3059 Results for: "6-NED+NHS+ester&pageNo=71"

Supplier: Bioss

Enteroviruses, such as enterovirus 71, are classified to be in the picornavirus family, pico [small] + RNA [ribonucleic acid] + virus. Picornaviruses are among the smallest and simplest ribonucleic acid containing viruses known (1). The RNA for many enteroviruses have now been cloned and complete genomic sequences have been obtained. The RNA from all sequenced enteroviruses are similar in length, about 7400 nucleotides, and have identical organization (1). The human alimentary tract is the predominant site of enterovirus replication and these viruses were first isolated from enteric specimens. These viruses are the cause of paralytic poliomyelitis, aseptic meningitis-encephalitis, myocarditis, pleurodynia, hand-foot-and-mouth disease, conjunctivitis, and numerous other syndromes associated with extra-intestinal target organs. There are 67 numbered types of enteroviruses in the enterovirus family (1): three polioviruses, twenty-three coxsackieviruses A, six coxsackieviruses B, thirty-one echoviruses, and four other enteroviruses.

Supplier: Bioss

Enteroviruses, such as enterovirus 71, are classified to be in the picornavirus family, pico [small] + RNA [ribonucleic acid] + virus. Picornaviruses are among the smallest and simplest ribonucleic acid containing viruses known (1). The RNA for many enteroviruses have now been cloned and complete genomic sequences have been obtained. The RNA from all sequenced enteroviruses are similar in length, about 7400 nucleotides, and have identical organization (1). The human alimentary tract is the predominant site of enterovirus replication and these viruses were first isolated from enteric specimens. These viruses are the cause of paralytic poliomyelitis, aseptic meningitis-encephalitis, myocarditis, pleurodynia, hand-foot-and-mouth disease, conjunctivitis, and numerous other syndromes associated with extra-intestinal target organs. There are 67 numbered types of enteroviruses in the enterovirus family (1): three polioviruses, twenty-three coxsackieviruses A, six coxsackieviruses B, thirty-one echoviruses, and four other enteroviruses.

Supplier: ProSci Inc.

DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex.DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). However, unlike the other family members, MBD3 is not capable of binding to methylated DNA. The predicted MBD3 protein shares 71% and 94% identity with MBD2 (isoform 1) and mouse Mbd3. MBD3 is a subunit of the NuRD, a multisubunit complex containing nucleosome remodeling and histone deacetylase activities. MBD3 mediates the association of metastasis-associated protein 2 (MTA2) with the core histone deacetylase complex. 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

Enteroviruses, such as enterovirus 71, are classified to be in the picornavirus family, pico [small] + RNA [ribonucleic acid] + virus. Picornaviruses are among the smallest and simplest ribonucleic acid containing viruses known (1). The RNA for many enteroviruses have now been cloned and complete genomic sequences have been obtained. The RNA from all sequenced enteroviruses are similar in length, about 7400 nucleotides, and have identical organization (1). The human alimentary tract is the predominant site of enterovirus replication and these viruses were first isolated from enteric specimens. These viruses are the cause of paralytic poliomyelitis, aseptic meningitis-encephalitis, myocarditis, pleurodynia, hand-foot-and-mouth disease, conjunctivitis, and numerous other syndromes associated with extra-intestinal target organs. There are 67 numbered types of enteroviruses in the enterovirus family (1): three polioviruses, twenty-three coxsackieviruses A, six coxsackieviruses B, thirty-one echoviruses, and four other enteroviruses.

Supplier: Bioss

Enteroviruses, such as enterovirus 71, are classified to be in the picornavirus family, pico [small] + RNA [ribonucleic acid] + virus. Picornaviruses are among the smallest and simplest ribonucleic acid containing viruses known (1). The RNA for many enteroviruses have now been cloned and complete genomic sequences have been obtained. The RNA from all sequenced enteroviruses are similar in length, about 7400 nucleotides, and have identical organization (1). The human alimentary tract is the predominant site of enterovirus replication and these viruses were first isolated from enteric specimens. These viruses are the cause of paralytic poliomyelitis, aseptic meningitis-encephalitis, myocarditis, pleurodynia, hand-foot-and-mouth disease, conjunctivitis, and numerous other syndromes associated with extra-intestinal target organs. There are 67 numbered types of enteroviruses in the enterovirus family (1): three polioviruses, twenty-three coxsackieviruses A, six coxsackieviruses B, thirty-one echoviruses, and four other enteroviruses.

Supplier: Bioss

Enteroviruses, such as enterovirus 71, are classified to be in the picornavirus family, pico [small] + RNA [ribonucleic acid] + virus. Picornaviruses are among the smallest and simplest ribonucleic acid containing viruses known (1). The RNA for many enteroviruses have now been cloned and complete genomic sequences have been obtained. The RNA from all sequenced enteroviruses are similar in length, about 7400 nucleotides, and have identical organization (1). The human alimentary tract is the predominant site of enterovirus replication and these viruses were first isolated from enteric specimens. These viruses are the cause of paralytic poliomyelitis, aseptic meningitis-encephalitis, myocarditis, pleurodynia, hand-foot-and-mouth disease, conjunctivitis, and numerous other syndromes associated with extra-intestinal target organs. There are 67 numbered types of enteroviruses in the enterovirus family (1): three polioviruses, twenty-three coxsackieviruses A, six coxsackieviruses B, thirty-one echoviruses, and four other enteroviruses.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: MIELE

The Aqua-Soft system provides a continual supply of soft water and is suitable for water with a hardness up to 71° dH. It operates as a level controlled two-tank system, consisting of two cartridges with ion exchange resins and a salt reservoir. The resins are enriched with sodium ions. The hard water flows over the resins in the first cartridge, where calcium and magnesium ions are exchanged for sodium ions. At this time, no water is flowing through the second cartridge. When one cartridge is exhausted, the water is routed to the second cartridge by means of a hardness level selector corresponding to the hardness of the local water, which is inserted by customer service when the device is used for the first time. At the same time, the regeneration of the resins from the exhausted container is activated. For this treatment, brine (NaCl) is drawn from the salt reservoir. The reservoir must be replenished regularly with coarse salt pellets. Fill quantity approx. 25 kg.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: Bioss

Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

Supplier: VWR Chemicals

A standard mixture, typically used for food testing, containing the following components: 100 ug/ml each of Acibenzolar-S-methyl [CAS:135158-54-2] ; Bupirimate [CAS:41483-43-6] ; Buprofezin [CAS:69327-76-0] ; Carboxin [CAS:5234-68-4] ; Clethodim [CAS:99129-21-2] ; Clothianidin [CAS:210880-92-5] ; Cyazofamid [CAS:120116-88-3] ; Ethiprole [CAS:181587-01-9] ; Ethofumesate [CAS:26225-79-6] ; Fenamidone [CAS:161326-34-7] ; Fipronil [CAS:120068-37-3] ; Flubendiamide [CAS:272451-65-7] ; Flufenacet [CAS:142459-58-3] ; Hexythiazox [CAS:78587-05-0] ; Mefenacet [CAS:73250-68-7] ; Mesotrione [CAS:104206-82-8] ; Methoprotryne [CAS:841-06-5] ; Metribuzin [CAS:21087-64-9] ; Prometryn [CAS:7287-19-6] ; Propargite [CAS:2312-35-8] ; Prothioconazole [CAS:178928-70-6] ; Pyridaben [CAS:96489-71-3] ; Simetryn [CAS:1014-70-6] ; Sulfentrazone [CAS:122836-35-5] ; Terbutryn [CAS:886-50-0] ; Thiabendazole [CAS:148-79-8] ; Thiacloprid [CAS:111988-49-9] ; Thiamethoxam [CAS:153719-23-4] ; Thiofanox [CAS:39196-18-4] ; Tricyclazole [CAS:41814-78-2] in Acetonitrile

Supplier: Biotium

Recognizes a sialoglycoprotein of 27-32 kDa, identified as CD99, or MIC2 gene product, or E2 antigen. MIC2 gene is located in the pseudo-autosomal region of the human X and Y chromosome. MIC2 gene encodes two distinct proteins, which are produced by alternative splicing of the CD99 gene transcript and are identified as bands of 30 and 32 kDa (p30/32).Although its function is not fully understood, CD99 is implicated in various cellular processes including homotypic aggregation of T cells, upregulation of T cell receptor and MHS molecules, apoptosis of immature thymocytes and leukocyte diapedesis.CD99 is expressed on the cell membrane of some lymphocytes, cortical thymocytes, and granulosa cells of the ovary. Most pancreatic islet cells, Sertoli cells of the testis, and some endothelial cells express this antigen. Mature granulocytes express very little or no CD99. MIC2 is strongly expressed on Ewing's sarcoma cells and primitive peripheral neuroectodermal tumors. This MAb shows a very similar reactivity to other CD99 MAbs (e.g. O13, 12E7, or HBA-71) and is excellent for immunohistochemical staining of formalin-fixed, paraffin-embedded tissues.

Supplier: Biotium

Recognizes a sialoglycoprotein of 27-32 kDa, identified as CD99, or MIC2 gene product, or E2 antigen. MIC2 gene is located in the pseudo-autosomal region of the human X and Y chromosome. MIC2 gene encodes two distinct proteins, which are produced by alternative splicing of the CD99 gene transcript and are identified as bands of 30 and 32 kDa (p30/32).Although its function is not fully understood, CD99 is implicated in various cellular processes including homotypic aggregation of T cells, upregulation of T cell receptor and MHS molecules, apoptosis of immature thymocytes and leukocyte diapedesis.CD99 is expressed on the cell membrane of some lymphocytes, cortical thymocytes, and granulosa cells of the ovary. Most pancreatic islet cells, Sertoli cells of the testis, and some endothelial cells express this antigen. Mature granulocytes express very little or no CD99. MIC2 is strongly expressed on Ewing's sarcoma cells and primitive peripheral neuroectodermal tumors. This MAb shows a very similar reactivity to other CD99 MAbs (e.g. O13, 12E7, or HBA-71) and is excellent for immunohistochemical staining of formalin-fixed, paraffin-embedded tissues.

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localised because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins

Supplier: Bioss

Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF-dependent neuronal differentiation.Neuronal activity dramatically increases the concentration of cytosolic Ca2+, which then serves as a second messenger to direct diverse cellular responses. Calmodulin is a primary mediator of Ca2+ signals in the nervous system. Ric, a protein related to the Ras subfamily of small GTPases, has the ability to bind calmodulin. In addition, two Ras-like human proteins, Rin and Rit (Ric-related gene expressed in many tissues), which are 71% and 66% identical to RIC respectively, share related G2 domains with Ric. While most members of the Ras subfamily are plasma membrane-associated and generally require a C-terminal isoprenyl group to bind to the plasma membrane, Rit and Rin lack the recognition signal for C-terminal prenylation. Transiently expressed Rit and Rin are plasma membrane-localized because both proteins contain a C-terminal cluster of basic amino acids, which provides a mechanism for membrane association. Rin binds calmodulin through a C-terminal binding motif. Rit and Ric are widely expressed, whereas expression of Rin is restricted to the neuron system. In conclusion, Rit and Rin define a novel subfamily of Ras-related proteins