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Bone Morphogenetic Protein 2 (BMP-2) is a ligand protein with pleiotropic, belongs to TNFβ family. BMP-2 formats BMP/TGFβ signaling to involve in vascular and valvular homeostasis, which is a critical process of embryonic development[1]. BMP-2/TGFβ signaling can be terminated by inhibitory SMADs including SMAD6 and SMAD7, which are activated and induced by BMP signaling and switch off BMP signaling via multiple mechanisms[2]. BMP-2 is widely found in different animals, while the sequence in human is similar to Rat (91.86%), and mouse (92.13%). BMPs exhibits critical contributions to the pathophysiology of atherosclerosis, pulmonary vascular disease, and vascular and valvular calcification[1]. BMP-2 binds different receptor, such as type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A), to regulate various calcification type[1]. BMP-2 promotes monocyte infiltration and inflammation of atherosclerotic legions[3]. It is linked to increased plaque formation via pro-inflammatory and pro-atherogenic effects, promoting oxidative stress, endothelial dysfunction and osteogenic differentiation[4]. BMP-2 is overexpressed in ossified regions of human calcified valves by myofibroblasts and pre-osteoblasts in areas densely infiltrated with B- and T-lymphocytes[5]. And it serves as the linkers between atherosclerotic vascular calcification with mechanisms of normal bone formation[6]. BMP-2 induces angiogenesis, endothelial cells (ECs) proliferation, and migration[7]. And BMP-2 also enhances the expression of the osteoblast and chondrocyte master transcriptional regulator RUNX2 to promote the mineralization of cultured human coronary vascular SMCs in a manner that was dependent on oxidative stress and endoplasmic reticulum (ER) stress[8].
The BMP-9/GDF-2 protein is a potent inhibitor of angiogenesis that selectively signals through AVRL1 in endothelial cells. Its signaling pathway requires the TGF-β coreceptor endoglin/ENG to effectively activate SMAD1. Animal-Free GDF-2/BMP-9 Protein, Human (His) is the recombinant human-derived animal-FreeBMP-9/GDF-2 protein, expressed by E. coli , with N-His labeled tag.
Bone morphogenetic protein 2 (BMP-2) is a pleiotropic ligand protein belonging to TNFβ family, and is involved in key embryonic development of vascular and valvular homeostasis. BMP-2 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to regulate various types of calcification, including atherosclerosis, chronic kidney disease, diabetes, and valve calcification. BMP-2 is overexpressed by myofibroblast and preosteoblast in the calcified area of human calcified valve, which are densely infiltrated by B lymphocytes and T lymphocytes. BMP-2 is the junction between atherosclerotic vascular calcification and normal bone formation mechanism. BMP-2 Protein, Human/Mouse/Rat is 114 a.a. (Q283-R396), expressed in E. coli.
Fibronectin type III domain-containing protein 5; Fibronectin type III repeat-containing protein 2; Irisin; FNDC5
Human
HEK293
Irisin is a hormone derived from the FNDC5 gene that promotes energy expenditure via thermogenesis. Irisin Protein, Human/Mouse/Rat (HEK293, Fc) is the recombinant human-derived Irisin protein, expressed by HEK293 , with C-hFc labeled tag. The total length of Irisin Protein, Human/Mouse/Rat (HEK293, Fc) is 112 a.a., with molecular weight of 45-60 kDa.
Bone morphogenetic protein 2A; BMP-2A; BDA2; SSFSC; SSFSC1
Human
P. pastoris
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/Mouse/Rat (P. pastoris, His) is the recombinant human-derived BMP-2 protein, expressed by P. pastoris , with N-6*His labeled tag.
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. Animal-Free BMP-2 Protein, Human/Mouse/Rat (His) is the recombinant human-derived animal-Free BMP-2 protein, expressed by E. coli , with C-His labeled tag.
Bone morphogenetic protein 4 (BMP-4) is a polymorphic ligand protein belonging to the TGF-β family, which is involved in the circulation of the vascular system and can activate receptors on vascular cells. BMP-4 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to increase plaque formation and promote oxidative stress, endothelial dysfunction, and osteogenic differentiation through its pro-inflammatory and pro-atherogenic effects. BMP-4 Protein, Mouse (HEK293, Fc) has a total length of 116 amino acids (S293-R408), is expressed in HEK293 cells with N-terminal rFc-tag.
Bone morphogenetic protein 4 (BMP-4) is a polymorphic ligand protein belonging to the TGF-β family, which is involved in the circulation of the vascular system and can activate receptors on vascular cells. BMP-4 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to increase plaque formation and promote oxidative stress, endothelial dysfunction, and osteogenic differentiation through its pro-inflammatory and pro-atherogenic effects. BMP-4 Protein, Human (His) has a total length of 116 amino acids (S293-R408), is expressed in E. coli cells with N-terminal 6*His-tag.
BDA2; BMP-2; BMP-2A; Bone morphogenetic protein 2a; SSFSC
Others
E. coli
Bone morphogenetic protein 2 (BMP-2) is a pleiotropic ligand protein belonging to TGFβ family, and is involved in key embryonic development of vascular and valvular homeostasis. BMP-2 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to regulate various types of calcification, including atherosclerosis, chronic kidney disease, diabetes, and valve calcification. BMP-2 is overexpressed by myofibroblast and preosteoblast in the calcified area of human calcified valve, which are densely infiltrated by B lymphocytes and T lymphocytes. BMP-2 is the junction between atherosclerotic vascular calcification and normal bone formation mechanism. Zebrafish BMP-2 Protein has a length of 386 a.a., BMP-2 Protein, Zebrafish is 105 a.a. (Q272-R386), expressed in E. coli cells with tag free.
Bone morphogenetic protein 5 (BMP-5) is a pleiotropic ligand protein belonging to the TGFβ family, which is mainly expressed in the lung and liver. After BMP-5 silencing, the activity of p38/ERK signaling pathway can be down-regulated to inhibit chondrocyte senescence and apoptosis and knee arthritis (OA). Bmp-5 initiates typical BMP signaling cascades by binding to type I receptor BMPR1A and type II receptor BMPR2, or triggers signals through atypical pathways such as MAPK p38 signaling cascades to promote chondrogenic differentiation. The total length of human BMP-5 protein is 454 amino acids (M1-H454), with 4 glycosylation domains. BMP-5 Protein, Human (HEK293, hFc) has a total length of 131 amino acids (Q324-H454), is expressed in HEK293 cells with a N-terminal hFc-tag.
Bone morphogenetic protein 11 (BMP-11; GDF11), also known as growth/differentiation factor 11, is a polymorphic ligand protein belonging to the TGFβ family. The GDF-11/BMP-11 signal activates the signal through activator receptor types I and II, resulting in the phosphorylation of SMAD2 and SMAD3. GDF-11/BMP-11 is an important regulator of central nervous system (CNS) formation and fate. Exogenous peripheral delivery of GDF-11/BMP-11 may enhance neurogenesis and angiogenesis and improve neuropathological outcomes in the elderly brain. The total length of human GDF-11/BMP-11 protein is 407 amino acids (M1-M407), with a glycosylation domain. Animal-Free GDF-11/BMP-11 Protein, Human (His) has a total length of 109 amino acids (N299-S407), is expressed in E. coli with C-terminal His-tag.
The BMP-9/GDF-2 protein is a potent inhibitor of angiogenesis that selectively signals through AVRL1 in endothelial cells. Its signaling pathway requires the TGF-β coreceptor endoglin/ENG to effectively activate SMAD1. GDF-2/BMP-9 Protein, Human (P. pastoris, His) is the recombinant human-derived GDF-2 protein, expressed by P. pastoris , with N-6*His labeled tag.
rHuGrowth/differentiation factor 11; Growth/differentiation factor 11; GDF-11; Bone morphogenetic protein 11; BMP-11
Human
HEK293
The GDF-11/BMP-11 protein is a secreted signaling protein that globally regulates anterior/posterior axis patterning during development and plays a key role in mesoderm and neural tissue patterning. GDF-11/BMP-11 is critical for vertebral and orofacial development and signals through type 2 activin receptors (ACVR2A and ACVR2B) and type 1 activin receptors (ACVR1B, ACVR1C and TGFBR1), leading to SMAD2 and SMAD3 phosphorylation. GDF-11/BMP-11 Protein, Human (HEK293, solution) is the recombinant human-derived GDF-11/BMP-11 protein, expressed by HEK293 , with tag free. The total length of GDF-11/BMP-11 Protein, Human (HEK293, solution) is 109 a.a., with molecular weight of ~14.0 kDa.
Bone morphogenetic protein 4 (BMP-4) is a polymorphic ligand protein belonging to the TGF-β family, which is involved in the circulation of the vascular system and can activate receptors on vascular cells. BMP-4 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to increase plaque formation and promote oxidative stress, endothelial dysfunction, and osteogenic differentiation through its pro-inflammatory and pro-atherogenic effects. BMP-4 Protein, Human has a total length of 116 amino acids (S293-R408), is expressed in E. coli cells with tag free.
Bone morphogenetic protein 7 (BMP-7) is a polymorphic ligand protein belonging to the TGFβ family. BMP-7 is involved in regulating the proliferation, invasion and migration of cancer cells and is associated with a variety of human tumors. BMP-7 binds ALK2 or ACVR2A/BMPR2 excitation signal, which is terminated by SMADs regulation. BMP-7 is involved in the BMP-7-SMad1/5/9 signaling pathway, which is associated with the epithelial-mesenchymal transition (EMT) process. BMP-7 also eliminates vascular inflammation, maintains vascular integrity, reduces vascular calcification, and stimulates in situ phosphate ossification deposition. The total length of human BMP-7 protein is 431 amino acids (M1-H431), with 4 glycosylation domains. BMP-7 Protein, Human has a total length of 139 amino acids (S293-H431), is expressed in E. coli cells.
Bone morphogenetic protein 15 (BMP-15; GDF9B), also known as growth differentiation factor 9B (GDF9B), is a polymorphic ligand protein of the TGFβ family and is only expressed in follicular cells. BMP15 is closely related to GDF9 and synergistically regulates the genetic development of follicles. BMP15 is involved in p38 MAPK and HIF-1α/SCF signaling pathway, respectively, and can up-regulate the expression of anti-Mullerian hormone (AMH) and polycystic ovarian syndrome (PCOS) related stem cell factor (SCF) in granulosa cells. The total length of human BMP-15 protein is 392 amino acids (M1-R392), with 4 glycosylation domains. BMP-15 Protein, Human (His, Myc) has a total length of 125 amino acids (Q268-R392), is expressed in E. coli cells with a N-terminal His-tag, a C-terminal Myc-tag, respectively.
BMP 1; BMP-1; BMP1; BMP1_HUMAN; Bone morphogenetic protein 1; Mammalian tolloid protein; mTld; OI13; PCOLC; PCP; PCP2; Procollagen C endopeptidase; Procollagen C proteinase; Procollagen C-proteinase; TLD; Tolloid; Drosophila; homolog of
Human
E. coli
Bone morphogenetic protein 1 (BMP-1), also known as metalloproteinases, belongs to the BMP-1/tolloidlike proteinases (BTP) family. BMP-1 is also a signature extracellular matrix (ECM) protein associated with high metastatic potential in breast tumors. BMP-1 processes growth factors, including TGF-β, BMP-2, BMP-4, and GFD8, regulates morphogenesis, and mediates the cleavage of COOH-terminal propeptide of type I procollagen (CICP) in the extracellular space. The total length of human BMP-1 protein is 986 amino acids (M1-K986), with 4 glycosylation domains. BMP-1 Protein, Human (His) has a total length of 866 amino acids (A121-K986), is expressed in E. coli cells with a N-terminal *His-tag.
Growth/differentiation factor 10; GDF-10; Bone morphogenetic protein 3B;
BMP-3B
Mouse
HEK293
Bone morphogenetic protein 3 (BMP-3; GDF10) is a polymorphic ligand protein belonging to the TGF-β family. BMP-3 is the main component of osteoblast and has osteogenic activity. BMP-3 plays an inhibitory role in the carcinogenic process, and inhibits the occurrence of colon tumors through ActRIIB/ SMad2-dependent and TAK1/JNK signaling pathways. BMP-3B/GDF10 Protein, Mouse (HEK293, Fc) has a total length of 110 amino acids (Q367-R476), is expressed in HEK293 cells.
BMP-10 is essential for embryonic cardiomyocyte proliferation, preventing premature activation of CDKN1C/p57KIP and ensuring optimal expression of MEF2C and NKX2-5.As a ligand for AVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, it activates SMAD1, SMAD5 and SMAD8, regulating key signaling pathways.Animal-Free BMP-10 Protein, Human (His) is the recombinant human-derived animal-FreeBMP-10 protein, expressed by E.coli , with C-His labeled tag.
BMP-3 Protein, a TGF-beta superfamily member, crucially influences early skeletal formation and acts as a bone density negative regulator. It counteracts osteogenic BMPs, hindering osteoprogenitor differentiation. BMP-3 initiates signaling via ACVR2B, activating SMAD2-dependent and SMAD-independent pathways, including TAK1 and JNK. Structurally, it forms homodimers with disulfide bonds, interacting with ACVR2B to regulate functions. Animal-Free BMP-3 Protein, Human (His) is the recombinant human-derived animal-FreeBMP-3 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free BMP-3 Protein, Human (His) is 110 a.a., with molecular weight of ~13.34 kDa.
Bone morphogenetic protein 4 (BMP-4) is a polymorphic ligand protein belonging to the TGF-β family, which is involved in the circulation of the vascular system and can activate receptors on vascular cells. BMP-4 binds to type I receptors (ALK-2/-3/-6) and type II receptors (BMPR2, ACVR2A) to increase plaque formation and promote oxidative stress, endothelial dysfunction, and osteogenic differentiation through its pro-inflammatory and pro-atherogenic effects. Animal-Free BMP-4 Protein, Human (His) has a total length of 106 amino acids (K303-R408), is expressed in E. coli cells with a C-terminal His-tag.
