Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: ProSci Inc.

This gene is one of several CC cytokine genes clustered on the p-arm of chromosome 9. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. Similar to other chemokines the protein encoded by this gene inhibits hemopoiesis and stimulates chemotaxis. This protein is chemotactic in vitro for thymocytes and activated T cells, but not for B cells, macrophages, or neutrophils. The cytokine encoded by this gene may also play a role in mediating homing of lymphocytes to secondary lymphoid organs. It is a high affinity functional ligand for chemokine receptor 7 (CCR7) that is expressed on T and B lymphocytes and a known receptor for another member of the cytokine family (small inducible cytokine A19). [provided by RefSeq].

Supplier: ProSci Inc.

RBM5 is a component of the spliceosome A complex.It regulates alternative splicing of a number of mRNAs. RBM5 may modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. RBM5 may both positively and negatively regulate aopotosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, RBM5 promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis.

Supplier: ProSci Inc.

Interferon-gamma-inducible 10 kD protein (IP-10), is a CXC chemokine with chemoattractant properties for CD4-positive T cells and inhibits early normal and leukemic hemopoietic progenitor proliferation. IP-10 is produced by a wide variety of cell types ranging from neutrophils and monocytes to hepatocytes, endothelial cells and keratinocytes. The cytokine is reported to be involved in a scala of inflammatory pathologies such as HIV encephalitis, cutaneous T cell lymphoma, chronic hepatitis and acute anterior uveitis. Various observations strongly suggest a role for the CXC chemokines IL-8 and IP-10 in the regulation of angiogenic activity in cancer and in idiopathic pulmonary fibrosis.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: ProSci Inc.

Interferon-gamma-inducible 10 kD protein (IP-10), is a CXC chemokine with chemoattractant properties for CD4-positive T cells and inhibits early normal and leukemic hemopoietic progenitor proliferation. IP-10 is produced by a wide variety of cell types ranging from neutrophils and monocytes to hepatocytes, endothelial cells and keratinocytes. The cytokine is reported to be involved in a scala of inflammatory pathologies such as HIV encephalitis, cutaneous T cell lymphoma, chronic hepatitis and acute anterior uveitis. Various observations strongly suggest a role for the CXC chemokines IL-8 and IP-10 in the regulation of angiogenic activity in cancer and in idiopathic pulmonary fibrosis.

Supplier: ProSci Inc.

SARM Antibody: Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SARM (SAM and ARM-containing protein), along with other molecules such as TIRP, TRIF, TIRAP, and MyD88, is thought to serve as an adaptor protein for the TLRs that allows for the activation of downstream kinases and NF-kappa B, and ultimately the expression of proteins involved in host defense. While SARM has not been conclusively shown to associate directly with TLRs, the presence of a Toll-interluekin-1 (TIR) domain in SARM is consistent with a role as a signaling molecule.

Supplier: ProSci Inc.

Interferon-gamma-inducible 10 kD protein (IP-10), is a CXC chemokine with chemoattractant properties for CD4-positive T cells and inhibits early normal and leukemic hemopoietic progenitor proliferation. IP-10 is produced by a wide variety of cell types ranging from neutrophils and monocytes to hepatocytes, endothelial cells and keratinocytes. The cytokine is reported to be involved in a scala of inflammatory pathologies such as HIV encephalitis, cutaneous T cell lymphoma, chronic hepatitis and acute anterior uveitis. Various observations strongly suggest a role for the CXC chemokines IL-8 and IP-10 in the regulation of angiogenic activity in cancer and in idiopathic pulmonary fibrosis.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome. Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling. Negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3. Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway. Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages. Plays a role in the regulation of the cell cycle progression. Enhances the decapping activity of DCP2. Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules. At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified. The common feature of these proteins is their ability to bind HY RNAs.2.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: Bioss

IQCG is a 443 amino acid protein containing one IQ domain. Widely distributed in nature, the IQ domain forms an amphiphilic seven-turn α-helix capable of binding calmodulin in a Ca2+-independent manner. The level of intracellular calcium is tightly regulated in all eukaryotic cells. A modest increase in this level can result in a myriad of physiological responses, most of which are mediated by calmodulin (CaM), the universal calcium sensor. In acute T-lymphoid/myeloid leukemia, IQCG forms a complex with Nup98, an O-linked glycoprotein and a component of the nuclear pore complex. NUP98-IQCG complex bind co-activators and/or co-repressors, which suggest a role in transcriptional regulation.Nup98-IQCG complex inhibits 32Dcl3 cell apoptosis induced by Arabinofuranosylcytosine (Ara-C) and partially blocks granulocyte differentiation induced by G-CSF. IQCG exists as two isoforms due to alternatively splicing events.

Supplier: ProSci Inc.

CCL8 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The protein is structurally related to the CXC subfamily of cytokines. Members of this subfamily are characterized by two cysteines separated by a single amino acid. This cytokine displays chemotactic activity for monocytes, lymphocytes, basophils and eosinophils. By recruiting leukocytes to sites of inflammation this cytokine may contribute to tumor-associated leukocyte infiltration and to the antiviral state against HIV infection.This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The protein encoded by this gene is structurally related to the CXC subfamily of cytokines. Members of this subfamily are characterized by two cysteines separated by a single amino acid. This cytokine displays chemotactic activity for monocytes, lymphocytes, basophils and eosinophils. By recruiting leukocytes to sites of inflammation this cytokine may contribute to tumor-associated leukocyte infiltration and to the antiviral state against HIV infection. 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.

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FAM19A4 is a secreted, 12 kDa member of the FAM19/TAFA family of chemokine-like proteins. Like other members of the FAM19/TAFA family, with the exception of TAFA5, mature FAM19A4 contains 10 regularly spaced cysteine residues. The FAM19A4 proteins are predominantly expressed in specific regions of the brain and the biological functions of FAM19A4 family members remain to be determined, but there are a few tentative hypotheses. First, FAM19A4 may modulate immune responses in the CNS by functioning as brain specific chemokines, and may act with other chemokines to optimize the recruitment and activity of immune cells in the CNS. Second, FAM19A4 may represent a novel class of neurokines that act as regulators of immune nervous cells. And third, FAM19A4 may control axonal sprouting following brain injury.

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CCL4 Antibody: CCL4, also known as macrophage inflammatory protein 1-beta (MIP1B), belongs to the intercrine beta (chemokine CC) family. Both CCL4 and the related protein CCL3 participate in the host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells. While both CCL4 and CCL3 exert similar effects on monocytes, their effect on lymphocytes differ; with CCL4 selectively attracting CD4+ lymphocytes and CCL3 selectively attracting CD8+ lymphocytes. Additionally, both have been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. The processed form of CCL4 can induce down-modulation of surface expression of the chemokine receptor CCR5, thus inhibiting the CCR5-mediated entry of HIV-1 in T cells.

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Toll-like receptors (TLRs) play an essential role in the detection and elimination of invading microbes. They are type-1 transmembrane receptors, containing extracellular leucine rich repeats and an intracellular Toll/interleukin-1 receptor (TIR) domain. Upon stimulation, these receptors interact with specific TIR domain-containing adaptor proteins. Five such adaptors have been discovered to date, MyD88, Mal (MyD88 adaptor-like)/TIRAP (TIR domain-containing adaptor protein), Trif (TIR-domain-containing adaptor inducing interferon-beta), TRAM (Trif-related adaptor molecule) and SARM (SAM and ARM-containing protein). Different TLRs use different combinations of these adaptors, leading to the activation of common and unique pathways involved in the elimination of the invading microbe.

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CCL16 is a member of CC chemokine family. CCL16 cDNA encodes a 120 amino acid peptide along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. CCL16 is distantly related to other CC chemokines, showing less than 30% sequence identity. CCL16 elicits its effects on cells by interacting with cell surface chemokine receptors such as CCR1, CCR2, CCR5 and CCR8. Recombinant CCL16 has been shown to chemoattract human monocytes and THP1 cells but not resting lymphocytes nor neutrophils. CCL16 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16ninduces a calcium flux in THP1 cells that can be desensitized by prior exposure to RANTES, suggesting that CCL16 and RANTES share the same receptor in THP1 cells.