Endoproteinase Asp-N  (Synonyms: Asp-N)

Endoproteinase Asp-N (Asp-N) is a metalloprotease that can specifically cleave the N-terminal side of aspartyl and cysteic acid residues^[1].

Product Information
Asp-N protease is a recombinantly expressed metalloprotease derived from Pseudomonas fragi bacteria, with a molecular weight of 22.4 kDa and optimal activity at pH 7.5-8.5. The product contains trehalose and Tris-HCl and can be used for protein sequencing characterization and proteomics research.

Instructions
1. Reconstitution: It can be reconstituted with 20 μL ultrapure water (1 mg/mL). After dissolution, it can be divided and stored at -20℃ to avoid repeated freezing and thawing. It can be stored for 1-2 weeks.
2. Enzyme cleavage
1) Applicable enzyme cleavage buffer solution: 20 mmol Tris, 50 mmol HEPES buffer; pH value is in the range of 7.5-8.5
2) Reaction conditions: 1:10-1:50 (w/w, enzyme: denatured protein sample), the protein concentration of the enzyme cleavage reaction is controlled at 0.2-0.5 μg/μL, incubated at 37℃ for 2 h.

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

55576-49-3

Solid

White to off-white

[Endoproteinase Asp-N]

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Ingrosso D, et, al. Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins. Biochem Biophys Res Commun. 1989 Aug 15;162(3):1528-34.  [Content Brief]

  [2]. Grillon C, et, al. Involvement of thymosin beta 4 and endoproteinase Asp-N in the biosynthesis of the tetrapeptide AcSerAspLysPro a regulator of the hematopoietic system. FEBS Lett. 1990 Nov 12;274(1-2):30-4.  [Content Brief]