MBTPS2 ANTIBODY

Source

Rabbit

Reactivity

Mouse

Background

Membrane-bound transcription factor protease site 2, also known as site-2 protease, is a zinc metalloprotease in the Golgi membrane. It regulates cholesterol metabolism and unfolded protein response. When cells are deprived of cholesterol, sterol regulatory element-binding proteins move from the endoplasmic reticulum to the Golgi apparatus and are cleaved by site-1 protease and site-2 protease sequentially to release the active amino-terminal domains. These amino-terminal domains of SREBPs then translocate into the nucleus to induce expression of genes for cholesterol biosynthesis. During UPR, activating transcription factor 6 transports from ER to Golgi apparatus and is cleaved by S1P and S2P to release a cytosolic fragment. This cytosolic fragment relocates to the nucleus and activates the UPR gene expression.

References

[1] Rawson, R.B. et al. (1997) Mol. Cell 1, 47-57.
[2] Zelenski, N.G. et al. (1999) J. Biol. Chem. 274, 21973-21980.
[3] Shen, J. and Prywes, R. (2004) J. Biol. Chem. 279, 43046-43051.
[4] Lee, K. et al. (2002) Genes Dev. 16, 452-466.
[5] DeBose-Boyd, R.A. et al. (1999) Cell 99, 703-712.
[6] Brown, M.S. and Goldstein, J.L. (1999) Proc. Natl. Acad. Sci. USA 96, 11041-11048.
[7] Kaufman, R.J. et al. (2002) Nat. Rev. Mol. Cell Biol. 3, 411-421.

Raw materials

Preparation Products