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(Pentamethylcyclopentadienyl)iridium(III)+dichloride+dimer
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(Pentamethylcyclopentadienyl)iridium(III)+dichloride+dimer
Supplier:
Strem Chemicals Inc
Description:
Potassium hexacyanoferrate(III) 99 ACS
Supplier:
THERMO FISHER SCIENTIFIC CHEMICALS
Description:
Rhodium(III) chloride Rh 48.6-49.2%, anhydrous
Supplier:
THERMO FISHER SCIENTIFIC CHEMICALS
Description:
Antimony (III) sulfide 98%
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:
(10412-916)
Supplier:
Bioss
Description:
E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. 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, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.
Catalog Number:
(77440-400)
Supplier:
Bioss
Description:
The human protooncogene JUN is the putative transforming gene of avian sarcoma virus 17, and it encodes a protein which is highly homologous to the viral protein. cJun (previously known as the Fos binding protein p39) and c Fos form a complex in the nucleus. AP 1 (activating protein 1) is a collective term referring to these dimeric transcription factors composed of Jun, Fos or ATF subunits that bind to a common DNA site, the AP1 binding site. AP 1 proteins, mostly the Jun group, regulate the expression and function of cell cycle regulators such as Cyclin D1, p53, p21 (cip1/waf1), p19 (ARF) and p16. Fos and Jun proto oncogene expression is induced transiently by a variety of extracellular stimuli associated with mitogenesis, differentiation processes or depolarization of neurons. JUN has been mapped to 1p32 to p31, a chromosomal region involved in both translocations and deletions in human malignancies.
Catalog Number:
(77439-878)
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, E2F2 and E2F3, have an additional cyclin binding domain. This protein binds preferentially to retinoblastoma protein pRB in a cell-cycle dependent manner. It can mediate both cell proliferation and p53-dependent/independent apoptosis. [provided by RefSeq, Jul 2008]
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:
(75791-638)
Supplier:
Prosci
Description:
The tetrameric receptor complex for IFN gamma consists of two subunits, IFNGR1 (IFN gamma R alpha) and IFNGR2 (IFN gamma R beta ), through which the dimeric IFN- gamma exerts its biological functions, including antiviral, antiproliferation and immune-modulatory activity in mammals. Both IFNGR1 and IFNGR2 are single transmembrane proteins belonging to the class II cytokine family. FNGR1, widely expressed in most host cells, is essential for IFN gamma binding, receptor trafficking, and signal transduction. IFNGR1 possesses an intracellular Janus tyrosine kinase (JAK) 1 binding site, a signal transducer and activator of transcription 1 (STAT1) binding site. The resulting STAT1 homodimers translocate from the cytoplasm to the nucleus and bind to the interferon-gamma activated sequence (GAS) promoter to induce expression of downstream interferon stimulated genes (ISGs).
Catalog Number:
(10410-608)
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:
(10413-436)
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:
(76080-180)
Supplier:
Bioss
Description:
E2F's are DNA binding proteins, which associate with negative regulators, such as the retinoblastoma p107 protein, resulting in an altered rate of gene transcription. 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, E2F2 and E2F3, have an additional cyclin binding domain. E2F1 is proposed to be involved in several cellular processes that range from tumor suppressor, cell progression and oncogenesis. E2F1 overexpression can also drive cells into apoptosis.
Catalog Number:
(10413-416)
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:
(10413-422)
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:
(10413-412)
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:
(10749-640)
Supplier:
Prosci
Description:
UBC13 Antibody: Ubiquitin-conjugating enzyme 13 (Ubc13) was initially discovered in S. cerevisiae as a DNA-damage inducible protein involved in the error-free DNA postreplication repair pathway. It has recently been shown to be an important component of the Toll-like receptor and IL-1R signaling pathway. Signals from these pathways are relayed by a number of downstream molecules such as MyD88 and tumor necrosis factor receptor associated factor (TRAF6), ultimately activating various kinases and transcription factors. Ubc13 is part of a dimeric ubiquitin-conjugating enzyme complex also containing UEV1A (ubiquitin-conjugating enzyme E2 variant 1) that together with TRAF6 activates TAK1, a member of the mitogen-activated protein kinase kinase kinase family. The Ubc13-UEV1A complex also mediates the Lys-63 ubiquitination of TRAF-6, and this ubiquitination is essential for TAK1 activation.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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