15487 Results for: "Perfluoro(2-iodo-2-methylpentane)&pageNo=40&view=easy"

Supplier: Thermo Fisher Scientific

Benzyl mercaptan, polymer supported 2,0-4,0 mmol/g 2.0-4.0 mmol/g on poly(styrene-divinylbenzene), cross-linked with 1% DVB 100-200 mesh

Supplier: VWR Chemicals

Ferroin (1,10-phenanthrolineferrous sulphate complex) 1/40 mol/l, AVS TITRINORM redox indicator

Supplier: Merck

Tetrabutylphosphonium hydroxide 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Tetrabutylammonium hydroxide 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Benzyltrimethylammonium hydroxide 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Sodium deuteroxide 40% in D₂O (99% D) (Isotopic), Sigma-Aldrich®

Supplier: Merck

Pyruvaldehyde (methylglyoxal) 40% in aqueous solution, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific

Acrylamide : Bisacrylamide (19:1) 40% mix in water for biochemistry

Supplier: QED Bioscience

Anti-Amyloid Beta 1-40 Mouse Monoclonal Antibody

Supplier: Thermo Fisher Scientific

tri-Calcium phosphate (35 - 40% Ca) for analysis

Supplier: Merck

L(+)-Lactic acid 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Sodium permanganate 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Tetrabutylammonium hydroxide 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Pyruvaldehyde (methylglyoxal) 40% in aqueous solution, Sigma-Aldrich®

Supplier: Biorbyt

Anti-Adenovirus 40 + 41 Mouse Monoclonal Antibody

Supplier: Merck

Selenic acid 40% in aqueous solution, Sigma-Aldrich®

Supplier: Thermo Fisher Scientific

Acrylamide : Bisacrylamide (29:1) 40% mix in water for biochemistry

Supplier: Thermo Scientific

2-Mercaptopyridine-N-oxide sodium salt 40% in aqueous solution

Supplier: Abcam

Mouse monoclonal [AC-40] to Actin.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Abcam

Human Amyloid beta 1-40 ELISA kit is a Sandwich (quantitative) ELISA kit for the measurement of Human Amyloid beta 1-40 in Human in plasma, cell culture supernatant, Serum samples.

Supplier: ZEISS

Accessory for microscopes, For: Axiostar, Screw-in diaphragm part with field of view 18 mm

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen Signalling.

Supplier: Abcam

Human YKL-40 ELISA Kit is a single-wash 90-min Simplestep used to quantify Human YKL-40 with a sensitivity of 3,9 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader - Validated on a number of sample types including cerebrospinal fluid (CSF).

Supplier: Bioss

DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen Signalling.