11021 Results for: "Zinc"

Supplier: Bioss

Pokemon, the POK erythroid myeloid ontogenic factor, not only regulates the expression of many genes, but also plays an important role in cell tumorigenesis. To investigate the molecular mechanism regulating expression of the Pokemon gene in humans, its 5'-upstream region was cloned and analyzed. Transient analysis revealed that the Pokemon promoter is constitutive. Deletion analysis and a DNA decoy assay indicated that the NEG-U and NEG-D elements were involved in negative regulation of the Pokemon promoter, whereas the POS-D element was mainly responsible for its strong activity. Electrophoretic mobility shift assays suggested that the NEG-U, NEG-D and POS-D elements were specifically bound by the nuclear extract from A549 cells in vitro. Mutation analysis demonstrated that cooperation of the NEG-U and NEG-D elements led to negative regulation of the Pokemon promoter. Moreover, the NEG-U and NEG-D elements needed to be an appropriate distance apart in the Pokemon promoter in order to cooperate. Taken together, our results elucidate the mechanism underlying the regulation of Pokemon gene transcription, and also define a novel regulatory sequence that may be used to decrease expression of the Pokemon gene in cancer gene therapy.

Supplier: Bioss

Pokemon, the POK erythroid myeloid ontogenic factor, not only regulates the expression of many genes, but also plays an important role in cell tumorigenesis. To investigate the molecular mechanism regulating expression of the Pokemon gene in humans, its 5'-upstream region was cloned and analyzed. Transient analysis revealed that the Pokemon promoter is constitutive. Deletion analysis and a DNA decoy assay indicated that the NEG-U and NEG-D elements were involved in negative regulation of the Pokemon promoter, whereas the POS-D element was mainly responsible for its strong activity. Electrophoretic mobility shift assays suggested that the NEG-U, NEG-D and POS-D elements were specifically bound by the nuclear extract from A549 cells in vitro. Mutation analysis demonstrated that cooperation of the NEG-U and NEG-D elements led to negative regulation of the Pokemon promoter. Moreover, the NEG-U and NEG-D elements needed to be an appropriate distance apart in the Pokemon promoter in order to cooperate. Taken together, our results elucidate the mechanism underlying the regulation of Pokemon gene transcription, and also define a novel regulatory sequence that may be used to decrease expression of the Pokemon gene in cancer gene therapy.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Bioss

Immunoglobulins belong to a group of related glyco proteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin's lymphomas. Kappa light chain contains one immunoglobulin like domain. The EU sequence has the INV allotypic marker, Ala 45 and Val 83. The ROY sequence has the INV allotypic marker, Ala 45 and Leu 83.

Supplier: Prosci

Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms. Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.

Supplier: Prosci

Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms. Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.