Problem with protein identification in 2D gel

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Problem with protein identification in 2D gel

Post by jocelyn85ang » Mon Jan 11, 2010 1:31 am


can someone please help me on this?

if we use IPG strip with pH 4-7 for my isoelectric focusing prior gel electrophoresis (in 2D), what will happen to the protein with pH more than 7? I mean, where will they (protein >7) migrate in 2D gel?

This is becasue, after running my 2D, I have always detected a transcitption regulator, whereby the protein is said to have pH more than 8. and it seems to be in many places in the gel throughout the 2D, and also with different MW...

I m puzzled cos the strip for IEF was pH 4-7, is it possible to isolate a protein of pH more than 7? and why is it scatted around the 2D gel?

I aprreatiate any input and suggestions . Thanking you in advanced


Last edited by jocelyn85ang on Mon Jan 11, 2010 12:54 pm, edited 1 time in total.

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Inland Taipan
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Post by JackBean » Mon Jan 11, 2010 8:48 am

What about some post-translational modifications? If it has different mass as well, maybe alternative splicing.

Cis or trans? That's what matters.

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