Votre recherche pour: FAM-xtra+CPG

Numéro de catalogue: (BOSSBS-13025R-CY7)

Fournisseur: Bioss

Description: Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines residing in the dinucleotide CpG motif, and this methylation results in transcriptional repression of the target gene. The Dnmt enzymes are encoded by independent genes. Dnmt1 is the most abundant, and it preferentially methylates hemimethylated DNA and coordinates gene expression during development. Additional mammalian Dnmt proteins include Dnmt2 and Dnmt3. Dnmt2 lacks the large N-terminal regulator domain of Dnmt1, is expressed at substantially lower levels in adult tissues, and is likely involved in methylating newly integrated retroviral DNA. Dnmt3a and Dnmt3b are encoded by two distinct genes, but both are abundantly expressed in embryonic stem cells, where they also methylate CpG motifs on DNA.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5915R-A350)

Fournisseur: Bioss

Description: DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-5915R-A488)

Fournisseur: Bioss

Description: DNA methylation, or the addition of methyl groups to cytosine bases in the dinucleotide CpG, is imperative to proper development and regulates gene expression. The methylation pattern involves the enzymatic processes of methylation and demethylation. The demethylation enzyme was recently found to be a mammalian protein, which exhibits demethylase activity associated to a methyl-CpG-binding domain (MBD). The enzyme is able to revert methylated cytosine bases to cytosines within the particular dinucleotide sequence mdCpdG by catalyzing the cleaving of the methyl group as methanol. MeCP2 and MBD1 (PCM1) are first found to repress transcription by binding specifically to methylated DNA. MBD2 and MBD4 (also known as MED1) were later found to colocalize with foci of heavily methylated satellite DNA and believed to mediate the biological functions of the methylation signal. Surprisingly, MBD3 does not bind methylated DNA both in vivo and in vitro. MBD1, MBD2, MBD3, and MBD4 are found to be expressed in somatic tissues, but the expression of MBD1 and MBD2 is reduced or absent in embryonic stem cells, which are known to be deficient in MeCP1 activity. MBD4 have homology to bacterial base excision repair DNA N-glycosylases/lyases. In some microsatellite unstable tumors MBD4 is mutated at an exonic polynucleotide tract.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9393R-CY3)

Fournisseur: Bioss

Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9393R-CY5)

Fournisseur: Bioss

Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-11703R-A680)

Fournisseur: Bioss

Description: FMR2 is a 1311 amino acid nuclear protein belonging to the AF4 family. Expressed in the brain, placenta and lung, FMR2 exists as two isoforms produced by alternative splicing. Defects in the gene that encodes FMR2 have been found to be a cause of FRAXE, an X-linked form of mental retardation. Individuals expressing the FRAXE site also have more than two-hundred copies of a GCC repeat adjacent to CpG island, compared to six to thirty-five copies of the GCC repeat in a normal individual. It is believed that loss of FMR2 expression causes this GCC expansion of the FRAXE site.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9721R-CY3)

Fournisseur: Bioss

Description: Frequent loss of heterozygosity (LOH) at human chromosome 8p22-p21 is associated with various tumors including prostate and breast cancer. The 8p22-p21 region contains the FEZ1 gene, which is altered in tumors of the esophagus, prostate and breast. The FEZ1 protein (also known as leucine zipper putative tumor suppressor or LZTS1) contains a DNA-binding leucine zipper motif. FEZ1 is expressed in normal breast and prostate, but alterations in FEZ1 expression result in abnormal cell growth. The absence of FEZ1 expression is characteristic of breast and prostate cancer cell lines as well as primary breast and pro-state tumors. This absence of FEZ1 may be due to several factors, including mutations in the FEZ1 gene or hypermethylation of the CpG island flanking the FEZ1 promoter region. FEZ1 acts as a negative regulator of cell growth. During cell-cycle progression, FEZ1 localizes to microtubule components and is hyperphosphorylated by cAMP-dependent kinase.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9721R-A350)

Fournisseur: Bioss

Description: Frequent loss of heterozygosity (LOH) at human chromosome 8p22-p21 is associated with various tumors including prostate and breast cancer. The 8p22-p21 region contains the FEZ1 gene, which is altered in tumors of the esophagus, prostate and breast. The FEZ1 protein (also known as leucine zipper putative tumor suppressor or LZTS1) contains a DNA-binding leucine zipper motif. FEZ1 is expressed in normal breast and prostate, but alterations in FEZ1 expression result in abnormal cell growth. The absence of FEZ1 expression is characteristic of breast and prostate cancer cell lines as well as primary breast and pro-state tumors. This absence of FEZ1 may be due to several factors, including mutations in the FEZ1 gene or hypermethylation of the CpG island flanking the FEZ1 promoter region. FEZ1 acts as a negative regulator of cell growth. During cell-cycle progression, FEZ1 localizes to microtubule components and is hyperphosphorylated by cAMP-dependent kinase.

UOM: 1 * 100 µl

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Numéro de catalogue: (AATB2478)

Fournisseur: AAT BIOQUEST

Description: AzoDye-3 CPG is an excellent building block for preparing FRET oligo molecules.

UOM: 1 * 100 mg

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Numéro de catalogue: (BOSSBS-9393R-FITC)

Fournisseur: Bioss

Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-9393R-A647)

Fournisseur: Bioss

Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-8335R-A555)

Fournisseur: Bioss

Description: Facilitator of innate immune signaling that promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state following expression. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-8335R-A647)

Fournisseur: Bioss

Description: Facilitator of innate immune signaling that promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state following expression. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-0497R-CY5.5)

Fournisseur: Bioss

Description: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity.

UOM: 1 * 100 µl

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Numéro de catalogue: (BOSSBS-0497R-CY5)

Fournisseur: Bioss

Description: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity.

UOM: 1 * 100 µl

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Numéro de catalogue: (AATB2084)

Fournisseur: AAT BIOQUEST

Description: Tide Quencher™ 5.1 (TQ5.1) is a non-fluorescent molecule designed to efficiently quench the fluorescence of common NIR fluorophores such as Cy5, Cy5.5, Alexa Fluor® 647, Alexa Fluor® 647, iFluor® 647 and iFluor® 680.

UOM: 1 * 100 mg

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