BMP-2 Protein, Human (P. pastoris, His)

BMP-2 protein is an important member of the TGF-β superfamily and is critical in cardiogenesis, neurogenesis, and osteogenesis, inducing cartilage and bone formation. It initiates canonical BMP signaling by binding to BMPR1A and BMPR2, triggering BMPR2 phosphorylation and SMAD1/5/8 activation for gene transcription regulation. BMP-2 Protein, Human (P. pastoris, His) is the recombinant human-derived BMP-2 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of BMP-2 Protein, Human (P. pastoris, His) is 114 a.a., with molecular weight of 14.9 kDa.

BMP-2 Protein, a vital member of the TGF-beta superfamily, plays essential roles in diverse developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. It induces cartilage and bone formation and initiates the canonical BMP signaling cascade by binding to type I receptor BMPR1A and type II receptor BMPR2. This complex formation triggers BMPR2 phosphorylation, activating BMPR1A, which, in turn, phosphorylates SMAD1/5/8 to modulate gene transcription. BMP-2 also engages non-canonical pathways, such as the ERK/MAP kinase signaling cascade, influencing osteoblast differentiation. Additionally, it stimulates myoblast differentiation into osteoblasts through the EIF2AK3-EIF2A-ATF4 pathway. Acting as a positive regulator of odontoblast differentiation, BMP-2 forms homodimers and interacts with various proteins, including SOSTDC1, GREM2, RGMA, RGMB, RGMC, ASPN, FBN1, FBN2, SCUBE3, TNFAIP6, and ERFE. Its intricate interactions highlight its versatile regulatory roles in multiple cellular processes.

Human

P. pastoris

N-6*His

P12643 (Q283-R396)

650  [NCBI]

QAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGYHAFYCHGECPFPLADHLNSTNHAIVQTLVNSVNSKIPKACCVPTELSAISMLYLDENEKVVLKNYQDMVVEGCGCR

14.9 kDa

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

<1 EU/μg, determined by LAL method.