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P3303

Sigma-Aldrich

Endoproteinase Asp-N from Pseudomonas fragi mutant strain

suitable for protein sequencing, lyophilized powder

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About This Item

CAS Number:
9001-92-7
Enzyme Commission number:
3.4.24.33 (BRENDA, IUBMB)
EC Number:
232-642-4
MDL number:
MFCD02253021
UNSPSC Code:
12352204
NACRES:
NA.56

grade

Proteomics Grade

Quality Level

200

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.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

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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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
Insights into the molecular mechanisms of protein platination from a case study: the reaction of anticancer platinum(II) iminoethers with horse heart cytochrome c.
Casini A, et al.
Biochemistry, 46, 12220-12220 (2007)
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
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)
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