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γ-L-Glutamyl-p-nitroanilide hydrochloride, beige powder

Supplier: MP Biomedicals

Description: γ-L-Glutamyl-p-Nitroanilide hydrochloride is suitable for use as a substrate for g-Glutamyl transpeptidase.

N-α-Benzoyl-L-arginine 4-nitroanilide hydrochloride, white powder

Supplier: MP Biomedicals

Description: Chromogenic substrate for trypsin and other proteolytic enzymes.

L-Leucine-p-nitroanilide 99%

Supplier: Thermo Scientific

Description: L-Leucine-p-nitroanilide 99%

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L(-)-Glutathione (reduced form) ≥98%

Supplier: Thermo Scientific

Description: L(-)-Glutathione (reduced form) ≥98%

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L(-)-Glutathione (reduced form) ≥98%, high purity

Supplier: VWR Chemicals

Description: L(-)-Glutathione (reduced form) ≥98%, high purity

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L(-)-Glutathione (reduced form) ≥97%

Supplier: Thermo Scientific

Description: L(-)-Glutathione (reduced form) ≥97%

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Tritirachium album proteinase K, MP Biomedicals

Supplier: MP Biomedicals

Description: Suitable for both protein and nucleic acid isolation. Exhibits proteolytic activity on proteins, peptides, glycoproteins, amides and esters. Also active with nitroanilides of amino acids with protected amino groups, excluding arginine. Useful in the isolation of DNA and RNA, in the analysis of membrane structures and protein structure. Proteolytic activity: >30mAnson Units/mg Unit definition: One Anson unit is the amount of enzyme which liberates 1 µmol of Folin-positive amino acids per minute at pH 7,5 and 35 °C, using hemoglobin as substrate.

L(-)-Glutathione (reduced form) ≥98%, off-white powder

Supplier: MP Biomedicals

Description: Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutamyl amino acids and reductive cleavage of disulphide bonds.

L(-)-Glutathione (reduced form)

Supplier: PanReac AppliChem

Description: L(-)-Glutathione (reduced form)

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Alamethicin 50%, powder

Catalog Number: (ICNA0215900905)

Supplier: MP Biomedicals

Supplier Article Number:: 0215900905

Description: Alamethicin is a monovalent cation ionophore that can mimic nerve action potential across artificial membranes. It increases the incorporation of 32P into phosphatidylinositol 4-phosphate and sarcoplasmic reticulum vesicles permeability and causes fusion of lipid vesicles.

UOM: 1 * 5 mg

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Bovine alpha-Chymotripsin (from Pancreas), MP Biomedicals

Supplier: MP Biomedicals

Description: Preparation Method
Produced from 3× crystallised chymotrypsinogen

α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology.

Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.

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L(-)-Glutathione (reduced form) ≥98%, off-white powder cell culture reagent

Supplier: MP Biomedicals

Description: Storage: Store at +4 °C, store under nitrogen
Glutathione is the major low molecular weight thiol compound of the living plant or animal cell. It is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. The sulfhydryl (thiol) group (SH) of cysteine serves as a proton donor and is responsible for the biological activity of glutathione.
Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutanyl amino acids and reductive cleavage of disulfide bonds.
Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.