13602 Results for: "Wieszaki+na+odzie\u017C&pageNo=40"

Supplier: Merck

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

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: POCH AVANTOR BRAND

Petroleum spirit, 40…60 °C, pure analytical reagent

Supplier: CHEMPUR

Petroleum spirit, 40…60 °C, pure analytical reagent

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

Mouse monoclonal [AC-40] to Actin.

Supplier: Merck

Dimethylamine 40% in aqueous solution for synthesis, Sigma-Aldrich®

Supplier: Merck

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

Supplier: Merck

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

Supplier: Merck

Benzyltrimethylammonium hydroxide 40% in methanol for synthesis, Sigma-Aldrich®

Supplier: CHEMPUR

Ethylene glycol 40% in aqueous solution, Technical Grade

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: 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: 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: 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: VWR Collection

Plan achromatic objective, 40×

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: Spectrum Chemical

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

Supplier: Thermo Fisher Scientific

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

Supplier: Thermo Fisher Scientific

PIPES lysis buffer with NP-40 (2X), Thermo Fisher Scientific

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: VWR Collection

Achromatic objective, VWR®, 40×

Supplier: Abcam

Rabbit monoclonal [EPR16671-40] to STAT5a + STAT5b.

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)