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S-(Carboxymethyl)-L-cysteine 97%

Dodavatel: Thermo Scientific

Popis: S-(Carboxymethyl)-L-cysteine 97%

Bezpečnostní list

S-(Carboxymethyl)-L-cysteine 98%

Dodavatel: Thermo Scientific

Popis: CAS No.: 638-23-3

Bezpečnostní list

L-Cysteine-glutathione disulphide

Katalogové číslo: (APOSOR9955T-10MG)

Dodavatel: Apollo Scientific

Popis: L-Cysteine-glutathione disulphide

Měrná jednotka: 1 * 10 mg

Akce

N/A Each

S-(Carboxymethyl)-L-cysteine

Dodavatel: Spectrum Chemical

Popis: S-Carboxymethyl-L-cysteine, also known as Rhinathiol or Humex, is a mucolytic that minimizes the viscosity of sputum so it can be used to treat chronic obstructive pulmonary disorder and bronchiectasis.

Anti-NARF Rabbit Polyclonal Antibody

Katalogové číslo: (PRSI26-882)

Dodavatel: ProSci Inc.

Popis: Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. NARF binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. NARF is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases.Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins. Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif. This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A. The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain. It may be a component of a prelamin A endoprotease complex. The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited sequence similarity with iron-only bacterial hydrogenases. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.

Měrná jednotka: 1 * 50 µG

Akce

N/A Each

L(-)-Glutathion (redukovaná forma) ≥98%, off-white powder cell culture reagent

Dodavatel: MP Biomedicals

Popis: 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.