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Home > Products >  Recombinant lysine endopeptidase (Lys-C)

Recombinant lysine endopeptidase (Lys-C) CAS NO.72561-05-8

  • Min.Order: 100 Milligram
  • Payment Terms: T/T,MoneyGram
  • Product Details

Keywords

  • Recombinant lysine endopeptidase
  • Lys-C
  • lysine endopeptidase

Quick Details

  • ProName: Recombinant lysine endopeptidase (Lys-...
  • CasNo: 72561-05-8
  • Appearance: white or similar white freeze-dried po...
  • Application: Used for the production of biological ...
  • DeliveryTime: negotiatale
  • PackAge: vial
  • ProductionCapacity: 1000 Gram/Month
  • Purity: >99%
  • Storage: The lyophilized powder of this product...
  • Transportation: freight
  • LimitNum: 100 Milligram

Superiority

Animal origin free: Recombinant production, no exogenous virus contamination. No animal-derived material is used during production.

Stable quality: stable and continuous batch production can be guaranteed; T here is no difference between product batches and the quality is stable. High purity: no any other contaminated proteases, non- specific cutting sites.

Compliance with regulatory requirements: The production equipment and production environment comply with relevant regulatory requirements, and the production process is in full compliance with the NSF ISO 9001:2015 quality system and in accordance with GMP guidelines.

Complete quality documentation: Relevant regulatory support documents are available upon request.

 

 

Details

I. Product introduction

Lysyl Endopeptidase (EC 3.4.21.50) belongs to a serine protease that specifically cleaves peptide bonds at the carboxy terminus of lysine residues. Lysyl endo-enzyme can be widely used in various biotechnological processes, such as: proteolysis to produce peptides; proteolysis; GLP-1 drug preparation.The optimum reaction pH was 9.0~9.5, and the isoelectric point was pH 6.9~7.0.The optimum reaction temperature was 30~37℃, and the stability decreased above 50℃.The stability of this enzyme was good. After incubation in 4mol/L urea or 0.2%SDS solution at 30℃ for 6h, the biological activity did not decrease.Biological activity was inhibited by DFP, PMSF and TLCK.

 

II. Product characteristics

Source: E. coli

Character: white or off-white lyophilized powder

Specific activity: ≥1AU/mg Pro

Purity (SDS-PAGE) : single main band

Specificity: specific cleavage of lysine residues

 

III. Product use

Used for the production of biological products, such as insulin and analog production, GLP-1 analogue production; protein mass spectrometry, sequencing, peptide mapping analysis; production of small molecular proteins or peptides etc.

 

Iv. Recommend Usage

It is recommended to use 20-50mM Tris HCl, pH 8.5-9.5 system, enzyme: fusion protein = 1-100au: 1g, optimal pH 9.0-10.0, optimal temperature 25-37 ℃, reaction time 2-24h. After dissolving, repackage and store under - 15 ℃.Inorganic salts above 0.1M have a certain effect on the enzyme activity, and it is recommended to carry out the enzyme digestion reaction after desalting. If it is not possible to desalinate, it is recommended to increase the amount of enzyme and extend the digestion time.

 

V. Storage stability

The lyophilized powder of this product can be stably stored for at least 24 months at -15℃. When the Tris-HCl buffer was formulated into an enzyme solution, it can store at -20 ℃ for 5 times without loss of activity.

 

Vi. Product advantages

Animal origin free: Recombinant production, no exogenous virus contamination. No animal-derived material is used during production.

Stable quality: stable and continuous batch production can be guaranteed; T here is no difference between product batches and the quality is stable. High purity: no any other contaminated proteases, non- specific cutting sites.

Compliance with regulatory requirements: The production equipment and production environment comply with relevant regulatory requirements, and the production process is in full compliance with the NSF ISO 9001:2015 quality system and in accordance with GMP guidelines.

Complete quality documentation: Relevant regulatory support documents are available upon request.

 

 

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