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PharMed®+BPT+Precision+Pump+Tubing


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Numéro de catalogue: (BOSSBS-0744R-A750)

Fournisseur:  Bioss
Description:   Carcinoembryonic antigen-related cell adhesion molecule 8 (CEACAM8) is a highly glycosylated protein expressed only in neutrophils and eosinophils in humans. The precise function of CEACAM8 remains unclear. As a member of the family of carcinoembryonic antigen (CEA), it may play a role in the interaction between granulocytes or between granulocytes and epithelial cells. Expressed in leukocytes of chronic myeloid Leukemia patients and bone marrow.
UOM:  1 * 100 µl
Fournisseur:  INTERSCIENCE
Description:   FlexiPump® is a range of peristaltic pumps for culture media preparation. Use it for serial dispensing of culture media, agar or any liquid diluent for efficient sample preparation.
Fournisseur:  Binder
Description:   The MKF series of dynamic climate chambers has been specially developed as precision heating and cooling chambers for industrial material testing and environment simulation applications. The units are ideal for rapid temperature changes with humidity control and have a higher capacity which exceeds the capability of normal testing chambers. The stainless steel inner chamber has door heating, a heated viewing window with LED interior lighting and programmable condensation protection for the test materials.
Numéro de catalogue: (BOSSBS-0744R-A555)

Fournisseur:  Bioss
Description:   Carcinoembryonic antigen-related cell adhesion molecule 8 (CEACAM8) is a highly glycosylated protein expressed only in neutrophils and eosinophils in humans. The precise function of CEACAM8 remains unclear. As a member of the family of carcinoembryonic antigen (CEA), it may play a role in the interaction between granulocytes or between granulocytes and epithelial cells. Expressed in leukocytes of chronic myeloid Leukemia patients and bone marrow.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-2200R-A750)

Fournisseur:  Bioss
Description:   LDL and HDL transport both dietary and endogenous cholesterol in the plasma. LDL is the main transporter of cholesterol and cholesteryl esters and makes up more than half of the total lipoprotein in plasma. LDL is absorbed by the liver and other tissues via receptor mediated endocytosis. The cytoplasmic domain of the LDL receptor facilitates the formation of coated pits; receptor-rich regions of the membrane. The ligand binding domain of the receptor Recognises apo-B100 on LDL, resulting in the formation of a clathrin-coated vesicle. ATP-dependent proton pumps lower the pH inside the vesicle resulting dissociation of LDL from its receptor. After loss of the clathrin coat the vesicles fuse with lysozomes, resulting in peptide and cholesteryl ester enzymatic hydrolysis. The LDL receptor can be recycled to the cell membrane. Insulin, tri-iodothyronine and dexamethasome have shown to be involved with the regulation of LDL receptor mediated uptake. The protein component of LDL is apolipoprotein B100. LDL contains 2022% protein, 1015% triglycerides, 2028% phospholipids, 3748% cholesteryl esters and 810% cholesterol.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-4131R-CY5)

Fournisseur:  Bioss
Description:   Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-4131R-A350)

Fournisseur:  Bioss
Description:   Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity).
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12549R-A750)

Fournisseur:  Bioss
Description:   Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (AH) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6038R-CY5)

Fournisseur:  Bioss
Description:   A number of specific carrier proteins for members of the vitamin A family have been discovered. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The inducibility of the CRABP2 gene suggests that this isoform is important in retinoic acid-mediated regulation of human skin growth and differentiation. It has been postulated that the CRABP2 gene is transcriptionally regulated by a newly synthesized regulatory protein.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6038R-CY7)

Fournisseur:  Bioss
Description:   A number of specific carrier proteins for members of the vitamin A family have been discovered. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The inducibility of the CRABP2 gene suggests that this isoform is important in retinoic acid-mediated regulation of human skin growth and differentiation. It has been postulated that the CRABP2 gene is transcriptionally regulated by a newly synthesized regulatory protein.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-6038R-CY5.5)

Fournisseur:  Bioss
Description:   A number of specific carrier proteins for members of the vitamin A family have been discovered. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The inducibility of the CRABP2 gene suggests that this isoform is important in retinoic acid-mediated regulation of human skin growth and differentiation. It has been postulated that the CRABP2 gene is transcriptionally regulated by a newly synthesized regulatory protein.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12549R-CY7)

Fournisseur:  Bioss
Description:   Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.
UOM:  1 * 100 µl

Fournisseur:  Bioss
Description:   Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.
UOM:  1 * 100 µl
Numéro de catalogue: (BOSSBS-12549R-CY3)

Fournisseur:  Bioss
Description:   Vacuolar-type H+-ATPase (V-ATPase) is a multisubunit enzyme responsible for acidification of eukaryotic intracellular organelles. V-ATPases pump protons against an electrochemical gradient, while F-ATPases reverse the process, thereby synthesizing ATP. A peripheral V1 domain, which is responsible for ATP hydrolysis, and a integral V0 domain, which is responsible for proton translocation, compose V-ATPase. Nine subunits (A–H) make up the V1 domain and five subunits (a, d, c, c' and c") make up the V0 domain. Like F-ATPase, V-ATPase most likely operates through a rotary mechanism. The V-ATPase V1 B subunit exists as two isoforms. In the inner ear, the V-ATPase B1 isoform functions in proton secretion and is required to maintain proper endolymph pH and normal auditory function. The gene encoding the human V-ATPase B1 isoform maps to chromosome 2cen-q13. Mutations in this gene cause distal renal tubular acidosis associated with sensorineural deafness. The V-ATPase B2 isoform is expressed in kidney and is the only B isoform expressed in osteoclasts. The gene encoding the human V-ATPase B2 isoform maps to chromosome 8p22-p21.
UOM:  1 * 100 µl
Fournisseur:  JULABO GmbH
Description:   Les circulateurs réfrigérés DYNEO™ DD sont des unités de refroidissement puissantes adaptées aux applications internes ou externes entre -50 et +200 °C. Les circulateurs fonctionnent de manière précise et fiable, même à des températures ambiantes élevées, jusqu'à +40 °C. Grâce à l'affichage couleur multilingue de 8,89 cm et à un bouton rotatif unique, l'utilisation est simple et intuitive. Les appareils sont équipés de poignées ergonomiques et d'un robinet de vidange intégré pour un drainage facile et sûr.
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