P3303

Sigma-Aldrich

Endoproteinase Asp-N from Pseudomonas fragi mutant strain

suitable for protein sequencing, lyophilized powder

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.56

form

lyophilized powder

Quality Level

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.

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Target Organs

Respiratory system

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

C E Wobus et al.
The Journal of general virology, 79 ( Pt 8), 2023-2025 (1998-08-26)
The amino acid sequence of the genome-linked viral protein (VPg) of pea enation mosaic enamovirus (PEMV) has been determined. The VPg is encoded by nt 1811-1894 within ORF1 of RNA1 downstream of the proteinase motif. Direct N terminus sequencing of...
Human and murine class I MHC antigens share conserved serine 335, the site of HLA phosphorylation in vivo.
Guild BC and Strominger JL
The Journal of Biological Chemistry, 259, 9235-9235 (1984)
W Sun et al.
Proceedings of the National Academy of Sciences of the United States of America, 91(24), 11462-11466 (1994-11-22)
Endoproteinase Asp-N cleaves the 581-amino acid Escherichia coli primase (65,564 Da) into several major fragments. One of these, a 47-kDa fragment containing the complete N terminus and the first 422 amino acids of primase, is capable of primer RNA (pRNA)...
Takatoshi Ohkuri et al.
Journal of biochemistry, 154(4), 333-340 (2013-07-16)
A method was previously established for evaluating Asn deamidation by matrix-assisted laser desorption/ionization time of flight-mass spectrometry using endoproteinase Asp-N. In this study, we demonstrated that this method could be applied to the identification of the deamidation site of the...
Yan Wang et al.
Protein science : a publication of the Protein Society, 15(1), 122-134 (2005-12-03)
The identification of surface-exposed components of the major outer membrane protein (MOMP) of Chlamydia is critical for modeling its three-dimensional structure, as well as for understanding the role of MOMP in the pathogenesis of Chlamydia-related diseases. MOMP contains four variable...

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