You Searched For: Cyclopentadienylmolybdenum+tricarbonyl+dimer

Catalog Number: (10410-606)

Supplier: Bioss

Description: The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

Catalog Number: (10413-428)

Supplier: Bioss

Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

Catalog Number: (10751-846)

Supplier: Prosci

Description: Alpha-tubulin Antibody: Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter. Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase. Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle. Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.

Catalog Number: (10334-298)

Supplier: Bioss

Description: The kinesin motor proteins include at least two forms of conventional kinesin encoded by different genes and designated as ubiquitous kinesin, which is expressed in all cells and tissues, or neuronal kinesin, which is expressed exclusively in neural cells. Kinesin is a microtubule associated protein comprised of three different structural domains. A considerable globular N-terminal domain regulates the hydrolysis of ATP and also microtubule binding while central coiled-coil domains promote heavy chain dimerization. Lastly, small globular C-terminal domains interact with kinesin light chains, membranous organelles and vesicles. Expression of ubiquitous kinesin heavy chain, also designated UKHC, is found subcellularly in areas of heavy vesicular trafficking such as the microtubule pathways of neural cells and also the Golgi of non-neural cell types.

Catalog Number: (10410-614)

Supplier: Bioss

Description: The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

Catalog Number: (10410-604)

Supplier: Bioss

Description: The androgen receptor gene is more than 90 kb long and codes for a protein that has 3 major functional domains: the N-terminal domain, DNA-binding domain, and androgen-binding domain. The protein functions as a steroid-hormone activated transcription factor. Upon binding the hormone ligand, the receptor dissociates from accessory proteins, translocates into the nucleus, dimerizes, and then stimulates transcription of androgen responsive genes. This gene contains 2 polymorphic trinucleotide repeat segments that encode polyglutamine and polyglycine tracts in the N-terminal transactivation domain of its protein. Expansion of the polyglutamine tract causes spinal bulbar muscular atrophy (Kennedy disease). Mutations in this gene are also associated with complete androgen insensitivity (CAIS). Two alternatively spliced variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008]

Catalog Number: (10334-296)

Supplier: Bioss

Description: The kinesin motor proteins include at least two forms of conventional kinesin encoded by different genes and designated as ubiquitous kinesin, which is expressed in all cells and tissues, or neuronal kinesin, which is expressed exclusively in neural cells. Kinesin is a microtubule associated protein comprised of three different structural domains. A considerable globular N-terminal domain regulates the hydrolysis of ATP and also microtubule binding while central coiled-coil domains promote heavy chain dimerization. Lastly, small globular C-terminal domains interact with kinesin light chains, membranous organelles and vesicles. Expression of ubiquitous kinesin heavy chain, also designated UKHC, is found subcellularly in areas of heavy vesicular trafficking such as the microtubule pathways of neural cells and also the Golgi of non-neural cell types.

Catalog Number: (10230-028)

Supplier: Bioss

Description: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Catalog Number: (10106-984)

Supplier: Prosci

Description: E2F3 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. E2F3 binds specifically to retinoblastoma protein pRB in a cell-cycle dependent manner.

Catalog Number: (10062-028)

Supplier: Prosci

Description: Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter (reviewed in 1). Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase (2). Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle (3). Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.

Catalog Number: (77436-650)

Supplier: Bioss

Description: Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

Catalog Number: (76234-896)

Supplier: Rockland Immunochemical

Description: Rockland produces a wide range of human GST antibodies in our laboratories. Select appropriate GST antibodies for your research by isotype, epitope, applications and species reactivity. There are 22 members of the human GST family of proteins. GST is responsible for the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. The amino acid sequence GST is highly conserved in most organisms including mammals. GSTs proteins are typically homodimeric, with both heterologous GST dimers have been observed. GST monomers have an average molecular weight of approximately 25-28 kDa in size. Note a different form of non-human GST (Glutathione-S-Transferase) is used as a protein expression tag commonly in molecular biology applications. All anti-GST antibodies my not react with recombinant GST-fusion proteins.

Catalog Number: (10111-368)

Supplier: Prosci

Description: E2F5 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 is differentially phosphorylated and is expressed in a wide variety of human tissues. It is more homologous to E2F4, a family member, than to other members. Both this protein and E2F4 interact with tumor suppressor proteins p130 and p107, but not with pRB.

Catalog Number: (76081-806)

Supplier: Bioss

Description: JAK2 (Janus Activating Kinase 2) is a tyrosine kinase of the non-receptor type, that associates with the intracellular domains of cytokine receptors; JAK2 is the predominant JAK kinase activated in response to several growth factors and cytokines such as IL-3, GM-CSF and erythropoietin; it has been found to be constitutively associated with the prolactin receptor and is required for responses to gamma interferon. Ligand binding to a variety of cell surface receptors (e.g., cytokine, growth factor, GPCRs) leads to an association of those receptors with JAK proteins, which are then activated via phosphorylation on tyrosines 1007 and 1008 in the kinase activation loop. Activated JAK proteins phosphorylate and activate STAT (signal transducers and activators of transcription) proteins, which then dimerize and translocate to the nucleus. Once in the nucleus, STAT proteins bind to DNA and modify the transcription of various genes.

Catalog Number: (76081-804)

Supplier: Bioss

Description: JAK2 (Janus Activating Kinase 2) is a tyrosine kinase of the non-receptor type, that associates with the intracellular domains of cytokine receptors; JAK2 is the predominant JAK kinase activated in response to several growth factors and cytokines such as IL-3, GM-CSF and erythropoietin; it has been found to be constitutively associated with the prolactin receptor and is required for responses to gamma interferon. Ligand binding to a variety of cell surface receptors (e.g., cytokine, growth factor, GPCRs) leads to an association of those receptors with JAK proteins, which are then activated via phosphorylation on tyrosines 1007 and 1008 in the kinase activation loop. Activated JAK proteins phosphorylate and activate STAT (signal transducers and activators of transcription) proteins, which then dimerize and translocate to the nucleus. Once in the nucleus, STAT proteins bind to DNA and modify the transcription of various genes.

Catalog Number: (76100-036)

Supplier: Bioss

Description: Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilize XPC. May protect XPC from proteasomal degradation. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.