351 Results for: "200479"

Supplier: Bioss

The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).[supplied by OMIM, May 2008].

Supplier: Bioss

The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).[supplied by OMIM, May 2008].

Supplier: Bioss

The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).[supplied by OMIM, May 2008].

Supplier: Bioss

The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).[supplied by OMIM, May 2008].

Supplier: Genetex

GBA3, or cytosolic beta-glucosidase (EC 3.2.1.21), is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides (de Graaf et al., 2001 [PubMed 11389701]). GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism (Hayashi et al., 2007 [PubMed 17595169]).[supplied by OMIM]

Supplier: Prosci

HPRT1 has a central role in the generation of purine nucleotides through the purine salvage pathway. HPRT1 catalyzes conversion of hypoxanthine to inosine monophosphate and guanine to guanosine monophosphate via transfer of the 5-phosphoribosyl group from 5-phosphoribosyl 1-pyrophosphate.HPRT1 has a central role in the generation of purine nucleotides through the purine salvage pathway. HPRT1 catalyzes conversion of hypoxanthine to inosine monophosphate and guanine to guanosine monophosphate via transfer of the 5-phosphoribosyl group from 5-phosphoribosyl 1-pyrophosphate (Keebaugh et al., 2007 [PubMed 16928426]).

Supplier: Bioss

The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).[supplied by OMIM, May 2008].

Supplier: Prosci

Sodium hydrogen antiporters, such as NHEDC2, convert the proton motive force established by the respiratory chain or the F1F0 mitochondrial ATPase into sodium gradients that drive other energy-requiring processes, transduce environmental signals into cell responses, or function in drug efflux.Sodium hydrogen antiporters, such as NHEDC2, convert the proton motive force established by the respiratory chain or the F1F0 mitochondrial ATPase into sodium gradients that drive other energy-requiring processes, transduce environmental signals into cell responses, or function in drug efflux (Xiang et al., 2007 [PubMed 18000046]).

Supplier: Prosci

GBA3, or cytosolic beta-glucosidase (EC 3.2.1.21), is a predominantly liver enzyme that efficiently hydrolyzes beta-D-glucoside and beta-D-galactoside, but not any known physiologic beta-glycoside, suggesting that it may be involved in detoxification of plant glycosides (de Graaf et al., 2001 [PubMed 11389701]). GBA3 also has significant neutral glycosylceramidase activity (EC 3.2.1.62), suggesting that it may be involved in a nonlysosomal catabolic pathway of glucosylceramide metabolism (Hayashi et al., 2007 [PubMed 17595169]).

Supplier: Bioss

The content of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) in endosomal membranes changes dynamically with fission and fusion events that generate or absorb intracellular transport vesicles. VAC14 is a component of a trimolecular complex that tightly regulates the level of PtdIns(3,5)P2. Other components of this complex are the PtdIns(3,5)P2-synthesizing enzyme PIKFYVE (MIM 609414) and the PtdIns(3,5)P2 phosphatase FIG4 (MIM 609390). VAC14 functions as an activator of PIKFYVE (Sbrissa et al., 2007 [PubMed 17556371]).[supplied by OMIM, Feb 2010].

Supplier: Prosci

The sodium-iodide symporter (NIS, or SLC5A5) is a key plasma membrane protein that mediates active I- uptake in thyroid, lactating breast, and other tissues with an electrogenic stoichiometry of 2 Na+ per I-. In thyroid, NIS-mediated I- uptake is the first step in the biosynthesis of iodine-containing thyroid hormones.The sodium-iodide symporter (NIS, or SLC5A5) is a key plasma membrane protein that mediates active I- uptake in thyroid, lactating breast, and other tissues with an electrogenic stoichiometry of 2 Na+ per I-. In thyroid, NIS-mediated I- uptake is the first step in the biosynthesis of iodine-containing thyroid hormones (Dohan et al., 2007 [PubMed 18077370]).

Supplier: Prosci

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system. There are two major classes of GABA receptors: the GABAA and the GABAB subtype of receptors. GABAB receptors are heterodimeric G protein-coupled receptors that mediate slow synaptic inhibition in the central nervous system. It has recently been demonstrated that AMPK binds directly to GABAB receptors and phosphorylates S783 in the cytoplasmic tail of the R2 subunit and that S783 plays a critical role in enhancing neuronal survival after ischemia as phosphorylation of S783 is evident in many brain regions and is increased dramatically after ischemic injury to the brain (Kuramoto et al., 2007).

Supplier: Prosci

REL is a member of the Rel/NFKB family, which also includes RELA, RELB, NFKB1, and NFKB2. These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor.The REL gene encodes c-Rel, a transcription factor that is a member of the Rel/NFKB family, which also includes RELA (MIM 164014), RELB (604758), NFKB1 (MIM 164011), and NFKB2 (MIM 164012). These proteins are related through a highly conserved N-terminal region termed the 'Rel domain,' which is responsible for DNA binding, dimerization, nuclear localization, and binding to the NFKB inhibitor (MIM 164008) (Belguise and Sonenshein, 2007 [PubMed 18037997]).

Supplier: Rockland Immunochemical

Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. In early 2009, a novel H1N1 swine-origin influenza (S-OIV) A virus was identified in specimens obtained from patients in Mexico and the United States. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Supplier: Prosci

ETS2 contains an ETS DNA-binding domain and belongs to the ETS family. ETS2 is a target of protein kinase C and upregulates GM-CSF. Ets2 and its targets play essential roles in endothelial cell function. Coexpression of Ets-2 and SRC-1 significantly associated with the rate of recurrence and HER expression in breast cancer. Overexpression of ETS2 is associated with human esophageal squamous cell carcinoma. ETS transcriptions factors, such as ETS2, regulate numerous genes and are involved in stem cell development, cell senescence and death, and tumorigenesis. The conserved ETS domain within these proteins is a winged helix-turn-helix DNA-binding domain that recognizes the core consensus DNA sequence GGAA/T of target genes (Dwyer et al., 2007 [PubMed 17986575]).

Supplier: Prosci

MPP7 acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. MPP7 is involved in the assembly of protein complexes at sites of cell-cell contact.Membrane-associated guanylate kinases (MAGUKs) are important adaptor proteins involved in the assembly of protein complexes at sites of cell-cell contact. They are found in synapses, adherens junctions, and tight junctions. All MAGUKs contain at least 1 PDZ domain, an SH3 domain, and a GUK domain, and many contain 1 or 2 L27 domains, which are involved in multimerization of MAGUKs. MPP7 belongs to the p55 stardust subfamily of MAGUKs, which is named for a Drosophila gene required for establishment of cell polarity in the developing fly embryo (Bohl et al., 2007 [PubMed 17237226]).

Supplier: Prosci

Inositol phosphates (IPs) and diphosphoinositol phosphates (PP-IPs), also known as inositol pyrophosphates, act as cell signaling molecules. HISPPD1 has both IP6 kinase (EC 2.7.4.21) and PP-IP5 (also called IP7) kinase (EC 2.7.4.24) activities that produce the high-energy pyrophosphates PP-IP5 and PP2-IP4 (also called IP8), respectively.Inositol phosphates (IPs) and diphosphoinositol phosphates (PP-IPs), also known as inositol pyrophosphates, act as cell signaling molecules. HISPPD1 has both IP6 kinase (EC 2.7.4.21) and PP-IP5 (also called IP7) kinase (EC 2.7.4.24) activities that produce the high-energy pyrophosphates PP-IP5 and PP2-IP4 (also called IP8), respectively (Fridy et al., 2007 [PubMed 17690096]).

Supplier: Prosci

The KCTD gene family, including KCTD7, encode predicted proteins that contain N-terminal domain that is homologous to the T1 domain in voltage-gated potassium channels (see KCNA1; MIM 176260). KCTD7 displays a primary sequence and hydropathy profile indicating intracytoplasmic localization. EST database analysis showed that KCTD7 is expressed in human and mouse brain.The KCTD gene family, including KCTD7, encode predicted proteins that contain N-terminal domain that is homologous to the T1 domain in voltage-gated potassium channels (see KCNA1; MIM 176260). KCTD7 displays a primary sequence and hydropathy profile indicating intracytoplasmic localization. EST database analysis showed that KCTD7 is expressed in human and mouse brain (Van Bogaert et al., 2007 [PubMed 17455289]).

Supplier: Prosci

Swine H1N1 Hemagglutinin Monoclonal Antibody: Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. In early 2009, a novel H1N1 swine-origin influenza (S-OIV) A virus was identified in specimens obtained from patients in Mexico and the United States. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Supplier: Prosci

Gamma-aminobutyric acid (GABA) is the primary inhibitory neurotransmitter in the central nervous system. There are two major classes of GABA receptors: the GABAA and the GABAB subtype of receptors. GABAA-Rs are important therapeutic targets for a range of sedative, anxiolytic, and hypnotic agents and are implicated in several diseases including epilepsy, anxiety, depression, and sub-stance abuse. The GABAA-R is a multimeric subunit complex. To date six alphas, four betas and four gamma;s, plus alternative splicing variants of some of these subunits, have been identified (Olsen and Tobin, 1990; Whiting et al., 1999; Ogris et al., 2004). Injection in oocytes or mammalian cell lines of cRNA coding for alpha- and beta-subunits results in the expression of functional GABAA-Rs sensitive to GABA. However, coexpression of a gamma-subunit is required for benzodiazepine modulation. It has recently been suggested that PKCepsilon regulates the sensitivity of GABAA alpha1beta2gamma2 receptors to ethanol and benzodiazepines through phosphorylation of serine 327 in the large intracellular loop of gamma2 (Qi et al., 2007)

Supplier: Prosci

Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.

Supplier: Prosci

Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.

Supplier: Prosci

Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.

Supplier: Prosci

Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.

Supplier: Rockland Immunochemical

Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Supplier: Prosci

Swine H1N1 Hemagglutinin Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups. This antibody is specific for the novel swine influenza Hemagglutinin and will not recognize the corresponding Hemagglutinin sequence from the seasonal H1N1 influenza (A/Brisbane/59/2007 (H1N1)).

Supplier: Prosci

Hemagglutinin Monoclonal Antibody: Influenza A virus is a major public health threat, killing more than 30,000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. The more recent virulent strain of H5N1 is now seen in Africa and Europe, as well as in southeast Asia. There is some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability. While efforts were made to use relatively conserved regions of the viral sequence as the antigen, the influenza virus genome has drifted somewhat from what was first reported. However, this antibody was able to recognize peptides derrived from viruses from Indonesian human patients infected in 2007.

Supplier: Inorganic Ventures

200.7 CALIBRATION STANDARD

Supplier: Inorganic Ventures

200.7 CALIBRATION STANDARD

Supplier: Matrix Scientific

Matrix Scientific Part Number: 061868-500MG , MDL Number: MFCD12197818