LolA Protein, E.coli (P.pastoris, His)

LolA Protein translocates lipoproteins from bacterial inner to outer membranes, forming a complex dependent on the absence of aspartate after the N-terminal cysteine. Aspartate signals lipoproteins to stay in the inner membrane. LolA, as a monomer, efficiently moves lipoproteins between bacterial membrane compartments. LolA Protein, E.coli (P.pastoris, His) is the recombinant E. coli-derived LolA protein, expressed by P. pastoris , with N-His labeled tag. The total length of LolA Protein, E.coli (P.pastoris, His) is 182 a.a., with molecular weight of ~22.3 kDa.

LolA Protein is involved in the translocation of lipoproteins from the inner membrane to the outer membrane in bacterial cells. It forms a complex with lipoproteins, but this interaction is contingent upon the absence of aspartate immediately following the N-terminal cysteine in the lipoprotein sequence. The presence of aspartate serves as a targeting signal, indicating that the lipoprotein should remain in the inner membrane. LolA functions as a monomer in facilitating the efficient movement of lipoproteins between bacterial membrane compartments.

E.coli

P. pastoris

N-His

A7ZYJ5 (22D-203K)

58350987

DAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKSQQNGAVDAAKFTFTPPQGVTVDDQRK

Approximately 22.3 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.