Skip to Content
Merck

P3303

Asp-N Protease

Cleaves N-terminal to aspartic acid residues, suitable for Mass Spectrometry, from Pseudomonas fragi mutant strain

Sign In to View Organizational & Contract Pricing.

Select a Size

About This Item

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

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

Endoproteinase Asp-N from Pseudomonas fragi mutant strain, suitable for protein sequencing, lyophilized powder

grade

Proteomics Grade

form

lyophilized powder

analyte chemical class(es)

amino acids

packaging

vial of 2 μg

suitability

suitable for protein sequencing

storage temp.

2-8°C

Quality Level

200

Looking for similar products? Visit Product Comparison Guide

Related Categories

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.

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.

pictograms

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
0000500467
0000500467
0000498468
0000498468
0000474316

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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)
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
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
View All Related Papers

Related Content

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service