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Masterflex+Single-use+Flow+Sensor
Numéro de catalogue:
(BOSSBS-11332R-A555)
Fournisseur:
Bioss
Description:
Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11332R-FITC)
Fournisseur:
Bioss
Description:
Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11332R-A647)
Fournisseur:
Bioss
Description:
Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6634R-A647)
Fournisseur:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. 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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6634R-CY5)
Fournisseur:
Bioss
Description:
Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. 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.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1370R-CY3)
Fournisseur:
Bioss
Description:
Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. recognises the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1370R-CY7)
Fournisseur:
Bioss
Description:
Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. recognises the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1370R-A647)
Fournisseur:
Bioss
Description:
Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor. recognises the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism. Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN), TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Binds DNA ends. Plays a role in replication-dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation. Phosphorylates ATF2 which stimulates its function in DNA damage response.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11332R-HRP)
Fournisseur:
Bioss
Description:
Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
UOM:
1 * 100 µl
Fournisseur:
WTW
Description:
Ce multimètre portable et compact permet de mesurer le pH, la conductivité et l'oxygène dissous avec des capteurs numériques intelligents (IDS). Il dispose d'un canal de mesure universel pour tous les paramètres. Grâce à sa conception robuste et étanche, il est idéal pour des mesures sur le terrain et en laboratoire.
Fournisseur:
MIELE
Description:
The PLW 6111 SlimLine laboratory washer offer a comprehensive and systematic solution to the reprocessing of laboratory glassware for analytical experiments.
Numéro de catalogue:
(BOSSBS-7689R-CY5)
Fournisseur:
Bioss
Description:
Potassium channels are a group of ubiquitously expressed proteins that serve numerous functions in excitable and non-excitable cells. One class of integral membrane potassium channels is the large conductance, calcium-activated potassium channel (Maxi K+). Maxi K+ differs from most other potassium channels in that its activation is controlled by both increases in intracellular calcium and by membrane depolarization. Maxi K+ dual activation is possible because of its structure. The core of the channel, which is similar to other potassium channels, is a Maxi K+ alpha homotetramer that contains both a voltage sensor and an intracellular calcium binding domain. In vascular smooth muscle, an auxiliary beta-subunit is found in a 1:1 stoichiometry. The beta-subunit exhibits its effect on the Maxi K+ channel by effectively decreasing by 5- to 10- fold the concentration of calcium required to keep the pore open. Maxi K+ beta is the target for possible therapeutics because of its role in blood flow and blood pressure regulation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7689R-CY7)
Fournisseur:
Bioss
Description:
Potassium channels are a group of ubiquitously expressed proteins that serve numerous functions in excitable and non-excitable cells. One class of integral membrane potassium channels is the large conductance, calcium-activated potassium channel (Maxi K+). Maxi K+ differs from most other potassium channels in that its activation is controlled by both increases in intracellular calcium and by membrane depolarization. Maxi K+ dual activation is possible because of its structure. The core of the channel, which is similar to other potassium channels, is a Maxi K+ alpha homotetramer that contains both a voltage sensor and an intracellular calcium binding domain. In vascular smooth muscle, an auxiliary beta-subunit is found in a 1:1 stoichiometry. The beta-subunit exhibits its effect on the Maxi K+ channel by effectively decreasing by 5- to 10- fold the concentration of calcium required to keep the pore open. Maxi K+ beta is the target for possible therapeutics because of its role in blood flow and blood pressure regulation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7689R-CY3)
Fournisseur:
Bioss
Description:
Potassium channels are a group of ubiquitously expressed proteins that serve numerous functions in excitable and non-excitable cells. One class of integral membrane potassium channels is the large conductance, calcium-activated potassium channel (Maxi K+). Maxi K+ differs from most other potassium channels in that its activation is controlled by both increases in intracellular calcium and by membrane depolarization. Maxi K+ dual activation is possible because of its structure. The core of the channel, which is similar to other potassium channels, is a Maxi K+ alpha homotetramer that contains both a voltage sensor and an intracellular calcium binding domain. In vascular smooth muscle, an auxiliary beta-subunit is found in a 1:1 stoichiometry. The beta-subunit exhibits its effect on the Maxi K+ channel by effectively decreasing by 5- to 10- fold the concentration of calcium required to keep the pore open. Maxi K+ beta is the target for possible therapeutics because of its role in blood flow and blood pressure regulation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-7689R-CY5.5)
Fournisseur:
Bioss
Description:
Potassium channels are a group of ubiquitously expressed proteins that serve numerous functions in excitable and non-excitable cells. One class of integral membrane potassium channels is the large conductance, calcium-activated potassium channel (Maxi K+). Maxi K+ differs from most other potassium channels in that its activation is controlled by both increases in intracellular calcium and by membrane depolarization. Maxi K+ dual activation is possible because of its structure. The core of the channel, which is similar to other potassium channels, is a Maxi K+ alpha homotetramer that contains both a voltage sensor and an intracellular calcium binding domain. In vascular smooth muscle, an auxiliary beta-subunit is found in a 1:1 stoichiometry. The beta-subunit exhibits its effect on the Maxi K+ channel by effectively decreasing by 5- to 10- fold the concentration of calcium required to keep the pore open. Maxi K+ beta is the target for possible therapeutics because of its role in blood flow and blood pressure regulation.
UOM:
1 * 100 µl
Fournisseur:
WTW
Description:
L'inoLab® Multi 9310 est idéal pour tous les laboratoires qui ont besoin d'une documentation complète, ou qui veulent avoir les processus de mesure les plus efficaces et avec le moins d'erreurs possible. Pour la mesure d'un seul paramètre parmi le pH, la conductivité et l'oxygène.
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est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 016 385 011
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