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: Beckman Coulter

Optima™, SW 40 Ti swinging bucket rotor package, For: Ultracentrifugation

Supplier: Thermo Fisher Scientific

NP-40 lysis buffer, Thermo Fisher Scientific

Supplier: Thermo Fisher Scientific

Silica gel, Pore size: 40 Å 0.200-0.500 mm for chromatography

Supplier: Thermo Fisher Scientific

Polyethyleneimine, on silica beads 20-40 mesh anion exchange resin

Supplier: Thermo Fisher Scientific

Magnesium hydroxide carbonate tetrahydrate (∼40 - 43,5% MgO), Reagent Grade

Supplier: Thermo Fisher Scientific

Viscometry Standards, Viscosity at 40 °C: 930±6 cSt, Viscosity at 100 °C: 82 cSt

Supplier: Thermo Fisher Scientific

Diamond (natural) ≥99.9% (metals basis), powder 40-60 micron

Supplier: Antibodies.com

Human Cyclophilin 40 ELISA kit is a 90 minutes sandwich Enzyme-Linked Immunosorbent Assay (sELISA) designed for the in vitro quantitative determination of human Cyclophilin 40 in serum, plasma, and other biological fluids.

Supplier: Thermo Fisher Scientific

Silver ≥99.9% (metals basis), nanopowder APS 20-40 nm

Supplier: Thermo Fisher Scientific

Applications: Testing of peroxide

Supplier: Thermo Fisher Scientific

Diamond (synthetic) ≥99.9% (metals basis), powder 40-60 micron

Supplier: Thermo Fisher Scientific

Silica gel, Pore size: 40 Å 0.060-0.200 mm for chromatography

Supplier: Merck

Os EnCat® 40 is osmium tetroxide encapsulated within a porous cross-linked polyurea matrix.

Supplier: Merck

Glyoxal 40% in aqueous solution, Sigma-Aldrich®

Supplier: CHEMPUR

Hydrofluoric acid 40%, pure analytical reagent

Supplier: Merck

1-Hydroxy-2-pyridinthione sodium salt 40% in water

Supplier: CHEMPUR

Hydrogen peroxide 40%, pure analytical reagent

Supplier: Merck

Urea 40% in aqueous solution, Sigma-Aldrich®

Supplier: Merck

Benzyltrimethylammonium hydroxide 40% in methanol, Sigma-Aldrich®

Supplier: Abcam

Rabbit polyclonal to Cyclophilin 40.

Supplier: Merck

Petroleum spirit, 40…80 °C, EMPLURA®, Supelco®

Supplier: US Biological

Anti-Amyloid 1-40, 42 Mouse Monoclonal Antibody [clone: 6D4]

Supplier: Thermo Fisher Scientific

Calcium sulphate, Drierite™ 20-40 mesh for drying, without indicator

Supplier: CHEMPUR

Citric acid monohydrate 40% in aqueous solution

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

PE Mouse monoclonal [TP1/40] to CD11a.

Supplier: CHEMPUR

Nitric acid 40%, pure analytical reagent

Supplier: CHEMPUR

Acetic acid 40%, pure analytical reagent