MBS Offers 5 Clones Recognizing Human Osteopontin

Osteopontin (OPN) is a well-characterized secreted protein found in the circulation and is emerging as a potential biomarker for many cancers. Maine Biotechnology Services, Inc.(MBS), in collaboration with Maine Medical Center Research Institute (MMCRI) and the University of Southern Maine (USM), developed five anti-human OPN monoclonal Antibodies.  An article appeared recently in The Oncologist further validating Osteopontin as an emerging cancer biomarker. 

MAB193P Monoclonal Antibody to Osteopontin N-Terminal
MAB194P Monoclonal Antibody to Osteopontin N-Terminal
MAB195P Monoclonal Antibody to Osteopontin N-Terminal
MAB196P Monoclonal Antibody to Osteopontin N-Terminal
MAB197P Monoclonal Antibody to Osteopontin C-Terminal

An ELISA was performed using the human N-terminal (aa-1-166) or C-terminal (aa167-314) human recombinant fragments. 2C5, 2H9, 2F10, and 2E11 recognize OPN epitopes on the N-terminal fragment, while 1F11 recognizes an epitope on the C-terminal fragment All 5 clones recognize fl-OPN. (2)

Recognition of Native OPN

 A) Human milk OPN was used in ELISA, and 1F11 and 2F10 binding compared to an irrelevant antibody (MAb 1E3, control). B) Whole kidney lysates were collected from wild type (WT) mice, OPN heterozygous mice (Het), and OPN null mutant mice (Null). Lysates were loaded equally and analyzed by SDS-PAGE followed by immunoblotting using 1F11. Recombinant OPN was used as a control. C) Human aortic smooth muscle cells (SMC) were transduced with activated Notch1 receptor (2) to increase OPN expression, and compared to human umbilical vein endothelial cells (EC). Both 2F10 and 1F11 recognize OPN in SMC.

 Contact Sales@mainebiotechnology.com today to order!

Categorical meta-analysis of Osteopontin as a clinical cancer marker

References

(1)Alicia Plumer, Hongyi Duan, Sripriya Subramaniam, F Lee Lucas, Susan Miesfeldt, Ah-Kau Ng, Lucy Liaw Development of fragment specific osteopontin antibodies and ELISA for quantification in human metastatic breast cancer BMC Cancer 2008, 8:38 (31 January 2008)

(2)Christensen B, Nielsen MS, Haselmann KF, Petersen TE, Sorensen ES: Posttranslationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications. Biochem J 2005, 390(Pt 1):285-292.