M\\u00F6dinger+Elektro-Gro\\u00DFhandelshaus
Supplier:
HUMAN ACTIVE TECHNOLOGY, LLC
Description:
Add 4" or 8.5" of reach to an Innovative wall mount or pole mount product.
Catalog Number:
(10390-748)
Supplier:
Bioss
Description:
This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].
Catalog Number:
(10390-744)
Supplier:
Bioss
Description:
This gene encodes an accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), or NADH:ubiquinone oxidoreductase, the first multi-subunit enzyme complex of the mitochondrial respiratory chain. Complex I plays a vital role in cellular ATP production, the primary source of energy for many crucial processes in living cells. It removes electrons from NADH and passes them by a series of different protein-coupled redox centers to the electron acceptor ubiquinone. In well-coupled mitochondria, the electron flux leads to ATP generation via the building of a proton gradient across the inner membrane. Complex I is composed of at least 41 subunits, of which 7 are encoded by the mitochondrial genome and the remainder by nuclear genes. [provided by RefSeq, Jul 2008].
Supplier:
Electron Microscopy Sciences
Description:
Premiere® Blades are made from carbon steel, individually foil wrapped and gamma radiation sterilized.
Catalog Number:
(10244-110)
Supplier:
Bioss
Description:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalog Number:
(102096-348)
Supplier:
Electron Microscopy Sciences
Description:
Wipes are 100% biodegradable.
Supplier:
Electron Microscopy Sciences
Description:
Run antigen unmasking in 6 various buffers at once.
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Catalog Number:
(102091-638)
Supplier:
Electron Microscopy Sciences
Description:
Type 5 mini, super thin tips, 83 mm.
Catalog Number:
(101640-730)
Supplier:
Atrix International
Description:
The Express Plus 1 Quart HEPA dry particulate vacuum is an economical, light duty vacuum
Catalog Number:
(10390-260)
Supplier:
Bioss
Description:
Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. This nuclear gene encodes subunit VIb. Mutations in this gene are associated with severe infantile encephalomyopathy. Three pseudogenes COX6BP-1, COX6BP-2 and COX6BP-3 have been found on chromosomes 7, 17 and 22q13.1-13.2, respectively. [provided by RefSeq].
Supplier:
Electron Microscopy Sciences
Description:
These scales are used for the measuring of lengths of specimen or distances between points on a variety of different shaped objects.
Supplier:
Electron Microscopy Sciences
Description:
We are proud to offer a multi-compartment container in the shape of a dish and half prefilled with 10% Neutral buffered Formalin, for holding and transporting biopsies
Catalog Number:
(10108-840)
Supplier:
Prosci
Description:
Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. COX4I1 is the nuclear-encoded subunit IV isoform 1 of the human mitochondrial respiratory chain enzyme.Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. The complex consists of 13 mitochondrial- and nuclear-encoded subunits. The mitochondrially-encoded subunits perform the electron transfer and proton pumping activities. The functions of the nuclear-encoded subunits are unknown but they may play a role in the regulation and assembly of the complex. This gene encodes the nuclear-encoded subunit IV isoform 1 of the human mitochondrial respiratory chain enzyme. It is located at the 3' of the NOC4 (neighbor of COX4) gene in a head-to-head orientation, and shares a promoter with it.
Supplier:
Electron Microscopy Sciences
Description:
These can be used as buffer for diluting primary and secondary antibodies.
Supplier:
Transene
Description:
Transene Acetone LM grade is a "low metals" solvent suitable for electronics and semiconductor cleaning and processing. Low water content.
Supplier:
Electron Microscopy Sciences
Description:
These notebooks feature permanently bound pages with grid lines.
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