Bit of a specialist question.
Most commercial vendors info tells you if their antibody works on western blots or for immunohistochemistry or for immunocytochemistry.
Why should any antibody work for one of the above but not for all?
What properties of the antibody cause this difference in efficiency in various applications?
2006-09-29 09:38:19 · 2 answers · asked by the last ninja 6 in Science & Mathematics ➔ Biology
It isnt so much the antibody, its the epitope that it is made to. If the epitope is denatured from formalin fixation or methanol, it could assume a non-natural tertiary structure and only be recognized in some instances. It is even more specific than saying IHC or wester or IF, it can come down to fixation time and method. For instance some of my antibodies will work with 10%PBF fixation (4deg on), but NOT with 4% paraformaldehyde, or if I overfix in PBF. With denaturing gels you have another layer of denaturation built in as well.
2006-09-29 10:21:36 · answer #1 · answered by Anonymous · 2⤊ 0⤋
See? See? This is the monster I fear so greatly! I like to think I'm a somewhat intelligent person. Then I venture in here and I start to stutter. I start to sweat. I read the question and feel like a kid who forgot to do her homework last night. *sigh* How do I get past this monster without disappearing into the deep dark hole of nothingness?
But I would venture to say that it would depend on the strain of bacteria that is being fought. And wouldn't that definitely vary from place to place? (just a thought) *shrugs* As foar as what properties of the antibody cause this........? **runs to the library to find out**
2006-10-01 12:01:47 · answer #2 · answered by Marianne not Ginger™ 7 · 0⤊ 0⤋