15038 Results for: "3-Heptenoic+acid&pageNo=40"

Supplier: Abcam

PE Mouse monoclonal [HP-40] to IL-12.

Supplier: Abcam

Rabbit monoclonal [EPR22509-40] to CD36.

Supplier: Abcam

Rabbit monoclonal [EPR22959-40] to TrkC.

Supplier: Biorbyt

Anti-Adenovirus 40 + 41 Mouse Monoclonal Antibody

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: Abcam

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

Supplier: Honeywell Chemicals

Hydrofluoric acid 40 - 45%, Technical Grade, Fluka™

Supplier: Thermo Fisher Scientific

Acrylamide : Bisacrylamide (37.5:1) 40% mix in water for biochemistry

Supplier: Thermo Fisher Scientific

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

Supplier: Thermo Fisher Scientific

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

Supplier: EBRO

EBI 40 loggers are designed for mapping applications at high temperatures. In combination with thermal insulation box (620-1804), they can be used for 2 hours at 250 °C. At higher temperatures, the logger can be placed remotely and temperature characteristics viewed on the display.

Supplier: QED Bioscience

Anti-Amyloid Beta 1-40 Mouse Monoclonal Antibody

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 Signalling.

Supplier: Thermo Fisher Scientific

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

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: Merck

L(+)-Asparagine monohydrate ≥99.0% (dry basis) for biochemistry pH 4.0 - 5.5 (20 g/l, H₂O, 20 °C), Millipore®

Supplier: Merck

Amberlite® FPC23 hydrogen form 16 - 40 mesh (strongly acidic cation exchanger), Supelco®

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 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: 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: Thermo Fisher Scientific

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

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.