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4-Carboxy-2-nitrophenylboronsäure
Artikel-Nr:
(BOSSBS-1643R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-1643R-A750
Lokale Artikelnummer::
BOSSBS-1643R-A750
Beschreibung:
Estrogen and progesterone receptor are members of a family of transcription factors that are regulated by the binding of their cognate ligands. The interaction of hormone-bound estrogen receptors with estrogen responsive elements(EREs) alters transcription of ERE-containing genes. The carboxy terminal region of the estrgen receptor contains the ligand binding domain, the amino terminus serves as the transactivation domain, and the DNA binding domain is centrally located. Two forms of estrogen receptor have been identified, ER Alpha and ER Beta. ER Alpha and ER Beta have been shown to be differentially activated by various ligands. The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (hPR-A and hPR-B), which arise from alternative splicing. In most cells, hPR-B functions as a transcriptional activator of progesterone-responsive gene, whereas hPR-A function as a transcriptional inhibitor of all steroid hormone receptors.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11898R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11898R-A647
Lokale Artikelnummer::
BOSSBS-11898R-A647
Beschreibung:
NF-1, also designated CTF, consists of a family of CCAAT box binding proteins that stimulate DNA replication and activate transcription. Analysis of human NF-1 messenger RNA has revealed two forms of the NF-1 protein arising from an alternate splicing of a single NF-1 gene. NF-1 binds its consensus DNA element as a homodimer via an amino-terminal DNA binding domain, and activates transcription through a putatively novel, proline-rich, carboxy terminal transactivation domain. The NF-1 protein has been shown to recognize and bind the adenovirus type 2 promoter and activate transcription of herpes simplex virus thymidine kinase genes. The NF-1 consensus element has been found in the upstream promoter region of myriad eukaryotic genes, including that of Ha-Ras, alpha-globin, HSP 70, GRP 78, Histone H1, myelin basic protein and in the Xenopus laevis vitellogenin gene promoter.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13031R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13031R-CY5
Lokale Artikelnummer::
BOSSBS-13031R-CY5
Beschreibung:
ARID3A, also known as DRIL1 in humans and Bright (for B cell regulator of IgH transcription) in mice, are the mammalian homologs of the Drosophila Dri (dead ringer) protein. ARID3A is developmentally regulated and is expressed in a restricted set of cells, including differentiating cells of the gut and salivary glands. ARID3A represents a member of a unique family of transcriptional activators that shares sequence similarity to proteins of SWI/SNF complexes; it contains an A/T-rich DNA-binding (ARID) domain and a distinct domain involved in tetramerization. The gene encoding ARID3A is linked to a marker of Peutz-Jeghers syndrome, which is an autosomal-dominant disorder characterized by melanocytic macules of the lips, multiple gastrointestinal hamartomatous polyps and an increased risk for various neoplasms, including gastrointestinal cancer. E2FBP1 (E2F-1 binding protein 1) is identical to ARID3A in the carboxy terminal region. E2FBP1 appears to lack DNA binding and transactivation domains, and it functions to regulate the transcription of proteins involved in cell proliferation by binding to the transcription factor E2F-1.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11041R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11041R-CY3
Lokale Artikelnummer::
BOSSBS-11041R-CY3
Beschreibung:
The Bestrophins are a newly described family of anion channels unrelated in primary sequence to any previously characterized channel proteins. Bestrophins were originally defined as a family of over 20 related sequences of the C. elegans. The first mammalian Bestrophin was identified as the vitelliform macular dystrophy (VMD), 1 also known as Best disease. Three more members of the bestrophin family members were cloned and indentified recently, Bestrophin 2, 3 and 4. RT PCR analyses revealed tissue restricted expression of the three genes with both Bestrophin 1 and Bestrophin 2 are abundantly transcribed in colon. Functionally the bestrophines oligomerise to form tetramers and pentamers in order to act as calcium sensitive chloride channels. It has been shown that Bestrophin interacts with beta catalytic subunit of protein phosphatase 2A (PP2Ac). Such protein protein interaction between Bestrophin and PP2Ac and the structural subunit of PP2A, PR65, was confirmed by reciprocal immunoprecipitation. The interaction between PP2Ac and the Bestrophin takes place near the carboxy terminal end of the protein.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5193R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5193R-CY3
Lokale Artikelnummer::
BOSSBS-5193R-CY3
Beschreibung:
AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5193R-CY5.5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5193R-CY5.5
Lokale Artikelnummer::
BOSSBS-5193R-CY5.5
Beschreibung:
AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5193R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5193R-FITC
Lokale Artikelnummer::
BOSSBS-5193R-FITC
Beschreibung:
AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11234R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11234R-CY3
Lokale Artikelnummer::
BOSSBS-11234R-CY3
Beschreibung:
The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13591R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13591R-CY3
Lokale Artikelnummer::
BOSSBS-13591R-CY3
Beschreibung:
Proteins internalized into the endocytic pathway are usually degraded. Efficient proteolysis requires denaturation, induced by acidic conditions within lysosomes, and reduction of inter- and intrachain disulfide bonds. Cytosolic reduction is mediated enzymatically by thioredoxin. In the endocytic pathway, reduction of protein disulfide bonds is important for the generation of MHC class II-peptide complexes. This process is catalyzed by a gamma-interferon-inducible thiol reductase (GILT). GILT is synthesized as a precursor, and following delivery to MHC class II-containing compartments (MIICs), is processed to the mature form via cleavage of amino- and carboxy-terminal propeptides. A lysosomal thiol reductase, GILT, is optimally active at low pH and capable of catalyzing disulfide bond reduction both in vivo and in vitro. GILT is expressed constitutively in antigen-presenting cells and is induced by g-interferon in other cell types, suggesting a potentially important role in antigen processing. Additionally, T cell recognition of select exogenous and endogenous epitopes is dependent on tumor cell expression of GILT. The absence of GILT in melanomas alters antigen processing and the hierarchy of immunodominant epitope presentation.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13046R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13046R-CY3
Lokale Artikelnummer::
BOSSBS-13046R-CY3
Beschreibung:
Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-11234R-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-11234R-A750
Lokale Artikelnummer::
BOSSBS-11234R-A750
Beschreibung:
The Myc family, including c-Myc-, N-Myc- and L-Myc, are nuclear proteins with relatively short half lives that contribute an important role in cellular processes such as proliferation, differentiation, apoptosis and transformation. The c-Myc protein activates transcription as part of a heteromeric complex with a number of interacting partners, including Max and Mxi 1; however the transforming properties of the Myc proto-oncogene are believed to be associated with Myc-mediated transcriptional repression. A POZ domain Zn finger protein, designated Miz-1 for Myc-interacting Zn finger protein-1, is a specific target of Myc-induced gene repression. Miz-1 interacts with Myc, but not Max or other Myc partners, and binding of Myc to Miz-1 requires the helix-loop-helix domain of Myc and a short amphipathic helix located in the carboxy-terminus of Miz-1. Miz-1 associates with DNA elements on the adenovirus major late and cyclin D1 promoters and activates transcription of both promoters. Expression of Miz-1 induces potent growth arrest function, and this latency is reversed by the addition of Myc.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-7594R-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7594R-CY7
Lokale Artikelnummer::
BOSSBS-7594R-CY7
Beschreibung:
Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5182R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5182R-A680
Lokale Artikelnummer::
BOSSBS-5182R-A680
Beschreibung:
AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-5193R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-5193R-A680
Lokale Artikelnummer::
BOSSBS-5193R-A680
Beschreibung:
AKT, also known as protein kinase B (PKB), is a 57 kDa serine/threonine protein kinase. There are three mammalian isoforms of Akt: AKT1 (PKB alpha), AKT2 (PKB beta) and AKT3 (PKB gamma) with AKT2 and AKT3 being approximately 82% identical with the AKT1 isoform. Each isoform has a pleckstrin homology (PH)domain, a kinase domain and a carboxy terminal regulatory domain. AKT was originally cloned from the retrovirus AKT8, and is a key regulator of many signal transduction pathways. Its tight control over cell proliferation and cell viability are manifold; overexpression or inappropriate activation of AKT has been seen in many types of cancer. AKT mediates many of the downstream events of phosphatidylinositol 3 kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI3 kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13046R-A647)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13046R-A647
Lokale Artikelnummer::
BOSSBS-13046R-A647
Beschreibung:
Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-13046R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13046R-HRP
Lokale Artikelnummer::
BOSSBS-13046R-HRP
Beschreibung:
Excitatory Amino Acid Transporters (EAATs) are membrane-bound proteins that are localized in glial cells and pre-synaptic glutamatergic nerve endings. EAATs transport the excitatory neurotransmitters L-glutamate and D-aspartate, a process that is essential for terminating the postsynaptic action of glutamate. The re-uptake of amino acid neurotransmitters by EAAT proteins has been shown to protect neurons from excitotoxicity, which is caused by the accumulation of amino acid neurotransmitters. EAAT4 is an aspartate/glutamate transporter that is expressed predominantly in the cerebellum. The transport activity encoded by EAAT4 has high apparent affinity for L-aspartate and L-glutamate, and has a pharmacologic profile consistent with previously described cerebellar transport activities. EAAT5 is a glutamate transporter coupled to a chloride conductance which is expressed primarily in retina. Although EAAT5 shares the structural homologies of the EAAT family, a novel feature of the EAAT5 sequence is a carboxy-terminal motif previously identified in N-ethyl-D-aspartate receptors and potassium channels and shown to confer interactions with a family of synaptic proteins that promote ion channel clustering.
VE:
1 * 100 µl
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 noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
Lager für diesen Artikel ist begrenzt, kann aber in einem Lagerhaus in Ihrer Nähe zur Verfügung. Bitte stellen Sie sicher, dass Sie in sind angemeldet auf dieser Seite, so dass verfügbare Bestand angezeigt werden können. Wenn das
noch angezeigt wird und Sie Hilfe benötigen, rufen Sie uns an 1-800-932 - 5000.
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