ENDOSTATIN

GWB-FA3CC0

The monoclonal antibody 1837-46 can be used for Western blotting. flow cytometry and immunohistology on both frozen and paraffin sections. Furthermore the monoclonal antibody 1837-46 is useful as detector in immuno assays. Monoclonal antibody 1837-46 reacts with endostatin. a 20 kDa C-terminal fragment of collagen XVIII. Endostatin is able to evoke non-uniform response for proliferation. cell mount and migration of entothelial cells. with different endostatin binding characteristic. leads to the assumption that endostatin effect is strongly dependent from endothelial cell type. Furthermore endostatin inhibits angiogenesis and tumor growth in vivo by inducing apoptosis in endothelial cells. The local delivery of endostatin seems to specifically affect tumor-associated microvessels by reduction of the vessel density. diameter and functionality. Tumor cell migration and invasion was greatly reduced in the endostatin treated animals. Endostatin is non-toxic and does not induce acquired drug resistance and has therefore become a potent new therapy strategy in solid neoplasias. This therapy appear to have high potential not only for the treatment of gliomas. the most common brain tumours. but also of other tumours. The ability of endostatin to inhibit neoangiogenesis is mediated. at least in part. by Zn2+ binding and elastase processing. Widespread endostatin expression was found in elastic fibers in vessel walls and in some other basement membrane zones. Endostatin is released by neurons to accumulate in amyloid plaques in Alzheimer\' s disease.

Expressed in liver kidney lung skeletal muscle and testis.

Belongs to the multiplexin collagen family.

Contains 1 TSP N-terminal (TSPN) domain. [1] Jia S. Zhu F. Li H. He F. and Xiu R. et al. Anticancer treatment of endostatin gene therapy by targeting tumor neovasculature in C57/BL mice[2] Jia S. Zhu F. Xing G. Yu Y. Duan C. Xiu R. -J. and He F. et al. Anticancer treatment of targeted fusion protein delivery to tumor neovasculature[3] Jia S. Zhu F. Xing G. Yu Y. Duan C. Xiu R. -J. and He F. et al. Direct Submission[4] Rehn M. V. Hintikka E. Pihlajaniemi T. Primary structure of the alpha 1 chain of mouse type XVIII collagen partial structure of the corresponding gene and comparison of the alpha 1(XVIII) chain with its homologue the alpha 1(XV) collagen chain. [5] Rehn M. Hintikka E. Pihlajaniemi T. Characterization of the mouse gene for the alpha-1 chain of type XVIII collagen (COL18A1) reveals that the three variant N-terminal polypeptide forms are transcribed from two widely separated promoters. [6] Rehn M. V. Pihlajaniemi T. Alpha 1(XVIII) a collagen chain with frequent interruptions in the collagenous sequence a distinct tissue distribution and homology with type XV collagen. [7] Carninci P. Kasukawa T. Katayama S. Gough J. Frith M. C. Maeda N. Oyama R. Ravasi T. Lenhard B. Wells C. et al. The transcriptional landscape of the mammalian genome. [8] Rehn M. Pihlajaniemi T. Identification of three N-terminal ends of type XVIII collagen chains and tissue-specific differences in the expression of the corresponding transcripts. The longest form contains a novel motif homologous to rat and Drosophila frizzled proteins. [9] Oh S. P. Kamagata Y. Muragaki Y. Timmons S. Ooshima A. Olsen B. R. Isolation and sequencing of cDNAs for proteins with multiple domains of Gly-Xaa-Yaa repeats identify a distinct family of collagenous proteins. [10] Abe N. Muragaki Y. Yoshioka H. Inoue H. Ninomiya Y. Identification of a novel collagen chain represented by extensive interruptions in the triple-helical region.