You Searched For: 7.2+CPG+[TQ7.2+CPG]

Catalog Number: (10748-910)

Supplier: Prosci

Description: OASL (2'-5'-oligoadenylate synthetase-like), also known as p59OASL or TRIP14 (thyroid receptor-interacting protein 14), is a 514 amino acid protein that exists as two alternatively spliced isoforms, designated p56 and p30, and contains two ubiquitin-like domains. It is widely expressed in a variety of tissues and interacts with the ligand binding domain of the thyroid receptor (TR) and is able to bind double-stranded RNA and DNA, possibly playing a role in RNA degradation and the overall inhibition of protein synthesis (2-3). Methyl CpG-binding protein 1 (MBD1), which functions as a transcriptional repressor, was identified as a strong p59 OASL interactor.

Catalog Number: (76107-682)

Supplier: 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 <i>in vivo</i> 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.

Catalog Number: (76107-680)

Supplier: 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 <i>in vivo</i> 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.

Catalog Number: (89415-982)

Supplier: Prosci

Description: TLR9 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. TLR9 forms a subfamily along with TLR7 and TLR8 that recognize viral RNA and CpG DNA sequences and are localized in intracellular acidic compartments such as the phagolysosome. Unlike other TLRs which act through adaptor molecules such as TOLLIP, TIRAP, TRIF, and MyD88 to activate various kinases and transcription factors to respond to potential infection, TLR9 is strictly dependent on MyD88.

Catalog Number: (10482-218)

Supplier: 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.

Catalog Number: (10487-478)

Supplier: 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.

Catalog Number: (10487-470)

Supplier: 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.

Catalog Number: (10748-394)

Supplier: Prosci

Description: IRF8 Antibody: Interferons (IFN)s are involved in a multitude of immune interactions during viral infections and play a major role in both the induction and regulation of innate and adaptive antiviral mechanisms. During infection, host-virus interactions signal downstream molecules such as transcription factors such as IFN regulatory factor-3 (IRF3) which can act to stimulate transcription of IFN-alpha/beta genes. Unlike IRF3, IRF8 appears to act as a negative regulator of IFN-induced genes in most cases, but IRF8 mediates activation of NF-kappa B by the toll-like receptor 9 (TLR9) after stimulation by unmethylated CpG DNA in dendritic cells. Finally, it has been shown that IRF8 decreases bcl-2 expression and thus may play a role in chronic myelogenous leukemia.

Catalog Number: (10103-478)

Supplier: Prosci

Description: CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. TRDMT1 is a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome.CpG methylation is an epigenetic modification that is important for embryonic development, imprinting, and X-chromosome inactivation. Studies in mice have demonstrated that DNA methylation is required for mammalian development. This gene encodes a protein with similarity to DNA methyltransferases, but this protein does not display methyltransferase activity. The protein strongly binds DNA, suggesting that it may mark specific sequences in the genome. Alternative splicing results in multiple transcript variants encoding different isoforms.

Catalog Number: (89358-934)

Supplier: Genetex

Description: 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 Dnmt 1, Dnmt 2 and Dnmt 3. Dnmt 1 is constitutively expressed in proliferating cells and inactivation of this gene causes global demethylation of genomic DNA and embryonic lethality. Dnmt 2 is expressed at low levels in adult tissues and its inactivation does not affect DNA methylation or maintenance of methylation. The Dnmt3 family members, Dnmt 3a and Dnmt 3b, are strongly expressed in ES cells but their expression is down regulated in differentiating ES cells and is low in adult somatic tissue. Dnmt1 co-purifies with the retinoblastoma (Rb) tumour suppressor gene product, E2F 1, and HDAC 1. 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.

Catalog Number: (10487-476)

Supplier: 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.

Catalog Number: (10487-474)

Supplier: 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.

Supplier: Adipogen

Description: In recent years several groups have studied the sequence requirements, specificity, signaling pathways and kinetics of the TLR (Toll-like receptor) 9 suppression by inhibitory oligonucleotide motifs, which led to a class of novel inhibitory oligonucleotide (iODNs), that is independent of the previously thought species preference. Subsequently it has been discovered that telomeric DNA repeats (TTAGGG)n can block immune activation by CpG-ODNs. Short, 11-15 base long oligonucleotides were synthesized that were capable of potently inhibiting CpG-stimulation. The optimal inhibitory DNA motif consists of a pyrimidine-rich triplet, preferably CCT, which is positioned 5- to the GGG sequence in a singlestranded DNA molecule. Additionally, both the optimal spacing between the CCT and GGG motifs, as well as their relative order to each other, is of crucial importance for the inhibitory DNA action. Interestingly, although both TLR7/TLR8 ligands and bacterial DNA share the endosomal compartment for receptor binding and signal transduction, certain iODNs (G-type) suppress only TLR9-mediated activation, whereas prototype class I iODN may also interfere with the activation via the TLR7/TLR8 pathway. Recently, intriguing evidence has been presented that for some iODN classes the immuno-modulatory biological activity shows only limited sequence dependency or may not even involve TLR-mediated uptake and signaling pathways. For example iODNs of the class II are thought to act on immune activation through inhibition of STAT signaling and independent of TLR signaling via binding to a yet to be identified 'ODN-receptor'. Slightly modified phosphodiester versions of the most potent inhibitory ODNs were also able to profoundly block the immune activation of macrophages and just recently prove to be valuable tools for in vivo use in experimental animal models of inflammatory and auto-immune diseases. Based upon these recent insights the following classification for iODNs has been suggested: Class I: G-stretch ODNs: TLR9-specific competitors, some iODNs may also affect TLR7 and TLR8 signalingClass II: ODNs with telomeric repeats: TLR-independent inhibitors of STAT signaling (cellular uptake via an 'ODN receptor'?)Class III: Inhibitors of DNA uptake in a sequence independent mannerClass IV: Long phosphorothioate ODNs as direct competitors of TLR9 signaling in a sequence independent manner

Catalog Number: (102981-404)

Supplier: Adipogen

Description: In recent years several groups have studied the sequence requirements, specificity, signaling pathways and kinetics of the TLR (Toll-like receptor) 9 suppression by inhibitory oligonucleotide motifs, which led to a class of novel inhibitory oligonucleotide (iODNs), that is independent of the previously thought species preference. Subsequently it has been discovered that telomeric DNA repeats (TTAGGG)n can block immune activation by CpG-ODNs. Short, 11-15 base long oligonucleotides were synthesized that were capable of potently inhibiting CpG-stimulation. The optimal inhibitory DNA motif consists of a pyrimidine-rich triplet, preferably CCT, which is positioned 5- to the GGG sequence in a singlestranded DNA molecule. Additionally, both the optimal spacing between the CCT and GGG motifs, as well as their relative order to each other, is of crucial importance for the inhibitory DNA action. Interestingly, although both TLR7/TLR8 ligands and bacterial DNA share the endosomal compartment for receptor binding and signal transduction, certain iODNs (G-type) suppress only TLR9-mediated activation, whereas prototype class I iODN may also interfere with the activation via the TLR7/TLR8 pathway. Recently, intriguing evidence has been presented that for some iODN classes the immuno-modulatory biological activity shows only limited sequence dependency or may not even involve TLR-mediated uptake and signaling pathways. For example iODNs of the class II are thought to act on immune activation through inhibition of STAT signaling and independent of TLR signaling via binding to a yet to be identified 'ODN-receptor'. Slightly modified phosphodiester versions of the most potent inhibitory ODNs were also able to profoundly block the immune activation of macrophages and just recently prove to be valuable tools for in vivo use in experimental animal models of inflammatory and auto-immune diseases. Based upon these recent insights the following classification for iODNs has been suggested: Class I: G-stretch ODNs: TLR9-specific competitors, some iODNs may also affect TLR7 and TLR8 signalingClass II: ODNs with telomeric repeats: TLR-independent inhibitors of STAT signaling (cellular uptake via an 'ODN receptor'?)Class III: Inhibitors of DNA uptake in a sequence independent mannerClass IV: Long phosphorothioate ODNs as direct competitors of TLR9 signaling in a sequence independent manner

Supplier: Adipogen

Description: In recent years several groups have studied the sequence requirements, specificity, signaling pathways and kinetics of the TLR (Toll-like receptor) 9 suppression by inhibitory oligonucleotide motifs, which led to a class of novel inhibitory oligonucleotide (iODNs), that is independent of the previously thought species preference. Subsequently it has been discovered that telomeric DNA repeats (TTAGGG)n can block immune activation by CpG-ODNs. Short, 11-15 base long oligonucleotides were synthesized that were capable of potently inhibiting CpG-stimulation. The optimal inhibitory DNA motif consists of a pyrimidine-rich triplet, preferably CCT, which is positioned 5- to the GGG sequence in a singlestranded DNA molecule. Additionally, both the optimal spacing between the CCT and GGG motifs, as well as their relative order to each other, is of crucial importance for the inhibitory DNA action. Interestingly, although both TLR7/TLR8 ligands and bacterial DNA share the endosomal compartment for receptor binding and signal transduction, certain iODNs (G-type) suppress only TLR9-mediated activation, whereas prototype class I iODN may also interfere with the activation via the TLR7/TLR8 pathway. Recently, intriguing evidence has been presented that for some iODN classes the immuno-modulatory biological activity shows only limited sequence dependency or may not even involve TLR-mediated uptake and signaling pathways. For example iODNs of the class II are thought to act on immune activation through inhibition of STAT signaling and independent of TLR signaling via binding to a yet to be identified 'ODN-receptor'. Slightly modified phosphodiester versions of the most potent inhibitory ODNs were also able to profoundly block the immune activation of macrophages and just recently prove to be valuable tools for in vivo use in experimental animal models of inflammatory and auto-immune diseases. Based upon these recent insights the following classification for iODNs has been suggested: Class I: G-stretch ODNs: TLR9-specific competitors, some iODNs may also affect TLR7 and TLR8 signalingClass II: ODNs with telomeric repeats: TLR-independent inhibitors of STAT signaling (cellular uptake via an 'ODN receptor'?)Class III: Inhibitors of DNA uptake in a sequence independent mannerClass IV: Long phosphorothioate ODNs as direct competitors of TLR9 signaling in a sequence independent manner

Catalog Number: (10496-146)

Supplier: 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.