670 Results for: "bmp"

Supplier: Bioss

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].

Supplier: Bioss

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].

Supplier: Bioss

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].

Supplier: Bioss

The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq].

Supplier: Prosci

Human Recombinant BMP-10 Protein (from HEK293 cells)

Supplier: Prosci

Human, Mouse Recombinant BMP-2 Protein (from CHO cells)

Supplier: Bioss

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.

Supplier: Bioss

Growth differentiation factor 15 (GDF15) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. It has been implicated in a variety of functions directly related to tumorigenicity including antiproliferative and pro-apoptotic effects. BMP proteins are secreted growth factors that are characterized by seven conserved cysteine residues. In general, they are regulators of cell growth and differentiation in both embryonic and adult tissues.GDF15 is an important downstream mediator of DNA damage signaling and a transcriptional target of p53.

Supplier: Bioss

Growth differentiation factor 15 (GDF15) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. It has been implicated in a variety of functions directly related to tumorigenicity including antiproliferative and pro-apoptotic effects. BMP proteins are secreted growth factors that are characterized by seven conserved cysteine residues. In general, they are regulators of cell growth and differentiation in both embryonic and adult tissues.GDF15 is an important downstream mediator of DNA damage signaling and a transcriptional target of p53.

Supplier: Bioss

Growth differentiation factor 15 (GDF15) is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. It has been implicated in a variety of functions directly related to tumorigenicity including antiproliferative and pro-apoptotic effects. BMP proteins are secreted growth factors that are characterized by seven conserved cysteine residues. In general, they are regulators of cell growth and differentiation in both embryonic and adult tissues.GDF15 is an important downstream mediator of DNA damage signaling and a transcriptional target of p53.

Supplier: Bioss

The protein encoded by this gene is a member of the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. The members of this family are regulators of cell growth and differentiation in both embryonic and adult tissues. Studies in rodents suggest that this protein plays a role in the adult liver and in differentiation of cholinergic central nervous system neurons. [provided by RefSeq, Jul 2008].

Supplier: ANTIBODIES.COM LLC

Rabbit polyclonal antibody to BMP-6 for WB, IHC and ELISA with samples derived from Human.

Supplier: Bioss

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).

Supplier: Bioss

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).

Supplier: Prosci

ZCCHC12 contains 1 CCHC-type zinc finger. ZCCHC12 is the transcriptional coactivator in the bone morphogenetic protein (BMP)-signaling pathway. It positively modulates BMP signaling by interacting with SMAD1 and associating with CBP in the transcription complex. It contributes to the BMP-induced enhancement of cholinergic-neuron-specific gene expression.

Supplier: Bioss

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.

Supplier: Bioss

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.

Supplier: Bioss

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Binds to BMP-7, BMP-2 and, less efficiently, BMP-4. Binding is weak but enhanced by the presence of type I receptors for BMPs.

Supplier: Bioss

GDF10, or growth differentiation factor 10, bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. GDF10 is expressed in femur, brain, lung, skeletal muscle, pancreas and testis.

Supplier: Bioss

GDF10, or growth differentiation factor 10, bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. GDF10 is expressed in femur, brain, lung, skeletal muscle, pancreas and testis.

Supplier: Bioss

CHRDL2 is a novel chordin like protein that can act as a BMP antagonist. Amember of the chordin family of proteins, it contains a signal peptide andthree CR (cysteine-rich repeat) domains. When expressed as a recombinantprotein it is secreted and binds to activin A, but not to BMP-2, -4, -6. Differential expression has been detected in developing chondrocytes, myoblasts, osteoblasts, and osteoarthritic joints. Complex alternative splicing of CHRDL2 potentially results in distinct isoforms that differ at their C termini, in the expression of signal peptide, and in the content of CR domains. CHRDL2 was originally characterized as a novel protein exclusively expressed in breast, lung, and colon tumors.

Supplier: Bioss

CHRDL2 is a novel chordin like protein that can act as a BMP antagonist. Amember of the chordin family of proteins, it contains a signal peptide andthree CR (cysteine-rich repeat) domains. When expressed as a recombinantprotein it is secreted and binds to activin A, but not to BMP-2, -4, -6. Differential expression has been detected in developing chondrocytes, myoblasts, osteoblasts, and osteoarthritic joints. Complex alternative splicing of CHRDL2 potentially results in distinct isoforms that differ at their C termini, in the expression of signal peptide, and in the content of CR domains. CHRDL2 was originally characterized as a novel protein exclusively expressed in breast, lung, and colon tumors.

Supplier: Prosci

Bone Morphogenetic Protein Receptor II (BMPR-II) is a Type II Serine/Threonine Kinase that mediates cellular responses to BMPs. BMPR-II is characterized by lacking of a GS domain, and presence of a C-terminal extension typical of type II receptors. BMPRII binds BMP2, BMP4 and BMP7 weakly in the absence of type I receptor, and the binding can be facilitated by the presence of the type I receptor, including BMPR-IA/Brk1, BMPR-IB, and ActR-I. BMPR-II plays a key role in cell growth. Defects in BMPR-II have been linked to primary pulmonary hypertension. Human and mouse BMPR-II are highly conserved and share 97 % amino acid sequence identity.

Supplier: Prosci

Bone Morphogenetic Protein Receptor II (BMPR-II) is a Type II Serine/Threonine Kinase that mediates cellular responses to BMPs. BMPR-II is characterized by lacking of a GS domain, and presence of a C-terminal extension typical of type II receptors. BMPRII binds BMP2, BMP4 and BMP7 weakly in the absence of type I receptor, and the binding can be facilitated by the presence of the type I receptor, including BMPR-IA/Brk1, BMPR-IB, and ActR-I. BMPR-II plays a key role in cell growth. Defects in BMPR-II have been linked to primary pulmonary hypertension. Human and mouse BMPR-II are highly conserved and share 97 % amino acid sequence identity.

Supplier: Bioss

CHRDL2 is a novel chordin like protein that can act as a BMP antagonist. Amember of the chordin family of proteins, it contains a signal peptide andthree CR (cysteine-rich repeat) domains. When expressed as a recombinantprotein it is secreted and binds to activin A, but not to BMP-2, -4, -6. Differential expression has been detected in developing chondrocytes, myoblasts, osteoblasts, and osteoarthritic joints. Complex alternative splicing of CHRDL2 potentially results in distinct isoforms that differ at their C termini, in the expression of signal peptide, and in the content of CR domains. CHRDL2 was originally characterized as a novel protein exclusively expressed in breast, lung, and colon tumors.

Supplier: Bioss

CHRDL2 is a novel chordin like protein that can act as a BMP antagonist. Amember of the chordin family of proteins, it contains a signal peptide andthree CR (cysteine-rich repeat) domains. When expressed as a recombinantprotein it is secreted and binds to activin A, but not to BMP-2, -4, -6. Differential expression has been detected in developing chondrocytes, myoblasts, osteoblasts, and osteoarthritic joints. Complex alternative splicing of CHRDL2 potentially results in distinct isoforms that differ at their C termini, in the expression of signal peptide, and in the content of CR domains. CHRDL2 was originally characterized as a novel protein exclusively expressed in breast, lung, and colon tumors.

Supplier: Bioss

GDF10, or growth differentiation factor 10, bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. GDF10 is expressed in femur, brain, lung, skeletal muscle, pancreas and testis.

Supplier: Prosci

SkiP Antibody: TGF-beta and the bone morphogenic proteins (BMPs) are key signaling proteins that regulate numerous cellular processes such as embryonic development and tumorigenesis. Both signal through the Smad protein family and are negatively regulated by Ski and SnoN, two related proto-oncoproteins. Ski functions by binding to the Smad proteins activated by TGF-beta and the (BMPs) and preventing their phosphorylation, inhibiting their ability to bind DNA and activate the transcription of downstream genes. SkiP was originally identified as a Ski-interacting protein and was later found to augment the signals induced by TGF-beta but inhibit transcription induced by BMP-2 in C2C12 cells, suggesting that SkiP is a key player in the signaling cascades inititated by TGF-beta and the BMP protein family.

Supplier: Prosci

BMPs (bone morphogenetic proteins) belong to the TGF beta superfamily of structurally related signaling proteins. Members of this superfamily are widely represented throughout the animal kingdom and have been implicated in a variety of developmental processes. Proteins of the TGF beta superfamily are disulfide-linked dimers composed of two 12-15 kDa polypeptide chains. As implied by their name, BMPs initiate, promote and regulate bone development, growth, remodeling and repair.

Supplier: Prosci

Mouse Chordin-Like 2, also known as CHL2, is a novel chordin family member with structural homology to CHL1 which is implicated in tumor angiogenesis. The mouse CHL2 gene encodes a 426 amino acids (aa) protein with a 25 aa signal peptide. The mature chain of CHL2 protein contains two potential N-linked glycosylation sites, one putative NLS and three 63 aa cysteine-rich von Willebrand type C repeats (CRs). CHL2 gene is weakly expressed in the liver and kidney, partly expressed in the connective tissues of reproductive organs such as ligaments of the ovary and oviduct in females, and of testis, epididymis and certain male accessory sex glands in males. Recombinant mCHL2 protein interacted directly with five BMPs and one GDF thereby inhibiting, in vitro, several BMP/GDF-dependent processes including, osteogenic differentiation of C2C12 mesenchymal progenitor cells by several BMPs, ATDC5 embryonal carcinoma cells by GDF5 and BMP4-dependent lymphohematopoietic (CD34+CD31hi and CD34+CD31lo) progenitor cell development from ES cells. CHL2 may inhibits BMPs activity by blocking their interaction with their receptors, and has a negative regulator effect on the cartilage formation/regeneration from immature mesenchymal cells, by preventing or reducing the rate of matrix accumulation. Also, it may play a role during myoblast and osteoblast differentiation, and maturation.