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P3303

Asp-N Protease

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

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A propos de cet article

Numéro CAS:
Numéro CE :
UNSPSC Code:
12352204
NACRES:
NA.56
EC Number:
232-642-4
MDL number:
eCl@ss:
32160410
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Nom du produit

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

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

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.


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Health hazardExclamation mark

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Danger

Hazard Classifications

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

target_organs

Respiratory system

Classe de stockage

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



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Protocoles

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).


T H Jensen et al.
The Journal of biological chemistry, 270(23), 13777-13784 (1995-06-09)
Human immunodeficiency virus encodes the regulatory protein Rev, which is required for expression of viral structural proteins. It binds to an RNA element (RRE) in the viral transcript and up-regulates the cytoplasmic appearance of unspliced and singly spliced viral mRNA.
Wilson KJ, et al.
Methods in Protein Sequence Analysis: Proceedings of the 7th International Conference, Berlin, July 3?8, 1988, 310-310 (1988)
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)



Numéro d'article de commerce international

RéférenceGTIN
P3303-1VL04061834367659