小中大不同公司的抗体的表位不一样,分子量你可以参考文献或者理论分子量,一般翻译后修饰会分子量变化,如果同一个膜上面做出来不一样,那就比较麻烦,你可以具体把两个公司的抗体链接发上来看看
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Why is the actual band size different from the predicted?
Western blotting is a technique that separates proteins based on size - in general, the smaller the protein the faster it migrates through the gel. However, migration is also affected by other factors and so the actual band size observed may differ from that predicted. Common factors include...
post-translational modification - e.g. phosphorylation, glycosylation etc which increases the size of the protein
post-translation cleavage - e.g. many proteins are synthesized as pro-proteins, and then cleaved to give the active form, e.g. pro-caspases
splice variants - alternative splicing may create different sized proteins from the same gene
relative charge - the composition of amino acids (charged vs non-charged)
multimers - e.g. dimerisation of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands