15490 Results for: "Sartorius+Balances&pageNo=40&view=list"

Supplier: Merck

Sodium deuteroxide 40% in D₂O (99.5% D) (Isotopic), Sigma-Aldrich®

Supplier: Abcam

Rabbit monoclonal [EPR22366-40] to EPO-R.

Supplier: Merck

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

Supplier: Thermo Fisher Scientific

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

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: Merck

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

Supplier: PerkinElmer

Elemental analyser, Axial view purge extension window

Supplier: Merck

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

Supplier: Merck

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

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: QED Bioscience

Anti-Amyloid Beta 1-40 Mouse Monoclonal Antibody

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: Thermo Fisher Scientific

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

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: Spectrum Chemical

Polyoxyl 40 Stearate, Type II, NF is commonly used in pharmaceutical formulations as an emulsifier and a surfactant.

Supplier: PerkinElmer

Elemental analyser, Axial view purge extension window

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

Mouse monoclonal [AC-40] to Actin.

Supplier: Thermo Fisher Scientific

Tungsten, gauze woven from wire 40 mesh woven from 0.025mm (0.001in)

Supplier: Antibodies.com

Rabbit polyclonal antibody to YKL-40/CHI3L1 for WB and ICC/IF with samples derived from human and mouse.

Supplier: Antibodies.com

Rabbit polyclonal antibody to YKL-40 / CHI3L1 for WB and ICC/IF with samples derived from human and mouse.

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: 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: Thermo Fisher Scientific

Hexachloroplatinic(IV) acid hydrate (38 - 40% Pt) 99.9% (trace metals basis)

Supplier: DISCOVER ECHO

Fluorite ELWD objective, Revolve, 40×, Working distance: 2,7 - 4,0 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.