In article <487k1d$qdc at biovax.biobase.dk>, kjaer at biobase.dk (Svend Kjaer) writes:
>Currently, I'm doing western blots using a phage displayed pool of scFv's
>as the primary antibody. I test against the protein, that the phage were
>selected against in the first place and to check specificity, also against
>a bacterial cytosolic extract from the E.coli strain, TG-1.
>What I see after development is a pattern of 11 proteins in the extract
> recognized by the phage added. They are from 14 kDa to 40 kDa in size.
> They are not a result of crossreactivity from the scFv's as they also appear
> when I use helper phage as a negative control. It must then be a specific
>interaction between the phage-body and some bacterial proteins.
>>I know that thioredoxin is known to interact with the phage particle during
>the assembly process, but I was wondering if anyone could help me with
>other possible candidates for such interactions.
>>References would be appreciated