Hi there,

The behavior of your protein is dependent on the pH at which you are working. When pHpI it is negative (anion).

Hello dear, it can be determined by zeta potential mearuments.

Hi there,

The behavior of your protein is dependent on the pH at which you are working. When pHpI it is negative (anion).

Sequence based prediction can be done at numerous sites. e.g. http://protcalc.sourceforge.net/

Hi,

The charge will be dependent upon the buffer/solution pH that the protein is contained within. However, if you want to shortcut that, use a sequence based calculator as Karthik Rajasekar has provided a link for (http://protcalc.sourceforge.net/).

You can do native PAGE to determine whether it is basic (positively charged) or acidic  (negatively charged). If your protein enters on acidic page , then your protein is positive or if it enters basic page it is negative 

Cationic means that it is positively charged with negative counter ions while anionic means the opposite.  Since you provided the pI then you likely know its meaning and may rather be asking another question such as what may be a subsequent purification scheme?  

Use an online parameter calculator as mentioned above by a few others. I use http://web.expasy.org/protparam/

Then, it depends on your protein's pI (see Dr. Liger above). Then you can tweak your buffer pH to your own desire (within reason, of course). If you want to see how it effects your protein, you could run it over an anion- or cation-exchange column to do some coarse characterization. 

You can determine experimental. Electroforesis is a useful. Your ions's ionic characteristics must be stable during the test. travel of ions depend un viscosity. You can add dilutants for icreasing diffusion coefficient of media.

Also you can take information and use lab. facility in hematology services of hospitals.

You cannot calculate protein charge. Unfortunately, a number of biochemistry texts have suggested that charge may be determined from the pI. This simply is not so. Proteins bind monovalent ions (anions to a greater extent than cations), which alters their charge. At the moment, there are no programs, regardless of their sophistication or other virtues, that come close. A quick example- if you determine the pIs of freshly prepared human serum IgGs, they range from less than 4 to greater than 10. Yet, under physiological conditions all IgGs have a charge near -6.3. If you put IgGs in pH 6 solvent (formulation conditions for mAbs), the charge is "off" from the calculated values by ~20; at pH 5, it is off by ~50, at pH 3 it is off by ~100.

Charge may be measured accurately and quickly, and it must (at this point) be measured, not calculated.

you have to check the PI (whole PH)of your protein, and if more than 8.0 that is mean negative charge and will be run faster on the gel.