You Searched For: S-Farnesyl-L-cysteine+methyl+ester


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Catalog Number: (10481-398)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.


Catalog Number: (10072-596)
Supplier: Prosci
Description: Neurturin is a disulfide-linked homodimer neurotrophic factor structurally related to GDNF, Artemin, and Persephin. These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Neurturin signals through a multicomponent receptor system, composed of RET and one of four GFR alpha (alpha1-alpha4) receptors. Neurturin promotes the development and survival of sympathetic and sensory neurons by signaling through a receptor system composed of RET and GFRalpha2. The functional form of human Neurturin is a disulfide-linked homodimer, of two 11.8 kDa polypeptide monomers (206 total amino acid residues). Each monomer contains seven conserved cysteine residues, one of which (Cys 69) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cysteine knot configuration.


Catalog Number: (89356-356)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to Caspase 3 (caspase 3, apoptosis-related cysteine peptidase)


Catalog Number: (89321-342)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to Caspase 4 (caspase 4, apoptosis-related cysteine peptidase)


Catalog Number: (10481-394)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.


Catalog Number: (10481-396)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.


Catalog Number: (10481-400)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.


Catalog Number: (89356-440)
Supplier: Genetex
Description: Rabbit Polyclonal antibody to Caspase 8 (caspase 8, apoptosis-related cysteine peptidase)


Catalog Number: (CA80108-946)
Supplier: MilliporeSigma
Description: Member of the interleukin-1[beta] converting enzyme (ICE) family of cysteine proteases that exists in cells as an inactive proenzyme and is activated during the initiation of apoptosis

Catalog Number: (10424-026)
Supplier: Bioss
Description: CDO1 (cysteine dioxygenase, type I) is a 200 amino acid protein that belongs to the cysteine dioxygenase family and is involved in organosulfur biosynthesis. Existing as a monomer and expressed at high levels in liver and placenta and at lower levels in brain, pancreas and heart, CDO1 functions as a dioxygenase that uses iron and zinc as cofactors to catalyze the conversion of L-cysteine and oxygen to 3-sulfinoalanine. Via its catalytic activity, CDO1 is involved in pyruvate-, sulfate- and taurine-related metabolic pathways and is a crucial regulator of cysteine concentrations within the cell. Human CDO1 shares 94% amino acid identity with its rat counterpart, suggesting a conserved role between species. The gene encoding CDO1 maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm or of chromosome 5 altogether is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.PathwayOrganosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2.


Catalog Number: (10391-558)
Supplier: Bioss
Description: Cysteine protease ATG4D: Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms. Cysteine protease ATG4D, mitochondrial: Plays a role as an autophagy regulator that links mitochondrial dysfunction with apoptosis. The mitochondrial import of ATG4D during cellular stress and differentiation may play important roles in the regulation of mitochondrial physiology, ROS, mitophagy and cell viability.


Catalog Number: (76081-154)
Supplier: Bioss
Description: The cysteine-rich, adipose tissue-specific, secretory factor resistin (resistance to insulin, also known as ADSF) is a secreted hormone that potentially links obesity to diabetes. Resistin is rich in serine and cysteine residues and contains a unique cysteine repeat motif. Resistin and the resistin-like molecules share the characteristic cysteine composition and other signature features. Resistin-like a is a secreted protein that has restricted tissue distribution and is most highly expressed in adipose tissue. Another family member, Resistin-like b, is a secreted protein expressed only in the gastrointestinal tract, particularly in the colon, in both mouse and human. Resistin-like b expression is highest in proliferative epithelial cells and is markedly increased in tumors, suggesting a role in intestinal proliferation.


Supplier: Bachem Americas
Description: Sequence: Fmoc-Cys(StBu)-OH

Supplier: Peprotech
Description: Fractalkine is a CX3CL chemokine that signals through the CX3CR1 receptor. Fractalkine has been shown to chemoattract monocytes, microglia cells and NK cells. Fractalkine is, at this time, the only CXC3C chemokine that contains three amino acid residues between the first and second cysteine residues of the chemokine domain. The Fractalkine gene encodes for a 397 amino acid precursor protein containing a 24 amino acid signal sequence, a chemokine domain, and a "mucin-like stalk" sequence, which is followed by the transmembrane domain containing approximately 20 amino acids, and a C-terminal cytoplasmic domain. The extracellular chemokine domain contains 76 amino acid residues, including the four conserved cysteine residues found in other chemokines. Recombinant Human Fractalkine is an 8.5 kDa protein containing 76 amino acid residues, including the four conserved cysteine residues present in CC chemokines. Recombinant Rat Fractalkine (CX3CL1) is an 8.7 kDa protein containing 76 amino acid residues, including the four conserved cysteine residues present in CC chemokines.

Supplier: Bon Opus Biosciences
Description: Bon Opus Biosciences offers quality recombinant proteins products covering a broad collection of cytokines, enzymes, diagnostic and detection reagents, and other protein-related products

Supplier: Peprotech
Description: MEC is a secreted CC chemokine expressed primarily by epithelial cells of the bronchioles, salivary gland, mammary gland and colon. MEC signals through the CCR10 receptor, and chemoattracts resting CD4, CD8 T-cells and eosinophils. MEC contains six cysteines, including the four highly conserved cysteine residues present in CC chemokines. Recombinant Human MEC (CCL28) is a 12.3 kDa protein containing 108 amino acid residues.

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