Recombinant mouse Biglycan protein

ADPDEEASGS DTTSGVPDLD SVTPTFSAMC PFGCHCHLRV VQCSDLGLKT VPKEISPDTT LLDLQNNDIS ELRKDDFKGL QHLYALVLVN NKISKIHEKA FSPLRKLQKL YISKNHLVEI PPNLPSSLVE LRIHDNRIRK VPKGVFSGLR NMNCIEMGGN PLENSGFEPG AFDGLKLNYL RISEAKLTGI PKDLPETLNE LHLDHNKIQA IELEDLLRYS KLYRLGLGHN QIRMIENGSL SFLPTLRELH LDNNKLSRVP AGLPDLKLLQ VVYLHSNNIT KVGINDFCPM GFGVKRAYYN GISLFNNPVP YWEVQPATFR CVTDRLAIQF GNYKKLEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH

Bgn, also known as biglycan preproprotein, is a small leucine-rich repeat proteoglycan (SLRP). It binds to the growth factors BMP-4 and influences BMP-4 bioactivity. It plays an important role in stabilizing fibrotic scars after experimental myocardial infarction. It may function in connective tissue metabolism by binding to collagen fibrils and TGF-beta and may promote neuronal survival. Its ablation improves cardiac function and attenuates left ventricular hypertrophy and fibrosis after long-term pressure overload. It is found in a variety of extracellular matrix tissues, including bone, cartilage and tendon. Recombinant mouse Bgn, fused to hIgG-His-tag at C-terminus, was expressed in insect cell and purified by using conventional chromatography techniques.

< 1 EU per 1ug of protein (determined by LAL method)

Liquid in. Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol

Beetz N., et al. (2016) J Mol Cell Cardiol. 101:145-155.; ; Bianco P., et al. (1990) J Histochem Cytochem. 38:1549-1563.

Ala