描述：
BMP-3b, also known as GDF-10, belongs to the transforming growth factor β (TGF-β)
superfamily which includes the TGF-βs, bone morphogenetic proteins (BMPs), growth
differentiation factors (GDFs), Activins, Inhibins, Leftys, Nodal, Mullerian inhibitory substance
(MIS) and the glial cell linederived neurotrophic factors (GDNFs) . TGF-β family members
are synthesized and secreted as homodimeric or heterodimeric prepropeptides that are cleaved
by proprotein convertases such as furin to generate the carboxyterminal mature dimeric
protein that contains the characteristic conserved cysteine residues involved in the formation
of the cysteine knot domain. Within pro-BMP-3b, three dibasic cleavage sites have been
identified. Mature BMP-3B is a disulfidelinked homodimer of the C-terminal 110 amino acids.
Among TGF-β family members, BMP3b is most closely related to BMP-3, sharing 83% and
30% amino acid sequence identity in their mature and pro regions, respectively. BMP-3b is
highly conserved across animal species, the aa sequence of mature human BMP-3b is 98%
identical with that of the mouse or rat proteins. BMP-3b is expressed in developing skeletal
structures of the craniofacial region and the vertebral column, as well as in the adult trachea,
aorta, and most abundantly in the cerebellum and uterus. Interestingly, in the knockout mice,
no obvious abnormalities have been found in these tissues. The biological function of BMP-3b
is yet unknown, however studies have implicated it in the differentiation of osteoblasts,
augmenting BMP-2 activity.
原厂资料：
BMP-3b, also known as GDF-10, belongs to the transforming growth factor β (TGF-β)
superfamily which includes the TGF-βs, bone morphogenetic proteins (BMPs), growth
differentiation factors (GDFs), Activins, Inhibins, Leftys, Nodal, Mullerian inhibitory substance
(MIS) and the glial cell linederived neurotrophic factors (GDNFs) . TGF-β family members
are synthesized and secreted as homodimeric or heterodimeric prepropeptides that are cleaved
by proprotein convertases such as furin to generate the carboxyterminal mature dimeric
protein that contains the characteristic conserved cysteine residues involved in the formation
of the cysteine knot domain. Within pro-BMP-3b, three dibasic cleavage sites have been
identified. Mature BMP-3B is a disulfidelinked homodimer of the C-terminal 110 amino acids.
Among TGF-β family members, BMP3b is most closely related to BMP-3, sharing 83% and
30% amino acid sequence identity in their mature and pro regions, respectively. BMP-3b is
highly conserved across animal species, the aa sequence of mature human BMP-3b is 98%
identical with that of the mouse or rat proteins. BMP-3b is expressed in developing skeletal
structures of the craniofacial region and the vertebral column, as well as in the adult trachea,
aorta, and most abundantly in the cerebellum and uterus. Interestingly, in the knockout mice,
no obvious abnormalities have been found in these tissues. The biological function of BMP-3b
is yet unknown, however studies have implicated it in the differentiation of osteoblasts,
augmenting BMP-2 activity.
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