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Polyclonal Antibody Western Blotting Bone Remodeling

Also showing Polyclonal Antibody Western Blotting Regulation of Bone Remodeling, Polyclonal Antibody Negative Regulation of Bone Remodeling

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Connexin 43 (Cx43) is a member of the large family of gap junction proteins. Connexins assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Clusters of these channels assemble to make gap junctions. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (1,2). Ser368 of Cx43 is phosphorylated by protein kinase C (PKC) after activation by phorbol esters, which decreases cell-to-cell communication (3). Src can interact with and phosphorylate Cx43 to alter gap junction communication (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$303
100 µl
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Connexin 43 (Cx43) is a member of the large family of gap junction proteins. Connexins assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Clusters of these channels assemble to make gap junctions. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (1,2). Ser368 of Cx43 is phosphorylated by protein kinase C (PKC) after activation by phorbol esters, which decreases cell-to-cell communication (3). Src can interact with and phosphorylate Cx43 to alter gap junction communication (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Gremlin is a secreted antagonist of bone morphogenetic proteins that play important roles during development. Gene targeting generates gremlin deficient mice that die shortly after birth due to absent kidneys and defects in lung septation (1-3). Gremlin also plays a role in cardiomyogenesis and angiogenesis (4,5). TGF-β can induce gremlin expression under pathological conditions. Gremlin colocalizes with TGF-β in tubulointerstitial fibrosis associated with chronic allograft nephropathy and is expressed in diabetic nephropathy in vivo (6-8). Gremlin is widely expressed in cancer associated stromal cells and can enhance cancer cell proliferation (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Western Blotting

Background: Phosphatidylinositol lipids and phosphoinositides are important second messengers, their generation controlling many cellular events. Intracellular levels of these molecules are regulated by phosphoinositide kinases and phosphatases. One of the best characterized lipid kinases is phosphoinositide 3-kinase (PI3K), which is responsible for phosphorylation on the D-3 position of the inositide head group (1). This action of PI3K catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN, the well characterized partnering phosphatase, reverses this process by removing the phosphate from PI(3,4,5)P3 at the D-3 position to generate PI(4,5)P2 (1,2). Dephosphorylation on the D-5 position to generate PI(3,4)P2 occurs through the action of SHIP1 or SHIP2 (3), and dephosphorylation on the D-4 position to generate PI(3)P can occur through the action of inositol polyphosphate 4-phosphatase isoenzymes type I (INPP4a) and type II (INPP4b) (4,5). While INPP4a has been implicated in neuronal survival and megakaryocyte lineage determination (6,7), less is understood about INPP4b. It has been shown that two splice variants of INPP4b occur in mice, each showing distinct tissue distribution and subcellular localization (5,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Secreted Frizzled-related proteins (SFRPs) display homology and structural similarity to the extracellular cysteine-rich Wnt-binding domain of the G protein-coupled receptor Frizzled (1,2). To date, five distinct SFRPs (SFRP1 to 5) have been found in mammalian cells. These secreted proteins typically act as antagonists to Wnt signaling by directly binding and inhibiting Wnt proteins, or by binding Frizzled to block Wnt protein interaction with the receptor (3). The various SFRPs bind and regulate Wnt proteins differentially; these proteins also display distinct expression patterns as they play important roles in regulating development (4-7). SFRP proteins appear to act as tumor suppressors, with loss of expression or function correlating with many invasive forms of cancer. Deletion of the corresponding SFRP1 gene and promoter hypermethylation leading to gene silencing has been reported in a number of cancers. Abnormal expression of SRFP1 and other Wnt signaling proteins is associated with some cases of retinitis pigmentosa (reviewed in 8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: BMPR2 is a type II serine/threonine receptor kinase that binds to an array of secreted bone morphogenetic proteins (BMPs). BMPs belong to the superfamily of TGF-β ligands that modulate gastrulation, neurogenesis, chondrogenesis, interdigital cell death, and bone morphogenesis (1-5). In contrast to the TGF-β type II receptor, BMPR2 contains an extended carboxyl-terminal region that interacts with multiple signaling molecules to modulate the responsiveness of target genes to BMPs (6,7). BMP signaling requires oligomerization of both type I and type II receptors to elicit a functional response of target genes. BMP binding to type I and II receptors induces Smad1/5/8 phosphorylation which is required for the activation of target genes (7). In vitro and in vivo evidence suggests that defects in BMPR2 may contribute to pulmonary hypertension, inflammation, and endothelial injury (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Transforming growth factor-β (TGF-β) superfamily members are critical regulators of cell proliferation and differentiation, developmental patterning and morphogenesis, and disease pathogenesis (1-4). TGF-β elicits signaling through three cell surface receptors: type I (RI), type II (RII), and type III (RIII). Type I and type II receptors are serine/threonine kinases that form a heteromeric complex. In response to ligand binding, the type II receptors form a stable complex with the type I receptors allowing phosphorylation and activation of type I receptor kinases (5). The type III receptor, also known as betaglycan, is a transmembrane proteoglycan with a large extracellular domain that binds TGF-β with high affinity but lacks a cytoplasmic signaling domain (6,7). Expression of the type III receptor can regulate TGF-β signaling through presentation of the ligand to the signaling complex. The only known direct TGF-β signaling effectors are the Smad family proteins, which transduce signals from the cell surface directly to the nucleus to regulate target gene transcription (8,9).