- 商品介绍
- 规格参数
- 包装参数
General description
Recombinant His tag Achromobacter lyticus Lys-c (lysyl-endopeptidase) (206-473aa) was expressed in E.coli cells.
Overview
Lysyl-endopeptidase (Lys-c) was isolated from the Gram-negative soil bacterium Achromobacter lyticus by Msaki et al. The protein hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues making it an important tool for enzymatic protein sequencing and Lys-X compound synthesis.
Application
The enzyme functions optimally between 30-37 °C and suffers from degradation when subjected to temperatures above 50 °C. Lysyl-endopeptidase retains complete activity after incubation in 4M urea or in 0.1% SDS solution for up to 6 hours at 30 °C.
Biochem/physiol Actions
This enzyme hydrolyzes amide and peptide ester bonds at the carboxylic side of lysine and S-aminoethylcysteine residues, at a catalytic pH range of 9.0-9.5, catalytic temperature range of 30-37 °C.
Packaging
1mg/ml in Plastic
Preparation Note
Catalytic pH range 9.0-9.5. Catalytic temperature range 30-37 °C.
Store product at -20°C for up to one year. Avoid freeze/thaw cycles.
Other Notes
For R&D only.
| biological source | Achromobacter lyticus |
| Quality Segment | 100,200 |
| recombinant | expressed in E. coli (206-473aa) |
| grade | Proteomics Grade |
| form | ready-to-use solution |
| concentration | 1 mg/mL |
| optimum pH | 8.5 |
| pH range | 9.0-9.5(catalytic) |
| UniProt accession no. | P15636 |
| shipped in | dry ice |
| storage temp. | −20°C |
| 长度(mm) | |
| 宽度(mm) | |
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| 重量(kg) |




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