P3303
Endoproteinase Asp-N from Pseudomonas fragi mutant strain
suitable for protein sequencing, lyophilized powder
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About This Item
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grade
Proteomics Grade
Quality Level
form
lyophilized powder
analyte chemical class(es)
amino acids
packaging
vial of 2 μg
suitability
suitable for protein sequencing
storage temp.
2-8°C
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General description
Endoproteinase Asp-N is a metallo endoprotease. It is obtained from a mutant strain of Pseudomonas fragi, which hydrolyzes peptide bonds on the N-terminal side of aspartic and cysteic acid residues. Asp-N is used in proteomics for peptide mapping and protein sequence work due to its highly specific cleavage of peptides.
Application
Endoproteinase Asp-N from Pseudomonas fragi mutant strain has been used for the digestion of specific proteins to prepare peptides and for the analysis of generated peptides by MS (mass spectrometry) method.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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The Journal of biological chemistry, 270(23), 13777-13784 (1995-06-09)
Human immunodeficiency virus encodes the regulatory protein Rev, which is required for expression of viral structural proteins. It binds to an RNA element (RRE) in the viral transcript and up-regulates the cytoplasmic appearance of unspliced and singly spliced viral mRNA.
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Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs.
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Journal of Biochemistry, 134, 129-135 (2003)
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alpha-Synuclein is a component of the abnormal protein depositions in senile plaques and Lewy bodies of Alzheimer's disease (AD) and Parkinson's disease respectively. The protein was suggested to provide a possible nucleation centre for plaque formation in AD via selective
Sarah Murray et al.
Journal of virology, 80(12), 6171-6176 (2006-05-30)
Adeno-associated virus type 2 (AAV-2) capsid proteins have eight sequence motifs that are potential sites for O- or N-linked glycosylation. Three are in prominent surface locations, close to the sites of cellular receptor attachment and to neutralizing epitopes on or
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