30935 Results for: "Neu5Ac[1Me,4789Ac]alpha(2-6)Gal[2400,3Bn]-beta-MP"

Supplier: Proteintech

Propionyl-CoA carboxylase (PCC) catalyzes the biotin-dependent carboxylation of propionyl-CoA to D-methyl-malonyl CoA, a reaction that occurs in the mitochondrial matrix. PCC is involved in the catabolism of several essential amino acids (methionine, isoleucine, threonine and valine), as well as odd chain fatty acids and cholesterol. Deficiency of PCC results in propionic acidemia, a metabolic disorder characterized by severe metabolic ketoacidosis, vomiting, lethargy and hypotonia. PCC consists of nonidentical subunits (α and β) encoded by different genes (PCCA and PCCB, respectively). The αPCC cDNA contains an open reading frame of 2106 nucleotide bases and codes for a 702 amino acid polypeptide. The mature length subunit is 70 kDa and contains the biotin binding site.. This protein has 3 isoforms produced by alternative splicing with the molecular weight of 80 kDa, 77 kDa and 75 kDa. The full length protein has a transit peptide with 52 amino acids. This antibody is specific to PCCA.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Tonbo Biosciences

The O323 antibody reacts with human CD27 (TNFRSF7), a cell surface homodimer of 55 kDa subunits, which provides co-stimulatory signaling in support of the T cell (TCR) and B cell (BCR) receptors. By comparison with CD28, whose TCR co-stimulatory signal can trigger cell proliferation, CD27 signaling appears to promote cell survival and differentiation to effector / memory stages. Also in contrast with CD28, the CD27 receptor may be shed following interaction with its ligand CD70, which is typically expressed on activated dendritic cells, T cells and B cells. With respect to B cells, CD27 is considered to be a phenotypic marker for memory B cells. CD27 has been included within a group of phenotypic markers for identifying human B regulatory cells (Bregs), a cell type proposed to regulate CD4+ T cell proliferation and Foxp3 / CTLA-4 expression in Treg cells.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Prosci

CIDE-B Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. DFF45/ICAD has been identified as inhibitor of caspase activated DNase DFF40/CAD. DFF45 related proteins CIDE-A and CIDE-B (for cell death-inducing DFF-like effector A and B) were recently identified. CIDE contains a new type of domain termed CIDE-N, which has high homology with the regulatory domains of DFF45/ICAD and DFF40/CAD. Expression of CIDE-B induces apoptosis, which is inhibited by DFF45. CIDE-B is a DFF45-inhibitable effector that promotes cell death and DNA fragmentation. CIDE-B is expressed mainly in liver and at lower levels in spleen, kidney, peripheral blood lymphocytes, and bone marrow.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Prosci

Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. RXRA is a member of the steroid and thyroid hormone receptor superfamily of transcriptional regulators.Retinoid X receptors (RXRs) and retinoic acid receptors (RARs), are nuclear receptors that mediate the biological effects of retinoids by their involvement in retinoic acid-mediated gene activation. These receptors exert their action by binding, as homodimers or heterodimers, to specific sequences in the promoters of target genes and regulating their transcription. The protein encoded by this gene is a member of the steroid and thyroid hormone receptor superfamily of transcriptional regulators. 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: Enzo Life Sciences

The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits.  Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. Lmp2, Lmp7 and MECL are interferon gamma-inducible catalytic subunits of the 20S proteasome which may replace the constitutive catalytic subunits, delta, X and Z respectively, during proteasome biogenesis. Lmp2 and Lmp7 alter the cleavage site specificity of the 20S proteasome and are required for the efficient generation of T cell epitopes from a number of viral proteins and for optimal MHC class I cell surface expression.

Supplier: Tonbo Biosciences

The C17.8 antibody is specific for the 40 kDa (p40) protein subunit shared by the cytokines IL-12 and IL-23. To form IL-12, p40 assembles with a separate 35 kDa protein known as p35, resulting in a 70 kDa functional cytokine. IL-12 is secreted by activated monocytes, macrophages, and dendritic cells, and has been shown to target naïve, resting CD4+ T cells to promote their proliferation and secretion of cytokines. IL-23 contains the p40 subunit in combination with a 19 kDa protein chain, p19; its primary source being activated dendritic cells and other antigen-presenting cells. IL-23 appears to target different cell types than IL-12, acting on memory CD4+ T cells to induce a strong proliferative response and contributing to the generation and expansion of Th17 cells. Like the cytokines themselves, the receptors for IL-12 and IL-23 share one subunit, as well as containing distinct cytokine-specific subunits.

Supplier: Prosci

Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-κ-B activation and B-cell suvival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652', leading to activate the NF-κ-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also involved in triglyceride homeostasis. Serves as the receptor for phorbol esters, a class of tumor promoters.

Supplier: Prosci

ACTR1B is a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein and 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. ACTR1B, like ACTR1A, is an actin-related protein. These two proteins, which are of equal length and share 90% amino acid identity, are present in a constant ratio of approximately 1:15 in the dynactin complex.This gene encodes a 42.3 kD subunit of dynactin, a macromolecular complex consisting of 10 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, like ACTR1A, is an actin-related protein. These two proteins are of equal length and share 90% amino acid identity. They are present in a constant ratio of approximately 1:15 in the dynactin complex.

Supplier: Tonbo Biosciences

The C17.8 antibody is specific for the 40 kDa (p40) protein subunit shared by the cytokines IL-12 and IL-23. To form IL-12, p40 assembles with a separate 35 kDa protein known as p35, resulting in a 70 kDa functional cytokine. IL-12 is secreted by activated monocytes, macrophages, and dendritic cells, and has been shown to target naïve, resting CD4+ T cells to promote their proliferation and secretion of cytokines. IL-23 contains the p40 subunit in combination with a 19 kDa protein chain, p19; its primary source being activated dendritic cells and other antigen-presenting cells. IL-23 appears to target different cell types than IL-12, acting on memory CD4+ T cells to induce a strong proliferative response and contributing to the generation and expansion of Th17 cells. Like the cytokines themselves, the receptors for IL-12 and IL-23 share one subunit, as well as containing distinct cytokine-specific subunits.

Supplier: Prosci

PPFIBP1 is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein was found to interact with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis.The protein encoded by this gene is a member of the LAR protein-tyrosine phosphatase-interacting protein (liprin) family. Liprins interact with members of LAR family of transmembrane protein tyrosine phosphatases, which are known to be important for axon guidance and mammary gland development. It has been proposed that liprins are multivalent proteins that form complex structures and act as scaffolds for the recruitment and anchoring of LAR family of tyrosine phosphatases. This protein was found to interact with S100A4, a calcium-binding protein related to tumor invasiveness and metastasis. In vitro experiment demonstrated that the interaction inhibited the phosphorylation of this protein by protein kinase C and protein kinase CK2. Alternatively spliced transcript variants encoding distinct isoforms have been reported.

Supplier: Prosci

APP is a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.

Supplier: Enzo Life Sciences

The proteasome is widely recognised as the central enzyme of non-lysosomal protein degradation. It is responsible for intracellular protein turnover and it is also critically involved in many regulatory processes and, in higher eukaryotes, in antigen processing. The 26S proteasome is the key enzyme of the ubiquitin/ATP-dependent pathway of protein degradation. The catalytic core of this unusually large (2000kDa, 450Å in length) complex is formed by the 20S proteasome, a barrel shaped structure shown by electron microscopy to comprise of four rings each containing seven subunits. Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. Lmp2, Lmp7 and MECL are interferon gamma-inducible catalytic subunits of the 20S proteasome which may replace the constitutive catalytic subunits, delta, X and Z respectively, during proteasome biogenesis. Lmp2 and Lmp7 alter the cleavage site specificity of the 20S proteasome and are required for the efficient generation of T cell epitopes from a number of viral proteins and for optimal MHC class I cell surface expression.

Supplier: Prosci

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described.GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described. 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: Prosci

GALNT10 belongs to the polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family. Polypeptide GalNAc transferases initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc from UDP-GalNAc to the hydroxyl group of either a serine or threonine residue on the polypeptide acceptor. Following expression in insect cells, recombinant GalNAc transferase 10 showed significant GalNAcT activity toward mucin-derived peptides, and it utilized both nonglycosylated and glycosylated peptide substrates.This gene belongs to the polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) gene family. Polypeptide GalNAc transferases initiate the synthesis of mucin-type oligosaccharides by transferring GalNAc from UDP-GalNAc to the hydroxyl group of either a serine or threonine residue on the polypeptide acceptor. Following expression in insect cells, recombinant GalNAc transferase 10 showed significant GalNAcT activity toward mucin-derived peptides, and it utilized both nonglycosylated and glycosylated peptide substrates. Two transcript variants encoding distinct isoforms have been identified for this gene.

Supplier: Proteintech

LC3B, also named as MAP1LC3B, MAP1A/1BLC3, belongs to the MAP1 LC3 family. It is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, which are involved in microtubule assembly and important for neurogenesis. In cell biology, autophagy, or autophagocytosis, is a catabolic process involving the degradation of a cell's own components through the lysosomalmachinery. It is a major mechanism by which a starving cell reallocates nutrients from unnecessary processes to more-essential processes. Two forms of LC3, called LC3-I (17-19kd) and -II(14-16kd), were produced post-translationally in various cells. LC3-I is cytosolic, whereas LC3-II is membrane bound. The precursor molecule is cleaved by APG4B/ATG4B to form the cytosolic form, LC3-I. This is activated by APG7L/ATG7, transferred to ATG3 and conjugated to phospholipid to form the membrane-bound form, LC3-II. The amount of LC3-II is correlated with the extent of autophagosome formation. LC3-II is the first mammalian protein identified that specifically associates with autophagosome membranes. MAP1LC3 has 3 isoforms MAP1LC3A, MAP1LC3B and MAP1LC3C. MAP1LC3A and MAP1LC3C are produced by the proteolytic cleavage after the conserved C-terminal Gly residue, like their rat counterpart, MAP1LC3B does not undergo C-terminal cleavage and exists in a single modified form. This antibody is specific to LC3B.

Supplier: Prosci

GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described.GABA is the major inhibitory neurotransmitter in the mammalian brain where it acts at GABA-A receptors, which are ligand-gated chloride channels. Chloride conductance of these channels can be modulated by agents such as benzodiazepines that bind to the GABA-A receptor. At least 16 distinct subunits of GABA-A receptors have been identified. Transcript variants utilizing three different alternative non-coding first exons have been described. 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: Bioss

cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. This gene encodes one of the regulatory subunits. This protein was found to be a tissue-specific extinguisher that down-regulates the expression of seven liver genes in hepatoma x fibroblast hybrids. Mutations in this gene cause Carney complex (CNC). This gene can fuse to the RET protooncogene by gene rearrangement and form the thyroid tumor-specific chimeric oncogene known as PTC2. A nonconventional nuclear localization sequence (NLS) has been found for this protein which suggests a role in DNA replication via the protein serving as a nuclear transport protein for the second subunit of the Replication Factor C (RFC40). Three alternatively spliced transcript variants encoding the same protein have been observed. [provided by RefSeq, Jul 2008].

Supplier: Genetex

Methylation of DNA at cytosine residues plays an important role in regulation of gene expression, genomic imprinting and is essential for mammalian development. Hypermethylation of CpG islands in tumor suppressor genes or hypomethylation of bulk genomic DNA may be linked with development of cancer. To date, 3 families of mammalian DNA methyltransferase genes have been identified which include Dnmt1, Dnmt2 and Dnmt3. Dnmt1 is constitutively expressed in proliferating cells and inactivation of this gene causes global demethylation of genomic DNA and embryonic lethality. Dnmt2 is expressed at low levels in adult tissues and its inactivation does not affect DNA methylation or maintenance of methylation. The Dnmt3 family members, Dnmt3a and Dnmt3b, are strongly expressed in ES cells but their expression is down regulated in differentiating ES cells and is low in adult somatic tissue. Dnmt 1 co-purifies with the retinoblastoma (Rb) tumour suppressor gene product, E2F1, and HDAC1. Dnmt 1 also cooperates with Rb to repress transcription from promoters containing E2F binding sites suggesting a link between DNA methylation, histone deacetylase and sequence-specific DNA binding activity, as well as a growth-regulatory pathway that is disrupted in nearly all cancer cells.

Supplier: Prosci

PRKAA1 belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways.The protein encoded by this gene belongs to the ser/thr protein kinase family. It is the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK). AMPK is a cellular energy sensor conserved in all eukaryotic cells. The kinase activity of AMPK is activated by the stimuli that increase the cellular AMP/ATP ratio. AMPK regulates the activities of a number of key metabolic enzymes through phosphorylation. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. Alternatively spliced transcript variants encoding distinct isoforms have been observed.

Supplier: Prosci

Interleukin 11 is a stromal cell-derived cytokine that belongs to a family of pleiotropic and redundant cytokines that use the gp130 transducing subunit in their high affinity receptors. IL11RA is the IL-11 receptor, which is a member of the hematopoietic cytokine receptor family. This particular receptor is very similar to ciliary neurotrophic factor, since both contain an extracellular region with a 2-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain.Interleukin 11 is a stromal cell-derived cytokine that belongs to a family of pleiotropic and redundant cytokines that use the gp130 transducing subunit in their high affinity receptors. This gene encodes the IL-11 receptor, which is a member of the hematopoietic cytokine receptor family. This particular receptor is very similar to ciliary neurotrophic factor, since both contain an extracellular region with a 2-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. Alternative splicing has been observed at this locus and two variants, each encoding a distinct isoform, have been identified.

Supplier: Prosci

PPP1CA is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory.The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Supplier: Prosci

Interleukin 11 is a stromal cell-derived cytokine that belongs to a family of pleiotropic and redundant cytokines that use the gp130 transducing subunit in their high affinity receptors. IL11RA is the IL-11 receptor, which is a member of the hematopoietic cytokine receptor family. This particular receptor is very similar to ciliary neurotrophic factor, since both contain an extracellular region with a 2-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain.Interleukin 11 is a stromal cell-derived cytokine that belongs to a family of pleiotropic and redundant cytokines that use the gp130 transducing subunit in their high affinity receptors. This gene encodes the IL-11 receptor, which is a member of the hematopoietic cytokine receptor family. This particular receptor is very similar to ciliary neurotrophic factor, since both contain an extracellular region with a 2-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. Alternative splicing has been observed at this locus and two variants, each encoding a distinct isoform, have been identified.

Supplier: Prosci

The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The family member CHRNA7 is located on chromosome 15 in a region associated with several neuropsychiatric disorders. CHRFAM7A is is a hybrid between CHRNA7 and FAM7A. The nicotinic acetylcholine receptors (nAChRs) are members of a superfamily of ligand-gated ion channels that mediate fast signal transmission at synapses. The family member CHRNA7, which is located on chromosome 15 in a region associated with several neuropsychiatric disorders, is partially duplicated and forms a hybrid with a novel gene from the family with sequence similarity 7 (FAM7A). Alternative splicing has been observed, and two variants exist, for this hybrid gene. The N-terminally truncated products predicted by the largest open reading frames for each variant would lack the majority of the neurotransmitter-gated ion-channel ligand binding domain but retain the transmembrane region that forms the ion channel. Although current evidence supports transcription of this hybrid gene, translation of the nicotinic acetylcholine receptor-like protein-encoding open reading frames has not been confirmed.

Supplier: Prosci

A4GNT is a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1-->4Galbeta-->R and is largely associated with the Golgi apparatus membrane.This gene encodes a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1-->4Galbeta-->R and is largely associated with the Golgi apparatus membrane. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments.This gene encodes a protein from the glycosyltransferase 32 family. The enzyme catalyzes the transfer of N-acetylglucosamine (GlcNAc) to core 2 branched O-glycans. It forms a unique glycan, GlcNAcalpha1-->4Galbeta-->R and is largely associated with the Golgi apparatus membrane. Sequence Note: The RefSeq transcript and protein were derived from genomic sequence to make the sequence consistent with the reference genome assembly. The genomic coordinates used for the transcript record were based on alignments.

Supplier: Biosensis

Tyrosine hydroxylase is an excellent marker for dopaminergic and noradrenergic neurons. Tyrosine hydroxylase (a.k.a. tyrosine 3-monooxygenase) is the enzyme responsible for catalyzing the conversion of the amino acid L-tyrosine to L-3,4-dihydroxyphenylalanine (L-DOPA). L-DOPA is a precursor for dopamine, which, in turn, is a precursor for the important neurotransmitters norepinephrine (noradrenaline) and epinephrine (adrenaline). Tyrosine hydroxylase catalyzes the rate limiting step in this synthesis of catecholamines. In humans, tyrosine hydroxylase is encoded by the TH gene, and the enzyme is present in the central nervous system (CNS), peripheral symphatic neurons and the adrenal medulla. The enzymatic activity of TH requires ferrous ions as cofactors and is believed to be regulated by phosphorylation. At least four isoforms of human TH have been identified which result from alternative splicing. Tyrosine hydroxylase, phenylalanine hydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs). http://en.wikipedia.org/wiki/Tyrosine_hydroxylase

Supplier: Prosci

Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRB is thought to act as a cellular signaling activating receptor that associates with ITAM-bearing adapter molecules on the cell surface.Cell signaling pathways rely on a dynamic interaction between activating and inhibiting processes. SHP-1-mediated dephosphorylation of protein tyrosine residues is central to the regulation of several cell signaling pathways. Two types of inhibitory receptor superfamily members are immunoreceptor tyrosine-based inhibitory motif (ITIM)-bearing receptors and their non-ITIM-bearing, activating counterparts. Control of cell signaling via SHP-1 is thought to occur through a balance between PILRalpha-mediated inhibition and PILRbeta-mediated activation. These paired immunoglobulin-like receptor genes are located in a tandem head-to-tail orientation on chromosome 7. This particular gene encodes the non-ITIM-bearing member of the receptor pair, which has a truncated cytoplasmic tail relative to its ITIM-bearing partner and functions in the activating role. Alternative splicing has been observed at this locus and three variants, encoding two distinct isoforms, are described. Additional transcript variants have been identified but their full-length nature has not been determined.

Supplier: Bioss

May modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues.Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site. SerpinA12, also known as OL-64, Visceral adipose tissue-derived serine protease inhibitor, Vaspin, Visceral adipose-specific serpin and SERPINA12, is a secreted protein which belongs to the serpin family. SerpinA12 / Vaspin is expressed in visceral adipose tissues. It may modulates insulin action conceivably only in the presence of its yet undefined target proteases in white adipose tissues. SerpinA12 / Vaspin may be the compensatory molecule in the pathogenesis of metabolic syndrome and SerpinA12 / Vaspin recombinant protein or vaspin-mimicking agents such as vaspin analogs, or small molecule agents may be the link to drug discovery and development.