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5540 results for "2,2,2-trichloroethoxysulphonyl+chloride&pageNo=56"

5540 Results for: "2,2,2-trichloroethoxysulphonyl+chloride&pageNo=56"

PUMP ESYLDII WITH GASKET COUPLING 1 * 1 items

Supplier: Avantor Fluid Handling

PUMP ESYLDII WITH GASKET COUPLING 1 * 1 items

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TUBING SILICONE 0.64MM 1000' 1 * 1 items

Supplier: Avantor Fluid Handling

TUBING SILICONE 0.64MM 1000' 1 * 1 items

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VWR® Real Time Electrophoresis Systems

VWR® Real Time Electrophoresis Systems

Supplier: VWR Collection

VWR® Real Time electrophoresis systems have revolutionised DNA electrophoresis. it is no longer necessary to remove a gel from a tank, place it onto a transilluminator for viewing or place the gel into an imaging system to take a photo. These versatile and compact systems are an all-in-one replacement for a power supply, gel tank, transilluminator and gel imaging system.

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Avantor® Hichrom, HPLC Columns, C18, 5 μm

Avantor® Hichrom, HPLC Columns, C18, 5 μm

Supplier: Avantor

These Avantor® Hichrom C18 columns offer high performance in order to tackle the most challenging reversed-phase applications. The use of ultra pure silica, advanced bonding technology, superior column specification and comprehensive batch validation all contribute to the columns’ excellent reproducibility.

   Sustainable Options Available
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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Cy7®)

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Cy3®)

Supplier: Bioss

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.

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Pilot's jacket, Icon

Pilot's jacket, Icon

Supplier: FRISTADS KANSAS

Functional, two-tone winter jacket made from Beaver nylon (50% nylon, 50% cotton), a hard-wearing and tear-proof material that is resistant to dirt, oil and water. With faux fur on the collar and on the body, quilted lining in the sleeves and contrasting seams.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Alexa Fluor® 555)

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Alexa Fluor® 350)

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (FITC (Fluorescein Isothiocyanate))

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Cy5®)

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody

Supplier: Bioss

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.

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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Alexa Fluor® 647)

Supplier: Bioss

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.

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Storage tubes, 2D barcoded, Matrix™

Storage tubes, 2D barcoded, Matrix™

Supplier: THERMO MATRIX TECHNOLOGIES

Permanently attached, laser-etched 2D barcodes on the bottom of each tube allow you to scan and decode tubes at once without removing them from the rack and allow data to be associated with each tube.

   Sustainable Options Available
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Anti-ATP6V1B2 Rabbit Polyclonal Antibody (Alexa Fluor® 488)

Supplier: Bioss

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.

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Overall, C.I., Design B, black

Supplier: FRISTADS KANSAS

Industrial overall made of 65% polyester and 35% cotton, with soft nap on reverse side. The black overall is available with several different accent colours. The accent colour can be found on the top of the collar, on the inside front flap, on the pocket edges and and as a stripe on front and back.

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Industrial jacket, Fristads® PR54-420, design B, black

Industrial jacket, Fristads® PR54-420, design B, black

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Industrial jacket, Fristads® PR54-420, design B, navy blue

Industrial jacket, Fristads® PR54-420, design B, navy blue

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Industrial jacket, Fristads® PR54-420, design B, dark grey

Industrial jacket, Fristads® PR54-420, design B, dark grey

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Industrial jacket, Fristads® PR54-420, design B, royal blue

Industrial jacket, Fristads® PR54-420, design B, royal blue

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Masterflex L/S Drive with Easy-Load II High-Performance Pump Head, Stainless Steel, 600 rpm - Delivered with Masterflex Power Cord, 230 VAC, European Plug Type-F 180 cm long 1 * 1 items

Supplier: Avantor Fluid Handling

Masterflex L/S Drive with Easy-Load II High-Performance Pump Head, Stainless Steel, 600 rpm - Delivered with Masterflex Power Cord, 230 VAC, European Plug Type-F 180 cm long 1 * 1 items

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Trousers, Fristads® PR54-220, Design A, navy blue (long sizes)

Trousers, Fristads® PR54-220, Design A, navy blue (long sizes)

Supplier: FRISTADS KANSAS

Thanks to their durability and comfort, these trousers are perfectly suitable for use in garages as well as in industrial and service companies. The material is made of 65% polyester and 35% cotton. The inside is brushed and provides a comfortable cotton feel. The outside is very hardwearing and does not bleach, even after countless washes.

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Industrial jacket, Fristads® PR54-420, design A, black

Industrial jacket, Fristads® PR54-420, design A, black

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Industrial jacket, Fristads® PR54-420, design A, navy blue

Industrial jacket, Fristads® PR54-420, design A, navy blue

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Masterflex L/S Drive with Easy-Load II High-Performance Pump Head, Stainless Steel, 600 rpm - Delivered with Masterflex Power Cord, 230 VAC, British Plug Type-G 180 cm long 1 * 1 items

Supplier: Avantor Fluid Handling

Masterflex L/S Drive with Easy-Load II High-Performance Pump Head, Stainless Steel, 600 rpm - Delivered with Masterflex Power Cord, 230 VAC, British Plug Type-G 180 cm long 1 * 1 items

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3/32 X 15/32 PT TBNG 1 * 25 items

Supplier: Avantor Fluid Handling

3/32 X 15/32 PT TBNG 1 * 25 items

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Industrial jacket, Fristads® PR54-420, design A, dark grey

Industrial jacket, Fristads® PR54-420, design A, dark grey

Supplier: FRISTADS KANSAS

Thanks to its durability and high degree of comfort, the PR54 jacket is perfectly suited to workshops and industrial and service enterprises. The material is made from 65% polyester and 35% cotton. The inside is brushed and as a result conveys a pleasantly comfortably cotton feeling. The outside is also resistant to the roughest demands and will not fade even after countless washes.

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Dry box gloves, neoprene

Dry box gloves, neoprene

Supplier: PIERCAN

Ambidextrous gauntlets manufactured from soft black polychloroprene rubber that is self-extinguishing thus providing a good flame resistance for the gauntlet. It is the ideal elastomer providing the best compromise to the conjugate action of several potentially harmful agents, for example oil and ozone. Available for use with various diameter ports.

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UV/Vis Calibration Standards

UV/Vis Calibration Standards

Supplier: HELLMA

The Hellma® calibration standards comply with all necessary standards and regulations and thus offer the highest quality for recalibrating your spectrometer.

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