66857 Results for: "Rosolic acid (actin)"

Supplier: Proteintech

AIF1, also named as G1, IBA1 or daintain/AIF-1, is a 143 amino acid cytoplasmic, inflammation response scaffold protein. It is constitutively expressed in monocytes and macrophages and is known to be involved in macrophage activation. It is a marker of activated macrophage. Despite a lack of detailed knowledge on the in vivo physiological functions of AIF-1, there is growing evidence that shows its aberrant expression contributes to the pathogenesis of many autoimmune diseases, including rheumatoid arthritis. (20944424). AIF1 is an actin-binding protein that enhances membrane ruffling and RAC activation. It enhances lymphocyte migration and the actin-bundling activity of LCP1. AIF1 plays a role in RAC signaling and in phagocytosis and a role in vascular inflammation. AIF1 promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. It is also as a microglial cell marker.

Supplier: Prosci

AFAP1 Antibody: The actin filament-associated protein AFAP1 (AFAP-110) is an actin cross-linking protein first identified as a substrate of the viral oncogene v-Src. AFAP1 has a fundamental role in actin cytoskeleton arrangement. It contains a carboxyterminal actin-binding domain that directly binds to F-actin and serves as an adaptor protein in the regulation of SRC and PKC signal transduction by several functional domains, including 2 pleckstrin homology (PH) domains, a Src homology 3-binding (SH3-binding) motif, and several SH2-binding motifs. It is overexpressed in prostate carcinoma and contributes to tumor growth by regulating cell-matrix adhesions and migration in the cancer cells. AFAP1 represent a possible therapeutic target for controlling tumorigenesis and metastasis.

Supplier: Prosci

Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Adducins are heteromeric proteins composed of different subunits referred to as adducin alpha, beta and gamma. The three subunits are encoded by distinct genes and belong to a family of membrane skeletal proteins involved in the assembly of spectrin-actin network in erythrocytes and at sites of cell-cell contact in epithelial tissues. While adducins alpha and gamma are ubiquitously expressed, the expression of adducin beta is restricted to brain and hematopoietic tissues. Adducin, originally purified from human erythrocytes, was found to be a heterodimer of adducins alpha and beta. Polymorphisms resulting in amino acid substitutions in these two subunits have been associated with the regulation of blood pressure in an animal model of hypertension. Heterodimers consisting of alpha and gamma subunits have also been described. Structurally, each subunit is comprised of two distinct domains. The amino-terminal region is protease resistant and globular in shape, while the carboxy-terminal region is protease sensitive. The latter contains multiple phosphorylation sites for protein kinase C, the binding site for calmodulin, and is required for association with spectrin and actin. Various adducin beta mRNAs, alternatively spliced at 3'end and/or internally spliced and encoding different isoforms, have been described. The functions of all the different isoforms are not known.

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: Peprotech

GMF-β is a brain-specific protein that belongs to the actin-binding proteins ADF structural family. GMF-β appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines. Recombinant Human GMF-β is a 16.5 kDa globular protein containing 141 amino acid residues, including one intramolecular disulfide bond.

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

GDE3, also known as glycerophosphodiester phosphodiesterase 3, glycerophosphodiester phosphodiesterase domain containing 2 (GDPD2) or osteoblast differentiation promoting factor (OBDPF), is a 539 amino acid protein belonging to the glycerophosphoryl diester phosphodiesterase family. Possessing glycerophosphoinositol inositolphosphodiesterase activity, GDE3 hydrolyzes glycerophosphoinositol to form inositol 1-phosphate and glycerol, and is suggested to play a role in Actin cytoskeleton remodeling and osteoblast differentiation and growth. A multi-pass membrane protein, GDE3 localizes to cell membrane and cytoplasm, and colocalizes with actin in the cytoskeleton. GDE3 contains one GDPD domain, binds calcium as a cofactor and is encoded by a gene mapping to human chromosome Xq13.1.

Supplier: Bioss

GDE3, also known as glycerophosphodiester phosphodiesterase 3, glycerophosphodiester phosphodiesterase domain containing 2 (GDPD2) or osteoblast differentiation promoting factor (OBDPF), is a 539 amino acid protein belonging to the glycerophosphoryl diester phosphodiesterase family. Possessing glycerophosphoinositol inositolphosphodiesterase activity, GDE3 hydrolyzes glycerophosphoinositol to form inositol 1-phosphate and glycerol, and is suggested to play a role in Actin cytoskeleton remodeling and osteoblast differentiation and growth. A multi-pass membrane protein, GDE3 localizes to cell membrane and cytoplasm, and colocalizes with actin in the cytoskeleton. GDE3 contains one GDPD domain, binds calcium as a cofactor and is encoded by a gene mapping to human chromosome Xq13.1.

Supplier: Prosci

KRT24 is a member of the type I (acidic) keratin family, which belongs to the superfamily of intermediate filament (IF) proteins. Keratins are heteropolymeric structural proteins which form the intermediate filament. These filaments, along with actin microfilaments and microtubules, compose the cytoskeleton of epithelial cells. The type I keratin genes are clustered in a region of chromosome 17q12-q21.

Supplier: Prosci

GMF-β a brain-specific protein that belongs to the actin-binding proteins (ADF) structural family. GMF-β appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines. Recombinant human GMF-β is a 16.5 kDa globular protein containing 141 amino acid residues including one intramolecular disulfide bond.

Supplier: Thermo Scientific

The protein encoded by this gene is a member of a family of actin-related proteins which share significant amino acid sequence identity to conventional actins. Both actins and ARPs have an actin fold, which is an ATP-binding cleft, as a common feature. The ARPs are involved in diverse cellular processes, including vesicular transport, spindle orientation, nuclear migration and chromatin remodeling. This gene , and related gene, ACTL7A, are intronless, and are located approximately 4 kb apart in a head-to-head orientation within the familial dysautonomia candidate region on 9q31. Based on mutational analysis of the ACTL7B gene in patients with this disorder, it was concluded that it is unlikely to be involved in the pathogenesis of dysautonomia. Unlike ACTL7A, the ACTL7B gene is expressed predominantly in the testis, however, its exact function is not known.

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: Proteintech

Tropomyosins are ubiquitous proteins of 30 to 45 kD associated with the actin filaments of myofibrils and stress fibers.

Supplier: Bioss

GDE3, also known as glycerophosphodiester phosphodiesterase 3, glycerophosphodiester phosphodiesterase domain containing 2 (GDPD2) or osteoblast differentiation promoting factor (OBDPF), is a 539 amino acid protein belonging to the glycerophosphoryl diester phosphodiesterase family. Possessing glycerophosphoinositol inositolphosphodiesterase activity, GDE3 hydrolyzes glycerophosphoinositol to form inositol 1-phosphate and glycerol, and is suggested to play a role in Actin cytoskeleton remodeling and osteoblast differentiation and growth. A multi-pass membrane protein, GDE3 localizes to cell membrane and cytoplasm, and colocalizes with actin in the cytoskeleton. GDE3 contains one GDPD domain, binds calcium as a cofactor and is encoded by a gene mapping to human chromosome Xq13.1.

Supplier: Bioss

Cortactin is an 80/85 kDa cytoskeleton protein that facilitates assembly of cortical actin. Cortactin is widely expressed in most adherent cells and is a prominent substrate of protein tyrosine kinase Src in vivo and in vitro. The protein sequence of cortactin contains multiple amino terminal tandem repeats of a unique 37 amino acid sequence, which associates with actin, and a Src homology 3 (SH3) domain at the carboxyl terminus. Between the repeat and the SH3 domain, there is an alpha helical structure followed by a proline rich region. Between the proline rich region and the SH3 domain, there are a series of Src phosphorylation sites (Tyr421, Tyr470, and Tyr486). In vitro, cortactin binds to and cross links F actin into meshworks.

Supplier: Proteintech

Actin filament-associated protein 1 is a protein that in humans is encoded by the AFAP1 gene. The protein encoded by this gene is a Src binding partner. It may represent a potential modulator of actin filament integrity in response to cellular signals, and may function as an adaptor protein by linking Src family members and/or other signaling proteins to actin filaments.

Supplier: Proteintech

ACTA2 (also known as α-smooth muscle actin or α-SMA) belongs to the actin family. Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. ACTA2 is primarily expressed in vascular smooth muscle and anti-ACTA2 is commonly used to marker smooth muscle cells. This antibody may cross-react with other isoforms of actins.

Supplier: Proteintech

SEPT2, also named as DIFF6, KIAA0158, NEDD5 and Septin-2, belongs to the septin family. It is a filament-forming cytoskeletal GTPase. SEPT2 is required for normal organization of the actin cytoskeleton. It plays a role in ciliogenesis and collective cell movements. SEPT2 is coordinated expression with SEPT6 and SEPT7.

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

MARCKS-like protein 1 (MARCKSL1) is widely expressed in nervous tissue, it is also named MARCKS-like protein (MLP) or MARCKS-related protein (MRP) and belongs to the MARCKS family, which is a highly acidic myristoylated family of PKC substrates widely distributed in diverse cell types including macrophages. The protein has a calculated molecular weight of 20 kDa and an apparent molecular weight of 42-48 kDa due to anomalous migration on SDS gels or phosphorylation. Genetic disruption of MARCKSL1 results in neural tube closure defects, events that depend on coordinated control of actin functions, cell shape, and cell migration. MARCKSL1 are thought to regulate the actin cytoskeleton and thereby participate in major cellular responses such as phagocytosis, secretion, motility, mitogenesis, and membrane trafficking.

Supplier: Proteintech

MARCKS-like protein 1 (MARCKSL1) is widely expressed in nervous tissue, it is also named MARCKS-like protein (MLP) or MARCKS-related protein (MRP) and belongs to the MARCKS family, which is a highly acidic myristoylated family of PKC substrates widely distributed in diverse cell types including macrophages. The protein has a calculated molecular weight of 20 kDa and an apparent molecular weight of 42-48 kDa due to anomalous migration on SDS gels or phosphorylation. Genetic disruption of MARCKSL1 results in neural tube closure defects, events that depend on coordinated control of actin functions, cell shape, and cell migration. MARCKSL1 are thought to regulate the actin cytoskeleton and thereby participate in major cellular responses such as phagocytosis, secretion, motility, mitogenesis, and membrane trafficking.

Supplier: Proteintech

The family of LIM kinase (LIMK) includes two similar proteins, LIMK1 and LIMK2, that share overall identity of 53% with 75%, 55%, and 42% amino acid identity in the LIM, kinase, and PDZ domains, respectively. LIMK2 regulates actin cytoskeletal reorganization through phosphorylating and inactivating cofilin, an actin-depolymerizing factor of actin filaments. It also may associate with gamma-tubulin and play a role in mitotic spindle assembly. High levels of LIMK2 are evident in uterus, thymus, and spleen whereas lower levels are observed in brain, heart, liver, stomach, skeletal muscle, and testes according to the results of western blotting. It has 3 isoforms produced by alternative splicing of the molecular weight of 70-78 kDa. It can be detected a band of 47 kDa or 50-55 kDa in the testes because the antibody is recognizing the testis-specific variant of LIMK2 and the this difference could be due to species variation.

Supplier: Proteintech

AFAP1L2, also named as Actin filament-associated protein 1-like 2 or XB130, is a 818 amino acid protein, which contains two PH domains. AFAP1L2 is detected in spleen and thyroid, and at lower levels in kidney, brain, lung and pancreas. AFAP1L2 localizes in the cytoplasm and may play a role in a signaling cascade by enhancing the kinase activity of SRC. AFAP1L2 promotes thyroid tumor growth, and its expression in these cancer cells may affect cell proliferation and survival by controlling the expression of multiple genes, especially transcription regulators.

Supplier: Proteintech

Profilin-1 (PFN1) plays an important role in the control of actin dynamics, and could represent an important therapeutic target in several diseases. PFN1 is identified as a huntingtin aggregation inhibitor, and may serves as a tumor-suppressor. PFN1 is crucial for the conversion of monomeric (G)-actin to filamentous (F)-actin. Amyotrophic lateral sclerosis (ALS) is a late-onset neurodegenerative disorder resulting from motor neuron death. Cells expressing PFN1 mutants contain ubiquitinated, insoluble aggregates that in many cases contain the ALS-associated protein TDP-43. Recently, PFN1 is a potential biomarker for bladder cancer aggressiveness and may be of great clinical importance.

Supplier: Prosci

ACTR1A is a 42.6 kD subunit of dynactin, a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit is present in 8-13 copies per dynactin molecule, and is the most abundant molecule in the dynactin complex. It is an actin-related protein, and is approximately 60% identical at the amino acid level to conventional actin.This gene encodes a 42.6 kD subunit of dynactin, a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit is present in 8-13 copies per dynactin molecule, and is the most abundant molecule in the dynactin complex. It is an actin-related protein, and is approximately 60% identical at the amino acid level to conventional actin. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: Proteintech

CAPZA1 (F-actin-capping protein subunit alpha-1) is a member of the F-actin capping protein alpha subunit family and regulates actin filament growth, stability and disassembly. Differential expression of CAPZA1 has been found in gastric cancer and melanoma, indicating its possible role in tumorigenesis. (21566537, 23545944)

Supplier: Proteintech

CAPZA1 (F-actin-capping protein subunit alpha-1) is a member of the F-actin capping protein alpha subunit family and regulates actin filament growth, stability and disassembly. Differential expression of CAPZA1 has been found in gastric cancer and melanoma, indicating its possible role in tumorigenesis. (21566537, 23545944)

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: 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

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.