IBSP Protein, Human (His-SUMO)

The IBSP protein has a strong affinity for hydroxyapatite and plays a crucial role in mineralized matrix formation, indicating its overall nature in this regard. Its tight binding suggests an important role in cell-matrix interactions, particularly in promoting RGD-dependent cell attachment. IBSP Protein, Human (His-SUMO) is the recombinant human-derived IBSP protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of IBSP Protein, Human (His-SUMO) is 153 a.a., with molecular weight of ~32.4 kDa.

IBSP protein exhibits strong binding affinity to hydroxyapatite, suggesting a crucial role in the formation of the mineralized matrix. It is likely to be an integral component of this matrix, implying its significance in cell-matrix interactions. Notably, IBSP protein plays a key role in promoting Arg-Gly-Asp (RGD)-dependent cell attachment, emphasizing its involvement in cellular adhesion processes. The observed tight binding to hydroxyapatite and its apparent integration into the mineralized matrix underscore the importance of IBSP in contributing to the structural and functional aspects of cell-matrix interactions within biological systems.

Human

E. coli

N-6*His;N-SUMO

P21815 (A129-E281)

3381  [NCBI]

AIQLPKKAGDITNKATKEKESDEEEEEEEEGNENEESEAEVDENEQGINGTSTNSTEAENGNGSSGGDNGEEGEEESVTGANAEDTTETGRQGKGTSKTTTSPNGGFEPTTPPQVYRTTSPPFGKTTTVEYEGEYEYTGANEYDNGYEIYESE

Approximately 32.4 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.