Endoproteinase Asp-N, Sequencing grade

for Biochemistry

Manufacturer :: FUJIFILM Wako Pure Chemical Corporation

Storage Condition :: Keep at 2-10 degrees C.

CAS RN^® :: 9001-92-7

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Comparison	Product Number	Package Size	Price	Inventory
	Distributor 056-05921 Barcode No 4987481265349	2ug	List Price 175.00 USD	In stock	Certificate of Analysis

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Product Specification Sheet

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Overview / Applications

Outline	<Protein Engineering><Amino Acid Sequencing Analysis Reagent><Enzyme for sequence analysis>Cleavage of polypeptide chains by protease is performed under a mild condition and, therefore, modification (oxidation, halogenation, deamidation, etc.) of side-chain amino acid residues does not occur, and peptides containing the groups (binding sites in carbohydrate chains, lipids, phosphate, sulfuric acid, etc.) for modification are usually recovered in a complete form at a good yield. Segments with good reproducibility can be obtained under identical conditions of digestion. Highly substrate-specific enzymes are used for the primary structure analysis of proteins, because it is possible to roughly predict the number of fragments and their average sizes from amino-acid composition, and more importantly, because it is possible to avoid complex isolation due to partial (nonspecific) cleavages.This enzyme specifically cleaves the N-terminal end of aspartic acid residue in proteins and peptides.The solution after preparation should be stored -20 degrees centigrade.Specificity: Reaction rate after 1 hour using glucagon as a substrate: min 90%

Outline

<Protein Engineering><Amino Acid Sequencing Analysis Reagent><Enzyme for sequence analysis>Cleavage of polypeptide chains by protease is performed under a mild condition and, therefore, modification (oxidation, halogenation, deamidation, etc.) of side-chain amino acid residues does not occur, and peptides containing the groups (binding sites in carbohydrate chains, lipids, phosphate, sulfuric acid, etc.) for modification are usually recovered in a complete form at a good yield. Segments with good reproducibility can be obtained under identical conditions of digestion. Highly substrate-specific enzymes are used for the primary structure analysis of proteins, because it is possible to roughly predict the number of fragments and their average sizes from amino-acid composition, and more importantly, because it is possible to avoid complex isolation due to partial (nonspecific) cleavages.This enzyme specifically cleaves the N-terminal end of aspartic acid residue in proteins and peptides.The solution after preparation should be stored -20 degrees centigrade.Specificity: Reaction rate after 1 hour using glucagon as a substrate: min 90%

Property

Appearance	Lyophilisate
Origin / Source	Pseudomonas fragi mutant
Activity	Specific activity : min.20000units/mg protein
Purity	min. 90 % (SDS-PAGE)

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For research use or further manufacturing use only. Not for use in diagnostic procedures.

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