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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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1 VIAL
CHF 287.00

CHF 287.00


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1 VIAL
CHF 287.00

About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.56

CHF 287.00


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Grado

Proteomics Grade

Livello qualitativo

Stato

lyophilized powder

Classi chimiche degli analiti

amino acids

Confezionamento

vial of 2 μg

Compatibilità

suitable for protein sequencing

Temperatura di conservazione

2-8°C

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Descrizione generale

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.[1][2] Asp-N is used in proteomics for peptide mapping and protein sequence work due to its highly specific cleavage of peptides.[3][4]

Applicazioni

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.[5][6][7]

Pittogrammi

Health hazardExclamation mark

Avvertenze

Danger

Indicazioni di pericolo

Classi di pericolo

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

Organi bersaglio

Respiratory system

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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


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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
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)
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

Protocolli

An optimized LC-MS/MS based workflow for low artifact tryptic digestion and peptide mapping of monoclonal antibody, adalimumab (Humira) using filter assisted sample preparation (FASP).

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