecular biology of the cell, 16(4), 1593-1605 (2005-01-22)
Proteins are selectively packaged into vesicles at specific sites and then delivered correctly to the various organelles where they function, which is critical to the proper physiology of each organelle. The precursor form of the vacuolar hydrolase aminopeptidase I is
Indig, F.E., et al.
Febs Letters, 225, 237-237 (1989)
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
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
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