Rabbit Anti-C3 Recombinant Antibody (clone BA8) (CAT#: FAMAB-0160JF)

Figure 1 Coomassie blue staining of purified halibut (Ha) C3 under reducing conditions (lanes 2 and 3).

Human (Hu) C3 is used as a standard (lane 1) and the specificity of the anti-halibut C3 b-chain antibody tested on halibut serum in western blotting.

Lange, S., Bambir, S., Dodds, A. W., & Magnadóttir, B. (2004). An immunohistochemical study on complement component C3 in juvenile Atlantic halibut (Hippoglossus hippoglossus L.). Developmental & Comparative Immunology, 28(6), 593-601.

Figure 2 Immunohistochemical detection of C3 in different organs of halibut from the age of 37 until 10508 d p.h.

A positive response in the skeletal muscle fibres (striated muscle). The magnification is 40 ×.

Lange, S., Bambir, S., Dodds, A. W., & Magnadóttir, B. (2004). An immunohistochemical study on complement component C3 in juvenile Atlantic halibut (Hippoglossus hippoglossus L.). Developmental & Comparative Immunology, 28(6), 593-601.

Figure 3 Standards curves, obtained by CIF-ELISA, anti-C3 ELISA and C1q-ELISA, when twofold dilution of AGH were tested.

The data represent the mean of 3 experiments ± SD.

Stanilova, S. A., & Slavov, E. S. (2001). Comparative study of circulating immune complexes quantity detection by three assays—CIF-ELISA, C1q-ELISA and anti-C3 ELISA. Journal of immunological methods, 253(1-2), 13-21.

Figure 4 Flow cytometric analysis of selected mAb binding to C3 fragments fixed on B cells.

Splenocytes were incubated in autologous fresh mouse serum (shaded histogram) or EDTA-complemented serum (thick lines) to allow deposition of C3 on the cells.

Mastellos, D., Prechl, J., László, G., Papp, K., Oláh, E., Argyropoulos, E., ... & Erdei, A. (2004). Novel monoclonal antibodies against mouse C3 interfering with complement activation: description of fine specificity and applications to various immunoassays. Molecular immunology, 40(16), 1213-1221.