Protocol Online logo
Top : Forum Archives: : Protein and Proteomics

N-ethylmaleimide handling - (Jun/26/2006 )

Hi everybody. Does anybody here use N-ethylmaleimide (for stabilization of SUMO conjugates)? How do you normally use it? Ethanol stock, fresh powder directly into batch of lysis buffer,...? Which concentration (I´ve seen 1mM to 20mM for very similar approaches!!)? Data sheet from Sigma recomends dilution to 50mg/ml (aprox. 400mM) in ethanol for storage, but that means 400mM, just 20x stock in ethanol for some protocols. Is that correct?
Thanks in advance!

Miguelon

-miguelon-

How does it exactly stabilize SUMO-conjugates? Does it work also for Nedd8-conjugates?

-dnafactory-

QUOTE (dnafactory @ Jun 26 2006, 06:14 PM)
How does it exactly stabilize SUMO-conjugates? Does it work also for Nedd8-conjugates?


It´s supposed to inhibit, as part of its broad enzime inhibitor role, specific sterases that very efficiently would cleave SUMO from the target protein in native conditions.

I don´t know whether it works for "Nedd"ylation studies as well, but that inhibitor effect of NEM is supposed to be broad. Is Nedd8 conjugation as labile as SUMOylation?

-miguelon-

Thanks, I think it should interfere also with the de-Neddylation of proteins.

-dnafactory-

hello,

NEM acts to stabilize SUMO conjugates by covalently modifying the sulfhydryl group of the catalytic cysteine on SUMO-specific proteases (as well as pretty much any other reduced cysteine it has access to).

as for preparing it, I've always just made a fresh 1M stock (no need to make a bunch) in 95% ethanol for each exctraction. various groups use different concentrations of NEM in their buffers (ranging from 2 to 20mM). i've had good luck with 20mM.

if you're going to perform mass spec analysis on your NEM-treated samples, be sure to let include that in the searches, as some of your Cys residues will be alkylated w/ NEM and others w/ IAA.

-johanski-

QUOTE (johanski @ Jun 27 2006, 10:47 PM)
hello,

NEM acts to stabilize SUMO conjugates by covalently modifying the sulfhydryl group of the catalytic cysteine on SUMO-specific proteases (as well as pretty much any other reduced cysteine it has access to).

as for preparing it, I've always just made a fresh 1M stock (no need to make a bunch) in 95% ethanol for each exctraction. various groups use different concentrations of NEM in their buffers (ranging from 2 to 20mM). i've had good luck with 20mM.

if you're going to perform mass spec analysis on your NEM-treated samples, be sure to let include that in the searches, as some of your Cys residues will be alkylated w/ NEM and others w/ IAA.


Thanks!!

-miguelon-