Takara Edman degradation and protein sequencing: Pfu Pyroglutamate Aminopeptidase
Pfu Pyroglutamate Aminopeptidase는 단백질 및 펩타이드 N-말단의 pyroglutamic acid 제거에 사용됩니다. 고온(95–100°C)에서도 안정하며, 다양한 pH 범위에서 높은 활성 유지. 재조합 E. coli에서 생산된 효소로, Edman degradation 및 단백질 서열 분석에 적합.
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1개 옵션 · 카탈로그 번호를 클릭하면 복사됩니다Takara · Takara Edman degradation and protein sequencing: Pfu Pyroglutamate Aminopeptidase
Takara Pfu Pyroglutamate Aminopeptidase
Applications
- Removal of pyroglutamic acids from the N-termini of proteins and peptides
Components
Supplied Buffer
- Volume: 1 ml
- Composition: 250 mM sodium phosphate buffer (pH 7.0) containing 50 mM DTT and 5 mM EDTA
- Specific activity comparison:
- 5.83 U/mg protein at 37°C
- 12.2 U/mg protein at 50°C
- 28.3 U/mg protein at 75°C
Source
Recombinant Escherichia coli encoding the Pyrococcus furiosus pyroglutamate aminopeptidase gene.
Properties
| 항목 | 내용 |
|---|---|
| Systematic name | L-Pyrrolidone carboxyl peptidase |
| Enzyme code | 3.4.19.3 |
| Molecular weight | 24.072 kDa (calculated), 28 kDa (by SDS-PAGE) |
| Optimum temperature | 95–100°C |
| Thermo stability | ~90% activity at 75°C; pH 7.0, 150 min |
| Optimum pH | 6.0–9.0 (≥80% activity in pH 5.0–9.0 at 75°C after 30 min reactivation) |
| Tolerance to denaturants | ≤1 M Urea, ≤1 M Guanidine-HCl, ≤0.01% SDS |
| Inhibitors | PCMB, Hg²⁺ |
Definition of Activity
One unit of enzyme activity corresponds to the amount required to hydrolyze 1 µmol pyroglutamate p-nitroanilide at 37°C in 1 minute at pH 7.0.
References
- Hamazume, Y. & Mega, T. Positions of Disulfide Bonds in Riboflavin-Binding Protein of Hen Egg White. J. Biochem. 101, 217–223 (1987).
- Shimada, Y., Sugihara, A., Tominaga, Y., Iizumi, T. & Tsunasawa, S. cDNA molecular cloning of Geotrichum candidum lipase. J. Biochem. 106, 383–388 (1989).
Additional Product Information
Please refer to the product’s Certificate of Analysis for detailed information on storage conditions, components, and technical specifications.
Kit Components Lists and Certificates of Analysis are available under the Documents tab.
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