66859 Results for: "Rosolic acid (actin)"

Supplier: Proteintech

EVL (Ena/VASP-like protein) is implicated inprocesses that requires dynamic actin remodeling such as axon guidance and platelet activation.It has two isoforms, EVL and EVL-I,that are highly expressed in hematopoietic cells of thymus and spleen,and both isoforms can be phosphorylated by PKA in vitro.

Supplier: Proteintech

FERMT2, also named as KIND2, MIG2, PLEKHC1, MIG-2 and Kindlin-2, belongs to the kindlin family. There are three FERMT2 isoforms that participate in the connection between extracellular matrix (ECM) adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. FERMT2 recruits migfilin (FBLP1) protein to cell-ECM focal adhesion sites. Variable expression in human cancers and mesenchymal cancer invasion are now linked with FERMT2, which may plays important role in carcinormas development. Catalog#11453-1-AP is a rabbit polyclonal antibody against human FERMT2.

Supplier: Proteintech

ACTN4 (alpha actinin 4) is a ubiquitous actin-binding protein that cross-links actin filaments into bundles to form filopodia, and has a crucial role in cytoskeletal organization. ACTN4 is colocalized with actin stress fibers and is dispersed in the cytoplasm and in the nucleus. Increased levels of ACTN4 have been associated with cancer metastasis, indicating its implication in cancer cell migration and metastasis. Defects in ACTN4 cause glomerular disease. This antibody recognizes 100-105 kDa of endogenous ACTN4 protein in various lysates. (22370640, 10700177)

Supplier: Prosci

KANK2 Antibody: Ankyrins are membrane adaptor molecules that play important roles in the control of cytoskeleton formation by regulating actin polymerization. KANK2 (KN motif and ankyrin repeat domain-containing protein 2), was initially identified as a steroid receptor coactivator (SRC) interacting protein (SIP) that could sequester steroid receptor coactivators in the cytoplasm. More recent experiments have shown that while KANK2 is widely expressed, in kidney podocytes, KANK2 localizes to foot processes, suggesting that KANK2 may contribute to controlling actin dynamics in podocyte foot processes.

Supplier: Prosci

KANK3 Antibody: Ankyrins are membrane adaptor molecules that play important roles in the control of cytoskeleton formation by regulating actin polymerization. Like other members of the KANK family, KANK3 (KN motif and ankyrin repeat domain-containing protein 3), is thought to play a role in the formation of actin stress fibers. In zebrafish, the homolog of KANK3 interacts with the adaptor protein Numb, a protein implicated in multiple basic cellular processes, and is essential for epidermal integrity and neurulation, suggesting that KANK3 may play a similar role in higher organisms.

Supplier: Prosci

ENC-1 Antibody: The ectoderm-neural cortex-1 (ENC-1) protein is an early and highly specific marker of neural induction in vertebrates. It is a kelch family related protein that functions as an actin-binding protein and has been suggested to be involved in the organization of the actin cytoskeleton during neural fate specification and development of the nervous system. ENC-1 has also been shown to be required for adipocyte differentiation when cytoskeletal reorganization and cell shape change from fibroblastic preadipocytes to spherical adipocytes occur.

Supplier: Proteintech

Wiskott-Aldrich Syndrome protein (WASP) regulates actin cytoskeleton in hematopoietic cells and defects in WASP cause Wiskott-Aldrich Syndrome (WAS), an X-linked immunodeficiency and autoimmunity disorder of childhood.

Supplier: Prosci

ENC-1 Antibody: The ectoderm-neural cortex-1 (ENC-1) protein is an early and highly specific marker of neural induction in vertebrates. It is a kelch family related protein that functions as an actin-binding protein and has been suggested to be involved in the organization of the actin cytoskeleton during neural fate specification and development of the nervous system. ENC-1 has also been shown to be required for adipocyte differentiation when cytoskeletal reorganization and cell shape change from fibroblastic preadipocytes to spherical adipocytes occur.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Bioss

Catalyzes the release of fatty acids from phospholipids. It has been implicated in normal phospholipid remodeling, nitric oxide-induced or vasopressin-induced arachidonic acid release and in leukotriene and prostaglandin production. May participate in fas mediated apoptosis and in regulating transmembrane ion flux in glucose-stimulated B-cells. Has a role in cardiolipin (CL) deacylation. Required for both speed and directionality of monocyte MCP1/CCL2-induced chemotaxis through regulation of F-actin polymerization at the pseudopods. Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity.

Supplier: Prosci

TOCA-1 Antibody: Actin reorganization is important for the regulation of neuronal morphology. A protein involved in this process, the transducer of cdc42-dependent actin assembly 1 (TOCA-1) protein, a member of the evolutionarily conserved pombe CDC15 homology (PCH) protein family, is an essential component of the Cdc42 pathway. TOCA-1 binds both N-WASP and Cdc42 and is essential for Cdc42- and PIP2-induced actin polymerization, suggesting that TOCA-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Decreased expression of TOCA-1 significantly enhances neurite elongation in PC-12 cells; its overexpression in the same cells suppresses neurite elongation. It has been suggested that TOCA-1 negatively regulates axon branching by regulating membrane trafficking by regulating membrane trafficking through the F-BAR/EFC domain. Multiple isoforms of TOCA-1 are known to exist.

Supplier: Proteintech

Beta actin, also named as ACTB and F-Actin, belongs to the actin family. Actins are highly conserved globular proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. At least six isoforms of actins are known in mammals and other vertebrates: alpha (ACTC1, cardiac muscle 1), alpha 1 (ACTA1, skeletal muscle) and 2 (ACTA2, aortic smooth muscle), beta (ACTB), gamma 1 (ACTG1) and 2 (ACTG2, enteric smooth muscle). Beta and gamma 1 are two non-muscle actin proteins. Most actins consist of 376aa, while ACTG2 (rich in muscles) has 375aa and ACTG1(found in non-muscle cells) has only 374aa. Beta actin has been widely used as the internal control in RT-PCR and Western Blotting as a 42-kDa protein. This antibody was generated against N-terminal region of human beta actin protein and can cross-react with other actins.

Supplier: Prosci

TOCA-1 Antibody: Actin reorganization is important for the regulation of neuronal morphology. A protein involved in this process, the transducer of cdc42-dependent actin assembly 1 (TOCA-1) protein, a member of the evolutionarily conserved pombe CDC15 homology (PCH) protein family, is an essential component of the Cdc42 pathway. TOCA-1 binds both N-WASP and Cdc42 and is essential for Cdc42- and PIP2-induced actin polymerization, suggesting that TOCA-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Decreased expression of TOCA-1 significantly enhances neurite elongation in PC-12 cells; its overexpression in the same cells suppresses neurite elongation. It has been suggested that TOCA-1 negatively regulates axon branching by regulating membrane trafficking by regulating membrane trafficking through the F-BAR/EFC domain. Multiple isoforms of TOCA-1 are known to exist.

Supplier: Proteintech

Villin 1 (VIL1) is a 95-kd F-actin bundling and severing protein and its expression is restricted to epithelial cells with a brush border, like epithelial cells of the intestinal mucosa, gall bladder, renal proximal tubules and ductuli efferentes of the testis. VIL1 has been reported to be an epithelial cell-specific anti-apoptotic protein, and to have an important function in regulating actin dynamics, cell morphology, epithelial-to-mesenchymal transitions, cell migration and cell survival. In addition, VIL1 is a useful diagnostic marker for of various cancer, like cervical and endometrial adenocarcinomas, renal cell carcinoma. VIL1 was recently identified as a novel biomarker predictive for postoperative recurrence and poorer prognosis of high serum AFP associated HCC.

Supplier: Proteintech

Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin (ZYX) is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles.

Supplier: Prosci

KANK3 Antibody: Ankyrins are membrane adaptor molecules that play important roles in the control of cytoskeleton formation by regulating actin polymerization. Like other members of the KANK family, KANK3 (KN motif and ankyrin repeat domain-containing protein 3), is thought to play a role in the formation of actin stress fibers. In zebrafish, the homolog of KANK3 interacts with the adaptor protein Numb, a protein implicated in multiple basic cellular processes, and is essential for epidermal integrity and neurulation, suggesting that KANK3 may play a similar role in higher organisms.

Supplier: Prosci

KANK2 Antibody: Ankyrins are membrane adaptor molecules that play important roles in the control of cytoskeleton formation by regulating actin polymerization. KANK2 (KN motif and ankyrin repeat domain-containing protein 2), was initially identified as a steroid receptor coactivator (SRC) interacting protein (SIP) that could sequester steroid receptor coactivators in the cytoplasm. More recent experiments have shown that while KANK2 is widely expressed, in kidney podocytes, KANK2 localizes to foot processes, suggesting that KANK2 may contribute to controlling actin dynamics in podocyte foot processes.

Supplier: Prosci

Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

Supplier: Prosci

KLHL1 Antibody: The mammalian Kelch-like 1 (KLHL1) was initially discovered as a homolog to the Drosophila Kelch gene that is highly expressed in several brain tissues. The predicted protein domain structure of KLHL1 is characteristic of a number of proteins that bind actin, form dimers, and often act as actin-organizing proteins. Based on the presence of anti-sense RNA that spans the transcription and translation start sites as well as the first splice site of KLHL1 in brain tissue of individuals suffering from the neurodegenerative disorder spinocerebellar ataxia type 8 (SCA8), it has been suggested that KLHL1 is involved this disease and that regulation of KLHL1 protein may be affected by antisense RNA expression.

Supplier: Prosci

Bmf Antibody: Apoptosis is related to many diseases and development. Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3-only proteins, including Bad, Bid, Bik, Hrk, Bim, Noxa, and PUMA, form a growing subclass of the Bcl-2 family. A novel BH3-only protein was recently identified in human and mouse and designated Bmf (for Bcl-2-modifing factor). The BH3 domain in Bmf is required both for binding to Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf associates with the dynein light chain 2 (DLC2) component of the myosin V motors and is sequestered by the cell's actin cytoskeleton. Disruption of the actin cytoskeleton, either by depolymerization of actin filaments or by detachment of cells from the extracellular matrix, triggers release and activation of Bmf, initiating the downstream apoptotic program. Bmf is constitutively expressed in many tissues.

Supplier: Prosci

Podoplanin is a type-1 transmembrane protein that belongs to Podoplanin family. PDPN expressed in various specialized cell types throughout the body. It highly expressed in placenta, lung, skeletal muscle and brain, weakly expressed in brain, kidney and liver. In placenta, PDPN expressed on the apical plasma membrane of endothelium, in lung, expressed in alveolar epithelium. PDPN physiological function is related to its mucin-type character. PDPN may be involved in cell migration and/or actin cytoskeleton organization. When expressed in keratinocytes, induces changes in cell morphology with transfected cells showing an elongated shape, numerous membrane protrusions, and major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion. It requires for normal lung cell proliferation and alveolus formation at birth and Induces platelet aggregation. Nevertheless, it doesn’t have any effect on amino acid transport and the aquaporin-type water channels.

Supplier: Bioss

Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.

Supplier: Bioss

Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.

Supplier: Bioss

Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.

Supplier: Bioss

HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.

Supplier: Bioss

HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.

Supplier: Bioss

HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.

Supplier: Bioss

Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.