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Lysyl EndopeptidaseR, Mass Spectrometry Grade (Lys-C)

for Proteome Research
Manufacturer :
FUJIFILM Wako Pure Chemical Corporation
Storage Condition :
Keep at -20 degrees C.
  • Structural Formula
  • Label
  • Packing
SDS
Comparison
Product Number
Package Size
Price
Inventory
Distributor
125-05061
Barcode No
4987481427648
20ug x5
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In stock

Distributor
121-05063
Barcode No
4548995075888
20ug
Inquire

In stock

Document

SDS ...all
Product Specification Sheet
Package Insert
Spectral Data
Certificate of Analysis
Calibration Certificate

Application

Comparison of In-gel Digestion using Trypsin (Tp), Lysl Endopeptidase (Lep) and Lep Combined with Tp (Lep + Tp)

BSA band (100 ng) resolved by SDS-PAGE was in-gel digested with Tp, Lep and Lep + Tp and analyzed by MALDI-TOFMAS. The figure shows the individual mass spectra. The evaluation of these peptidases is summarized in the table.

Mass spectrum using Tp and Tp + Lep
00062325_img01.png

When Tp is used concurrently with Lep, additional peaks were found around m/z 2000 compared to when only Tp is used. It shows that the recovery rate of peptide increases.

Table. Comparison ofTp, Lep, and Tp + Lep
Tp Lep Tp + Lep
Cleavage site C-terminal of Arg and Lys C-terminal of Lys C-terminal of Arg and Lys
Missed Cleavage(Rates of missed cleavage) Many
(8 %)
Very few
(0 %)
Few
(3 %)
Number of identified peptides 17 19 22

※The coverage (percentage of available peptides in the entire sequence) obtained by database search using a parameter setting of Missed Cleavage = 0 was subtracted from the coverage obtained by using a parameter setting of Missed Cleavage = 1.The value resulted from subtracting the coverage obtained when database searches were performed with Missed cleavage 0 from that obtained when performed with Missed cleavage 1. “Coverage” is the percentage of peptides obtained after in-gel digestion in the whole sequence.

These results indicate there are very few missed cleavages obtained by Lep digestion. When Tp is used concurrently with Lep, missed cleavages decrease and the number of identified peptides increase compared to when only Tp is used.

Data wasprovided by Dr. Y. Wada, Osaka Medical Center and Research Institute for Maternal and Child Health.

References

  1. Wada, Y. and Kadoya, M.:J. Mass Spectrom., 38, 117(2003).
  2. Shevchenko, A., Wilm, M., Vorm, O. and Mann, M.:Anal. Chem., 68, 850(1996).

Overview / Applications

Outline This product is for research use only. Do not administer it to human.

[BIOCHEMISTRY]

For Proteome Research!

Among the most important techniques in proteome analyses is the in-gel digestion of protein spots/bands that have been resolved by electrophoresis using digestive enzymes, such as trypsin and lysyl endopoptidase. Proteins can be identified by mass spectrometry analysis of the peptides produced by in-gel digestion, and further information regarding post-translational modifications can be obtained.Lysyl Endopeptidase, Mass Spectrometry Grade is a freeze dried product that retained sufficient activity for in-gel digestion and packed in very small quantities for convenience purposes.

[Features]

  1. High specificity and efficiency of protein digestion allow for easy database searches by peptide mass.
  2. Improved cleavage at lysine residue and increase in the number of peptides are obtained by combination with trypsin.
  3. Packed in very small quantities according to the amounts used so that sufficient activity for in-gel digestion may be retained.

[Related Products]

  • Wako Catalog #293-57701 Negative Gel Stain MS Kit, for Electrophoresis (20 tests)
  • Wako Catalog #299-58901 Silver Gel Stain MS Kit, for Electrophoresis (20 tests)

[Physical properties]

  • Appearance: Lyophilized form containing ca. 10% Tris-HCl buffer, pH 8.
  • Activity: Shown on each label
  • Molecular Weight: 27,000 (gel filtration); 30,000 (SDS electrophoresis)
  • Solubility: Soluble in water or buffer solution.
  • Stability: Stable at 4 degrees C, when dissolved in buffer of pH 5~12. Stable at 30 degrees C in the range of pH 6~11, but unstable at 50 degrees C or higher.
  • Optimal pH: 9.0 -9.5 (Amidase activity)
  • Isoelectric point: 6.9~7.0
  • Substrate specificity:
  • Hydrolysable substrate ... Tos-Lys-Ome, Bz-Lys-NH2, Bz-Lys-pNA, Lys-pNA Unhydrolysable substrate ... Bz-Arg-NH2, Bz-Arg-pNa, Arg-pNA
  • Inhibitors: DFP, PMSF, TLCK
[References]
  1. Wada, Y., and Kadoya, M.: J. Mass Spectrom., 38, 117 (2003).
  2. Shevchenko, A., Wilm, MM., Vorm, O., and Mann., M.: Anal. Chem., 68, 850 (1996).

Source: Bacteria


Originally, the source of this product was indicated as "Achromobacter lyticus" based on the physiological and morphological properties of the bacteria. However, we confirmed that the 16SrDNA sequence was highly homologous to that of Lysobacter

Property

Appearance Lyophilisate
Origin / Source Bacteria
Activity 0.03 - 0.07AU/vial

Manufacturer Information

Alias

  • Lys-C

For research use or further manufacturing use only. Not for use in diagnostic procedures.

Product content may differ from the actual image due to minor specification changes etc.

If the revision of product standards and packaging standards has been made, there is a case where the actual product specifications and images are different.

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