You Searched For: Cyclopentadienylmolybdenum+tricarbonyl+dimer

Catalog Number: (76110-114)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

Supplier: Biotium

Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Catalog Number: (10668-280)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

Catalog Number: (10072-596)

Supplier: Prosci

Description: Neurturin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, Artemin, and Persephin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Neurturin signals through a multicomponent receptor system, composed of RET and one of four GFR alpha (alpha1-alpha4) receptors. Neurturin promotes the development and survival of sympathetic and sensory neurons by signaling through a receptor system composed of RET and GFRalpha2. The functional form of human Neurturin is a disulfide-linked homodimer, of two 11.8 kDa polypeptide monomers (206 total amino acid residues). Each monomer contains seven conserved cysteine residues, one of which (Cys 69) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.

Catalog Number: (10668-286)

Supplier: Bioss

Description: The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM7 (tripartite motif-containing 7), also known as RNF90 or GNIP, is a 511 amino acid protein that belongs to the TRIM family and contains one RING-type zinc finger, one B box-type zinc finger and one SPRY domain. Expressed in placenta and skeletal muscle and present at lower levels in brain, heart and pancreas, TRIM7 localizes to both the cytoplasm and the nucleus where it exists as dimers and is thought to participate in the initiation of glycogen synthesis. Multiple isoforms of TRIM7 exist due to alternative splicing events.

Catalog Number: (77439-390)

Supplier: Bioss

Description: The protein encoded by this gene is a member of the E2F family of transcription factors. The E2F family plays a crucial role in the control of cell cycle and action of tumor suppressor proteins and is also a target of the transforming proteins of small DNA tumor viruses. The E2F proteins contain several evolutionally conserved domains found in most members of the family. These domains include a DNA binding domain, a dimerization domain which determines interaction with the differentiation regulated transcription factor proteins (DP), a transactivation domain enriched in acidic amino acids, and a tumor suppressor protein association domain which is embedded within the transactivation domain. This protein and another 2 members, E2F1 and E2F2, have an additional cyclin binding domain. This protein binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner. [provided by RefSeq].

Catalog Number: (10458-616)

Supplier: Bioss

Description: Estrogen receptors (ER) are members of the steroid/thyroid hormone receptor superfamily of ligand-activated transcription factors. Estrogen receptors, including ER alpha and ER beta, contain DNA binding and ligand binding domains and are critically involved in regulating the normal function of reproductive tissues. ER alpha and ER beta A have been shown to be differentially activated by various ligands. Receptor-ligand interactions trigger a cascade of events, including dissociation from heat shock proteins, receptor dimerization, phosphorylation and the association of the hormone activated receptor with specific regulatory elements in target genes. Evidence suggests that ER alpha and ER beta may be regulated by distinct mechanisms even though they share many functional characteristics.

Catalog Number: (10463-352)

Supplier: Bioss

Description: B-ATF is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of B-ATF mediates dimerization with members of the Jun family of proteins. The B-ATF protein does not homodimerize efficiently, but rather forms a heterodimer preferentially with c-Jun. The B-ATF/c-Jun protein complex can interact with DNA containing a consensus binding site for AP-1, suggesting that B-ATF functions as a tissue-specific modulator of the AP-1 transcription complex in human cells. B-ATF also associates with IFP35, a leucine zipper protein that translocates to the nucleus following IFN treatment. The gene encoding B-ATF, also designated SFA-2, is strongly expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I.

Catalog Number: (MSPP-781711006)

Supplier: STEMCELL Technologies

Description: Epidermal growth factor receptor (EGFR) is a type I transmembrane protein and receptor tyrosine kinase. EGFR has been shown to bind to some members of the EGF family ligands including EGF, amphiregulin, TGF-α, betacellulin, epiregulin, heparin-binding EGF, and neuregulin-2α. EGFR ligand binding induces homodimerization, as well as heterodimerization of EGFR with ErbB2 or with ligand-activated ErbB3 or ErbB4 (Schlessinger). Dimerization results in kinase activation, phosphorylation, and cell signaling, mediated primarily through MEK/ERF and AKT pathways (Navlonic <i>et al.</i>). EGFR signaling has been shown to regulate cell proliferation, differentiation, motility, and apoptosis. Elevated levels of EGFR have been correlated with carcinogenesis (Maihle <i>et al.</i>). Protein contains a His-residue tag at the carboxyl end of the polypeptide chain.

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Catalog Number: (10463-336)

Supplier: Bioss

Description: B-ATF is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of B-ATF mediates dimerization with members of the Jun family of proteins. The B-ATF protein does not homodimerize efficiently, but rather forms a heterodimer preferentially with c-Jun. The B-ATF/c-Jun protein complex can interact with DNA containing a consensus binding site for AP-1, suggesting that B-ATF functions as a tissue-specific modulator of the AP-1 transcription complex in human cells. B-ATF also associates with IFP35, a leucine zipper protein that translocates to the nucleus following IFN treatment. The gene encoding B-ATF, also designated SFA-2, is strongly expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I.

Catalog Number: (10463-356)

Supplier: Bioss

Description: B-ATF is a nuclear basic leucine zipper protein that belongs to the AP-1/ATF superfamily of transcription factors. The leucine zipper of B-ATF mediates dimerization with members of the Jun family of proteins. The B-ATF protein does not homodimerize efficiently, but rather forms a heterodimer preferentially with c-Jun. The B-ATF/c-Jun protein complex can interact with DNA containing a consensus binding site for AP-1, suggesting that B-ATF functions as a tissue-specific modulator of the AP-1 transcription complex in human cells. B-ATF also associates with IFP35, a leucine zipper protein that translocates to the nucleus following IFN treatment. The gene encoding B-ATF, also designated SFA-2, is strongly expressed in mature T and B lymphocytes, and is up-regulated after transformation by human T-cell leukemia virus type I.

Supplier: Biotium

Description: This MAb recognizes TGF beta 1, 2 and 3. Three TGF betas have been identified in mammals. TGF beta 1, TGF beta 2 and TGF beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecules. Biologically active TGF beta requires dimerization of the monomers (usually homodimers) and release of the latent peptide portion. Overall, the mature region of the TGF beta 3 protein has approximately 80% identity to the mature region of both TGF beta 1 and TGF beta 2. However, the NH2 terminals or precursor regions of their molecules share only 27% sequence identity. TGF betas inhibit the growth of epithelial cells and stimulate the growth of mesenchymal cells.

Catalog Number: (75790-606)

Supplier: Prosci

Description: Superoxide Dismutase [Cu-Zn] (SOD1) is a soluble cytoplasmic and mitochondrial intermembrane space protein that belongs to the Cu-Zn superoxide dismutase family. SOD1 binds copper and zinc ions and is one of three isozymes responsible for destroying free superoxide radicals in the body. SOD1 neutralizes supercharged oxygen molecules, which can damage cells if their levels are not controlled. The enzyme protects the cell against dangerous levels of superoxide. Zinc binding promotes dimerization and stabilizes the native form. Mutations in SOD1 cause a form of familial amyotrophic lateral sclerosis. Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) which is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis.

Catalog Number: (10083-746)

Supplier: Proteintech

Description: RNF17 also termed as ring finger protein 17 is a 1623 amino acid protein, which contains 1 ring type zinc finger and 4 tudor domains. RNF17 is specifically expressed in testis. The RING finger motif presents in many ubiquitin E3 ligases. RNF17 interacts with all four members of the Mad family (Mad1, Mxi1, Mad3 and Mad4), which are basic-helix-loop-helix-leucine zipper transcription factors of the Myc oncoprotein network. RNF17 is component of the tectonic-like complex, which is required for ciliogenesis and sonic hedgehog/SHH signaling. RNF17 is able to form dimers or polymers both in vitro and in vivo, indicating that it may play a role in the assembly of RNF17 granules. RNF17 encodes a novel key regulator of spermiogenesis.

Supplier: Tonbo Biosciences

Description: The ACK2 antibody is specific for CD117, also called c-Kit, a 145 kDa cytokine receptor important in the development of hematopoietic stem cells, in oogenesis, and for functional activity of immune cells such as NK and mast cells. c-Kit binds to a ligand known as stem cell factor (SCF), or alternatively as mast cell growth factor. Ligand binding promotes the activation (dimerization) and subsequent tyrosine kinase activity of the c-Kit receptor and triggers key survival, expansion and maturation signals during hematopoietic progenitor cell development. Conversely, shedding of extracellular domain of c-Kit receptor is reported to induce inactivation or apoptosis within these cells. The survival signaling activity of c-Kit confers a proto-oncogenic attribute to the receptor, as overexpression or mutations in this protein are associated with tumor development.

Catalog Number: (10098-330)

Supplier: Prosci

Description: Interleukin 31 (IL-31) is a recently discovered T-cell cytokine closely related to IL-6 type cytokines and is preferentially produced by T helper type 2 cells. IL-31 activity is mediated through the ligand-induced oligomerization of a dimeric receptor complex containing IL-31 receptor A and oncostatin M receptor. In response to IL-31 binding, these proteins activate the JAK/STAT and the AKT signaling pathways. RNA levels of IL-31 receptor A and oncostatin M receptor are induced in activated monocytes but are expressed constitutively in epithelial cells. IL-31, when overexpressed in transgenic mice, results in the development of pruritis, alopecia and skin lesions, and in humans may result in atopic dermatitis, suggesting that IL-31 may represent a novel target for antipruritic drug development.