5367 Results for: "Methyl-5-methylthiazole-4-carboxylate&pageNo=56"

Supplier: Ahlstrom-Munksjö

Ahlstrom-Munksjö manufactures a series of extremely high purity, acid washed filter papers designed for use in analytical and gravimetric analysis. The quantitative grades are manufactured from top quality cotton linters using ultra-pure, deionised water and are further treated with dilute acid to remove any remaining organic and inorganic impurities. All quantitative grades are manufactured in a strictly controlled environment that ensures high uniformity and high purity from filter to filter.

Supplier: Whatman products (Cytiva)

The Whatman Mini-UniPrep Syringeless Filters combine four products into one syringeless filter solution for efficient chromatography sample preparation for a broad range of applications. They are built for fast and easy high performance liquid chromatography/ultra high performance liquid chromatography sample preparation and analysis.

Supplier: Avantor Fluid Handling

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

Supplier: Avantor Fluid Handling

FTNG MAXI FLANGEXB 3/4 PVDF 1 * 1 items

Supplier: Avantor Fluid Handling

ULTRA PLAT SIL 1/2X3/4 50FT 1 * 1 items

Supplier: Cole Parmer

HEATER ELEMENT ASSEMBLY 1 * 1 items

Supplier: Sartorius Balances

Semi-micro balances have a readability of 0,01 mg or 10 µg and a maximum weighing capacity of up to 220 g.

Supplier: Avantor Fluid Handling

ULTRA PLAT SIL 3/32X11/32 25FT 1 * 1 items

Supplier: Avantor Fluid Handling

Brooks Acrylic Variable Area Flowmeter, 1/8'' NPTF 0.1 - 10 LPM 1 * 1 items

Supplier: NICKEL ELECTRO

Lid, with insulated handles, 56liter, flat two piece, stainless steel, 40x30x2cm . 1 * 1 items

Supplier: Cole Parmer

Motor Assembly 1 * 1 items

Supplier: Avantor Fluid Handling

1/2 X 1 PT TBNG 1 * 100 items

Supplier: Thermo Fisher Scientific

Photoactivatable Biotin, Biotin-LC-ASA , Psoralen-PEG3-Biotin and TFPA-PEG3-Biotin each contain a photoactivatable group. When exposed to UV light, they become activated and insert non specifically into nearby molecules. These reagents may be used to label proteins and peptides, but they are also useful in labeling DNA, RNA and other molecules that do not contain any readily reactive functional groups. Psoralen-PEG3-Biotin contains a reactive psoralen group and is
designed to efficiently label nucleic acids. The psoralen group intercalates into the helix of DNA, allowing it to label efficiently and selectively. The psoralen can also stack along with the bases of single-stranded DNA or RNA increasing labeling efficiency and selectivity.

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.

Supplier: THERMO H + P LABORTECHNIK

Compact magnetic stirrers with VARIOMAG drive, hermetically sealed in resistant stainless steel housing (except MINI units which are plastic), making these stirrers ideal for use directly in water baths. MINI stirrers are ideal for integration in analytical instruments, cuvette holders or photometers due to their size, however these plastic units are not designed for use directly in baths. There are units with up to 60 stirring positions in this range, and a choice of three external control units. The TELEMODUL 7 has one power setting, the TELEMODUL 20 C has four power settings: 25%, 50%, 75% and 100% and can store three programmes, the TELEMODUL 40 C features ten different power settings from 10 to 100% and a RS232 interface.

Supplier: Bohlender

GL 32, Durchmesser: 10,0 mm , SW 32 Kappe aus PPS/Glasfaser schwarz, Innenteil aus PPS und PTFE, max. Temperatur + 250 C 1 * 1 items

Supplier: EPPENDORF

For any application that requires sample/reaction mixing and heating the Eppendorf® ThermoMixer F family is what you need. Whether you work with 0,5/1,5/2,0 ml tubes or plates (MTP and DWP) the dedicated fixed blocks offer a perfect solution for your special application.

Supplier: Brand

These tips are manufactured under cleanroom conditions and are automatically packaged to ensure that the tips are consistently free from contamination.

Supplier: SARSTEDT

S-Monovette® is a blood collection system that combines two blood collection techniques – aspiration and vacuum. The S-Monovette® is suitable for all vein conditions and achieves an optimal sample quality, thereby producing the best results. The aspiration technique is a gentle technique for routine blood collection. Using the vacuum technique, a 'fresh' vacuum is always available.

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.

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.

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.

Supplier: Cole Parmer

CHARGER FOR UK AND IRELAND 1 * 1 items

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.

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.

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.

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.

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.

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.

Supplier: ProSci Inc.

There are two types of cytokeratins/keratins/CKs: the acidic type I cytokeratins and the basic or neutral type II cytokeratins. The subsets of cytokeratins which an epithelial cell expresses depends mainly on the type of epithelium, the moment in the course of terminal differentiation and the stage of development. Thus this specific keratin fingerprint allows the classification of all epithelia upon their keratin expression profile. Furthermore this applies also to the malignant counterparts of the epithelia (carcinomas), as the keratin profile tends to remain constant when an epithelium undergoes malignant transformation. The main clinical implication is that the study of the keratin profile by immunohistochemistry techniques is a tool of immense value widely used for tumor diagnosis and characterization in surgical pathology. [Wiki].