CEMP1 Protein, Human (P.pastoris, His)

CEMP1 protein may play a key role in the development of periodontal tissue, promoting the differentiation of periodontal ligament cells into cementoblasts and promoting cementum formation. CEMP1 exhibits affinity for hydroxyapatite, suggesting involvement in cementum biomineralization. CEMP1 Protein, Human (P.pastoris, His) is the recombinant human-derived CEMP1 protein, expressed by P. pastoris , with N-His labeled tag. The total length of CEMP1 Protein, Human (P.pastoris, His) is 247 a.a., with molecular weight of ~28.0 kDa.

The CEMP1 protein is implicated in potentially playing a crucial role in the development of the periodontium, the supportive tissue surrounding the teeth. It is suggested to promote the differentiation of multi-potent cells from the periodontal ligament into cementoblasts, contributing to the formation of the cementum, as evidenced by various studies. CEMP1 exhibits an affinity for hydroxyapatite and may play a role in promoting the biomineralization of the cementum, further underlining its potential involvement in the mineralization processes of dental tissues. Additionally, CEMP1 is associated with the promotion of cell proliferation, as supported by multiple studies. The multifaceted functions of CEMP1 in periodontal development and tissue mineralization emphasize its significance in dental biology, warranting further exploration to unravel its specific mechanisms and regulatory roles in these processes.

Human

P. pastoris

N-His

Q6PRD7 (1M-247G)

752014  [NCBI]

MGTSSTDSQQAGHRRCSTSNTSAENLTCLSLPGSPGKTAPLPGPAQAGAGQPLPKGCAAVKAEVGIPAPHTSQEVRIHIRRLLSWAAPGACGLRSTPCALPQALPQARPCPGRWFFPGCSLPTGGAQTILSLWTWRHFLNWALQQREENSGRARRVPPVPRTAPVSKGEGSHPPQNSNGEKVKTITPDVGLHQSLTSDPTVAVLRAKRAPEAHPPRSCSGSLTARVCHMGVCQGQGDTEDGRMTLMG

Approximately 28.0 kDa

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

<1 EU/μg, determined by LAL method.