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5-Carboxy-2-fluorphenylborons\u00E4ure
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5-Carboxy-2-fluorphenylborons\u00E4ure
Artikel-Nr:
(BOSSBS-12536R-HRP)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12536R-HRP
Lokale Artikelnummer::
BOSSBS-12536R-HRP
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-7594R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7594R-A680
Lokale Artikelnummer::
BOSSBS-7594R-A680
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 specialised 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.
VE:
1 * 100 µl
Artikel-Nr:
(PRSI7327P)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
7327P
Lokale Artikelnummer::
PRSI7327P
Beschreibung:
16 amino acids near the carboxy terminus of human GBP5.
VE:
1 * 50 µG
Artikel-Nr:
(PRSI7393P)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
7393P
Lokale Artikelnummer::
PRSI7393P
Beschreibung:
18 amino acids near the carboxy terminus of human LPIN.
VE:
1 * 50 µG
Artikel-Nr:
(PRSI7381P)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
7381P
Lokale Artikelnummer::
PRSI7381P
Beschreibung:
15 amino acids near the carboxy-terminus of human N-RAS.
VE:
1 * 50 µG
Lieferant:
Spectrum Chemical
Beschreibung:
Carbomer 940, NF is a polyvinyl carboxy polymer.
Artikel-Nr:
(ABNOMAB14425)
Lieferant:
Abnova
Hersteller-Artikelnummer::
MAB14425
Lokale Artikelnummer::
ABNOMAB14425
Beschreibung:
Mouse monoclonal antibody raised against human testosterone.
VE:
1 * 100 µG
Artikel-Nr:
(PRSI7333P)
Lieferant:
ProSci Inc.
Hersteller-Artikelnummer::
7333P
Lokale Artikelnummer::
PRSI7333P
Beschreibung:
19 amino acid peptide near the carboxy terminus of human APO-E.
VE:
1 * 50 µG
Artikel-Nr:
(BOSSBS-13046R-A555)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13046R-A555
Lokale Artikelnummer::
BOSSBS-13046R-A555
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-A750)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13046R-A750
Lokale Artikelnummer::
BOSSBS-13046R-A750
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-13591R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13591R-CY5
Lokale Artikelnummer::
BOSSBS-13591R-CY5
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-13591R-A680)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-13591R-A680
Lokale Artikelnummer::
BOSSBS-13591R-A680
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-7594R-FITC)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-7594R-FITC
Lokale Artikelnummer::
BOSSBS-7594R-FITC
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-12537R-CY5)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12537R-CY5
Lokale Artikelnummer::
BOSSBS-12537R-CY5
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12536R-CY7)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12536R-CY7
Lokale Artikelnummer::
BOSSBS-12536R-CY7
Beschreibung:
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.
VE:
1 * 100 µl
Artikel-Nr:
(BOSSBS-12539R-CY3)
Lieferant:
Bioss
Hersteller-Artikelnummer::
BS-12539R-CY3
Lokale Artikelnummer::
BOSSBS-12539R-CY3
Beschreibung:
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.
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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