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Artikel-Nr: (BOSSBS-7689R-A647)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-A647
Beschreibung: 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


Artikel-Nr: (BOSSBS-6634R-A555)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-6634R-A555
Beschreibung: 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


Artikel-Nr: (BOSSBS-6634R-CY5.5)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-6634R-CY5.5
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-FITC)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-FITC
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-A555)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-A555
Beschreibung: 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


Lieferant: INTERSCIENCE
Beschreibung: Verteileranordnung innen für einfache Pumpe (Ø 3,2 mm), Für: Dilu<i>Flow</i>® Elite, Dilu<i>Flow</i>® Pro

Artikel-Nr: (ENDR8F3B25-34VW1)
Lieferant: Endress+Hauser
Hersteller Artikel Nummer : 8F3B25-34VW1
Beschreibung: Promass F has a long-standing reputation as a highly accurate sensor.
UOM: 1 * 1 ST


Lieferant: VWR Collection
Beschreibung: Avantor's high pressure single-use transfer hose with Avantor SterilEnz™ connections maintain the durability of high pressure hose products while providing the benefits and flexibility of single-use assemblies.

Artikel-Nr: (SCOI285103553)
Lieferant: SI Analytics
Hersteller Artikel Nummer : 285103553
Beschreibung: Einzel-Platinelektrode, mit Glasschaft und ringförmigem Sensor (Ø 6 mm). Für Titrationsanwendungen.
UOM: 1 * 1 ST


Artikel-Nr: (BOSSBS-7689R-A350)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-A350
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-CY3)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-CY3
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-CY5)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-CY5
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-CY7)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-CY7
Beschreibung: 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


Artikel-Nr: (BOSSBS-7689R-CY5.5)
Lieferant: Bioss
Hersteller Artikel Nummer : BS-7689R-CY5.5
Beschreibung: 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


Artikel-Nr: (BEHRB00645358)
Lieferant: BEHR
Hersteller Artikel Nummer : B00645358
Beschreibung: Soxhlet-Extraktionsapparate, WD 30 Monitoring unit with two flow sensors and solenoid valve, as well as cables to connect it to the controller (1.5 m)
UOM: 1 * 1 ST


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