You can usually tell if it is in inclusion body because they do not dissolve in detergent.  A membrane bound protein should wash away when you dissolve the membrane.  (Still, some may be in membrane and some in inclusion body... it doesn't have to be one or the other).

To make inclusion bodies, I lyse cells in 50 mM Tris-HCl (pH 8.0), 1 mM EDTA (pH 8.0), 0.01% sodium azide, 1 mM DTT, 200 mM sodium chloride, 1.0% sodium deoxycholate, and 1.0% Triton X-100. Then was away membranes with wash buffer: 50 mM Tris-HCl (pH 8.0), 1 mM EDTA (pH 8.0), 0.01% sodium azide, 1 mM DTT, 100 mM sodium chloride, and 0.5% Triton X-100. I sonicate to resuspend in wash buffer and do at least 3 washes. Centrifuge 6000 x G for 30 minutes to pellet after each wash. No amount of washing will dissolve inclusion bodies.  

Did you express your protein with a His tag from the vector?  If you did then you could test for the His tag by western blot using Rabbit anti-6His HRP (cat number A190-114P from BETHYL Labs Inc).  First, dissolve some inclusion body pellet in 8M Urea, dilute 1:10 in SDS-PAGE loading dye with reducing agent, heat sample, run gel, transfer  to PVDF membrane for western blot, and develop with ECL reagent (for example GE Healthcare RPN2232). Use a 6His protein ladder as a marker for the blot(Qiagen number 34705). If a tag lights up in the inclusion body sample then at least some of your protein is there. 

Thanks a lot! I Will try this out

Dr Nelson has given all you need. In addition to it I wish to tell, you can try various different strategies if the said protocol doesn't work (as it happens in certain cases).  Urea, Guanidine Hydrochloride, high pH etc are few among them. For help try to check papers by Dr.Amulya Panda.