Skip to Content
Merck

Skip To

ENDOLYSS-RO

Roche

Endoproteinase Lys-C Sequencing Grade

from Lysobacter enzymogenes

Synonym(s):

lys-c, lysyl endopeptidase, protease

Sign In to View Organizational & Contract Pricing.

Select a Size

Change View
Size/SKUAvailabilityPrice
5 μg
Please contact Customer Service for Availability
1 960,00 kr
3 x 5 μg
Please contact Customer Service for Availability
5 270,00 kr

About This Item

UNSPSC Code:
12352204
EC Number:
NACRES:
NA.54
eCl@ss:
32160703
Specific activity:
≥200 units/mg protein (at 25 °C, with Chromozym PL)
Biological source:
bacterial (Lysobacter enzymogenes)

1 960,00 kr


Please contact Customer Service for Availability

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


biological source

bacterial (Lysobacter enzymogenes)

form

lyophilized

specific activity

≥200 units/mg protein (at 25 °C, with Chromozym PL)

mol wt

33 kDa by SDS-PAGE (reducing)

purified by

electrophoresis

packaging

pkg of 3 × 5 μg (11047825001), pkg of 5 μg (11420429001)

manufacturer/tradename

Roche

storage condition

(Keep container tightly closed in a dry and well-ventilated place.)

technique(s)

activity assay: suitable

color

white

optimum pH

8.5-8.8

pH range

5-12

solubility

water: soluble

suitability

suitable for enzyme test

UniProt accession no.

storage temp.

2-8°C

General description

Endoproteinase Lys-C Sequencing Grade is isolated from Lysobacter enzymogenes as a highly purified and specific protease. Endoproteinase Lys-C from Lysobacter enzymogenes is a member of the peptidase S1 family. It is mostly used for the initial fragmentation of polypeptide chains in protein sequence analysis.

Application

Use Endoproteinase Lys-C Sequencing Grade  for protein structure analysis and for sequence analysis. It is suitable to digest proteins in solution, in polyacrylamide gels or on blotting membranes.

Biochem/physiol Actions

This enzyme is a serine protease that specifically hydrolyzes amide, ester, and peptide bonds at the carboxylic side of Lys (in Tris-HCl buffer, pH 7.0 to 9.0).
Heat inactivation: Enzyme can be denatured using heat (5 min at 100 °C) or by TCA.

Preparation Note

Storage conditions (working solution): +2 to +8 °C
Lyophilized Endoproteinase Lys-C sequencing grade is reconstituted in 50 μl double-dist. water. This results in a buffer concentration of 50 mM Hepes, pH 8.0, 10 mM EDTA and 5 mg/ml raffinose. To avoid autolysis, the incubation temperature should not exceed 37 °C.
Stable in 4 M urea.

Other Notes

For life science research only. Not for use in diagnostic procedures.

Compare Similar Items

View Full Comparison

Show Differences

1 of 1

This Item
324715ENDOGLUSROENDOARGSRO
description

from Lysobacter enzymogenes

description

-

description

from Staphylococcus aureus V8

description

from Pseudomonas fragi

technique(s)

activity assay: suitable

technique(s)

protein mass spectrometry: suitable

technique(s)

-

technique(s)

-

specific activity

≥200 units/mg protein (at 25 °C, with Chromozym PL)

specific activity

≥200 units/mg protein

specific activity

≥15 units/mg protein

specific activity

≥20000 units/mg protein

biological source

bacterial (Lysobacter enzymogenes)

biological source

-

biological source

Staphylococcus aureus (V8)

biological source

-

suitability

suitable for enzyme test

suitability

-

suitability

-

suitability

-

form

lyophilized

form

lyophilized

form

lyophilized, lyophilized (salt-free)

form

lyophilized

optimum pH

8.5-8.8

optimum pH

-

optimum pH

4.0-7.8

optimum pH

7.0-8.0


Storage Class

11 - Combustible Solids

Flash Point (°F)

does not flash

Flash Point (°C)

does not flash

Pictograms

Health hazard

Signal Word

Warning

Hazard Codes

Precautionary Statements

Hazard Classifications

STOT RE 2

WGK

WGK 3



Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

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.

Already Own This Product?

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

Visit the Document Library