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Description: MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.

Catalog Number: 10388-480

Supplier: Bioss

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Description: Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling.

Catalog Number: 10342-634

Supplier: Bioss

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Description: Goat Polyclonal antibody to MAD4 / MXD4 (MAX dimerization protein 4) Purity: Antigen affinity chromatography. Species Reactivity: Human Tested Applications: ELISA WB Pkg Size: 100 ug

Catalog Number: 89287-952

Supplier: Genetex

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Description: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization.

Catalog Number: 77438-742

Supplier: Bioss

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Description: BATF is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of this protein mediates dimerization with members of the Jun family of proteins. This protein is thought to be a negative regulator of AP-1/ATF transcriptional events. The protein encoded by this gene is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of this protein mediates dimerization with members of the Jun family of proteins. This protein is thought to be a negative regulator of AP-1/ATF transcriptional events.

Catalog Number: 10101-490

Supplier: Prosci

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Description: PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs; PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-B. PDGFR-a is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-B interacts with only PDGF-BB and PDGF-AB. Recombinant human PDGF-AB is a 25.5 kDa disulfide-linked dimer, consisting of one A chain and one B chains (234 total amino acids).

Catalog Number: 10072-564

Supplier: Prosci

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Description: The epidermal growth factor (EGF) family of receptor tyrosine kinases consists of four receptors, EGFR (ErbB1), ErbB2 (neu), ErbB3, and ErbB4. Members of the EGFR family contain 3 domains: an extracellular domain that is involved in ligand binding and receptor dimerization, a single transmembrane domain and a cytoplasmic domain. EGF exerts its actions by binding to the EGFR, a 170 kDa protein. Activation of EGFR initiates diverse cellular pathwaysIn response to toxic environmental stimuli, or to EGF binding to the receptor, the EGFR forms homo- or heterodimers with other family members. Each dimeric receptor complex initiates a distinct signaling pathway by recruiting different Src homology 2 (SH2) containing effector proteins.

Catalog Number: 89359-422

Supplier: Genetex

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Description: NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity.Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.

Catalog Number: 102980-376

Supplier: Adipogen

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Description: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity.

Catalog Number: 77438-832

Supplier: Bioss

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Description: Designed for use in library prep for DNA, ChIP DNA and RNA (but not Small RNA), the NEBNext Adaptors enable high-efficiency adaptor ligation and high library yields, with minimized adaptor-dimer formation.

Catalog Number: CA76540-502

Supplier: New England Biolabs (NEB)

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Description: MRPL12 is a component of the 39S subunit of mammalian mitochondrial ribosomes. This protein forms homodimers whereas in prokaryotic ribosomes two L7/L12 dimers and one L10 protein form the L8 protein complex.

Catalog Number: 10388-464

Supplier: Bioss

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Description: ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Catalog Number: 10410-060

Supplier: Bioss

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Description: ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Catalog Number: 10410-080

Supplier: Bioss

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Description: ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Catalog Number: 10410-058

Supplier: Bioss

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Description: MA1-250 detects CHOP protein in human and mouse samples. MA1-250 has successfully been used in Western blot, immunoprecipitation, immunocytochemistry, and immunofluorescence procedures. By Western blot, this antibody detects an ~31 kDa protein representing CHOP from primary human fibroblast extract. The MA1-250 immunizing protein corresponds to a bacterially expressed, mouse CHOP fusion protein. Clone 9C8 has been shown to recognize an epitope in the N-terminal region of CHOP. This antibody was orginally validated as part of a Thermo Scientific Cellomics High Content Screening Kit. The antibody sold separately may have slightly different performance and may need to be further optimized for the best results. CHOP (also known as GADD153, Growth Arrest and DNA Damage Inducible Protein 153, and C/EBP Homology Protein) is a small nuclear protein that is capable of dimerizing with transcription factors C/EBP alpha and beta. Once dimerized, this complex inhibits the normal binding and function of C/EBP to classical binding sites. Inversely, the C/EBP-CHOP dimer gains binding activity to other non-classical C/EBP stress related targets. Under normal cellular conditions this protein is not expressed in detectable levels, but is highly upregulated during times of cellular/ER stress. Examples of CHOP inducing stress include: treatment with tunicamycin, nutrient starvation and reducing agents that interfere with the calcium flux across the ER membrane.

Catalog Number: CAPIMA1250

Supplier: Thermo Scientific

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Description: ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Catalog Number: 10410-074

Supplier: Bioss

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