U heeft gezocht op: KCL+by+Honeywell

Catalogus nummer: (BOSSBS-11754R-HRP)

Leverancier: Bioss

Omschrijving: SCGN is a 276 amino acid cytoplasmic protein that contains six EF-hand domains and is related to the calicium-binding proteins Calretinin and Calbindin D28K. Expressed in a variety of tissues including stomach, thyroid, colon, brain and neuroendocrine cells, SCGN is thought to be involved in cell proliferation and KCl (potassium chloride)-mediated calcium flux events. Through its interaction with KCl and its subsequent ability to modulate calcium storage pools within the cell, SCGN may function to negatively control growth and differentiation rates and, thus, indirectly inhibit cell replication.

UOM: 1 * 100 µl

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Catalogus nummer: (TEST0554.2051)

Leverancier: Testo

Omschrijving: Opslagdop voor testo 205, met KCI-gelvulling

UOM: 1 * 1 ST

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Leverancier: VWR Chemicals

Omschrijving: A complete range of certified control standards with values ranging from 1,3 to 500000 µs to meet all the requirements for electrochemical analysis.

MSDS Certificaten

Catalogus nummer: (BOSSBS-11754R-A350)

Leverancier: Bioss

Omschrijving: SCGN is a 276 amino acid cytoplasmic protein that contains six EF-hand domains and is related to the calicium-binding proteins Calretinin and Calbindin D28K. Expressed in a variety of tissues including stomach, thyroid, colon, brain and neuroendocrine cells, SCGN is thought to be involved in cell proliferation and KCl (potassium chloride)-mediated calcium flux events. Through its interaction with KCl and its subsequent ability to modulate calcium storage pools within the cell, SCGN may function to negatively control growth and differentiation rates and, thus, indirectly inhibit cell replication.

UOM: 1 * 100 µl

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Catalogus nummer: (BOSSBS-11754R-A488)

Leverancier: Bioss

Omschrijving: SCGN is a 276 amino acid cytoplasmic protein that contains six EF-hand domains and is related to the calicium-binding proteins Calretinin and Calbindin D28K. Expressed in a variety of tissues including stomach, thyroid, colon, brain and neuroendocrine cells, SCGN is thought to be involved in cell proliferation and KCl (potassium chloride)-mediated calcium flux events. Through its interaction with KCl and its subsequent ability to modulate calcium storage pools within the cell, SCGN may function to negatively control growth and differentiation rates and, thus, indirectly inhibit cell replication.

UOM: 1 * 100 µl

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Catalogus nummer: (BOSSBS-11754R-FITC)

Leverancier: Bioss

Omschrijving: SCGN is a 276 amino acid cytoplasmic protein that contains six EF-hand domains and is related to the calicium-binding proteins Calretinin and Calbindin D28K. Expressed in a variety of tissues including stomach, thyroid, colon, brain and neuroendocrine cells, SCGN is thought to be involved in cell proliferation and KCl (potassium chloride)-mediated calcium flux events. Through its interaction with KCl and its subsequent ability to modulate calcium storage pools within the cell, SCGN may function to negatively control growth and differentiation rates and, thus, indirectly inhibit cell replication.

UOM: 1 * 100 µl

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Leverancier: WATER ID PRIMELAB

Omschrijving: The next generation of multitest Photometer, with pH - EC - TDS - ORP - Temperature measurement functionality.

Leverancier: WTW

Omschrijving: Hoogwaardige, verbeterde sensortechnologie gecombineerd met de meest moderne meetelektronica.

Leverancier: G-Biosciences

Omschrijving: 10X PBS (Phosphate Buffered Saline) is a 10 fold concentrated, sterile, pH adjusted blend of phosphate buffer and saline solution, which when diluted 1 to 10 in ultrapure water produces a phosphate buffered saline of 8mM NaH2PO4, 150mM NaCl, 3mM KCl, and 2mM KH2PO4 at pH 7.4.

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Leverancier: WTW

Omschrijving: Deze bewezen en geteste pH-elektroden zijn eenvoudig te gebruiken en bieden hoge kwaliteit en precisie.

Leverancier: WTW

Omschrijving: These special pH electrodes extend the range of the IDS series for enhanced applications in Life Sciences and related applications.

Leverancier: VWR Chemicals

Omschrijving: Avantor offers a comprehensive range of conductivity standards as Certified Reference Materials with the primary use calibrating of conductivity meters.

MSDS Certificaten

Catalogus nummer: (BOSSBS-12997R-A647)

Leverancier: Bioss

Omschrijving: Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

UOM: 1 * 100 µl

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Catalogus nummer: (BOSSBS-12997R)

Leverancier: Bioss

Omschrijving: Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

UOM: 1 * 100 µl

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Catalogus nummer: (BOSSBS-12997R-FITC)

Leverancier: Bioss

Omschrijving: Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

UOM: 1 * 100 µl

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Catalogus nummer: (BOSSBS-12997R-CY3)

Leverancier: Bioss

Omschrijving: Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

UOM: 1 * 100 µl

Sale