SDS-PAGE of P35 Protein. Lane 1: Molecular Weight Marker. Lane 2: P35 Protein. Load: 10 µl. Predicted/Observed size: 69.5 kDa fusion protein, 27.1 kDa for P35, 42.4 kDa for MBP alone.
SDS-PAGE of P35 Protein. Lane 1: Molecular Weight Marker. Lane 2: P35 Protein. Load: 10 µl. Predicted/Observed size: 69.5 kDa fusion protein, 27.1 kDa for P35, 42.4 kDa for MBP alone.
Recombinant Borrelia burgdorferi P35 protein, fused to an MBP-tag and produced in E. coli (>90% purity).
P35 protein is produced by the spirochete B. burgdorferi, which is carried by Ixodes ticks. Strain B31 is the type strain (ATCC 35210) for this organism and was derived by limited dilutional cloning from the original Lyme-disease tick isolate obtained by A. Barbour (Johnson, et al., 1984). The bba64 gene of B. burgdorferi encodes a surface-exposed 35-kDa antigen which has been shown to be a statistically significant marker in IgG immunoblots in a study of patients with early Lyme disease who presented with erythema migrans (Fikrig, et al., 1997).
P35 expression is induced in the tick vector during feeding and maintained during infection of the vertebrate host. The expression of a majority of the proteins expressed in early Lyme disease is affected by pH, being abundantly expressed at pH 7.0 (resembling the tick mid-gut pH of 6.8 during feeding) but only sparsely at pH 8.0 (a condition closer to that of the unfed tick mid-gut pH of 7.4) and the encoding genes may be coregulated (Gilmore Jr, et al., 2010). Borrelia may also change its antigenic composition in its need for adaptation to stresses imposed by changes in conditions from cycling between its arthropod and mammalian hosts (Fikrig, et al., 1997).
The expression of bba64 is down-regulated in the absence of RpoS which has also been shown to be the sole determinant of differential bba64 expression in cultured spirochetes. P35 expression in B. burgdorferi is upregulated in the stationary growth phase, and influenced by a temperature of 34°C (but not 24°C) (Gautam, et al., 2008).
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