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

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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P6181A3352EMS0006
vibrant-m

EMS0006

Recombinant Trypsin

suitability

suitable for protein sequencing

suitability

suitable for protein sequencing

suitability

-

suitability

suitable for , suitable for mass spectrometry

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

form

lyophilized powder

form

lyophilized powder

form

powder

form

lyophilized powder

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

analyte chemical class(es)

amino acids

analyte chemical class(es)

amino acids

analyte chemical class(es)

-

analyte chemical class(es)

-

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

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_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1).
Bienkiewicz EA, et al.
Biochemistry, 41, 752-752 (2002)
S R Paik et al.
The Biochemical journal, 340 ( Pt 3), 821-828 (1999-06-09)
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
Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs.
Kameoka D, et al.
Journal of Biochemistry, 134, 129-135 (2003)
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
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)

Protocols

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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