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Catalog Number: (BOSSBS-8300R-A555)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8300R-FITC)
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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-CY3)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-FITC)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8300R-A750)
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 oxidised 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 oxidised 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 oxidised Prx can be reduced back to the active form during recovery after oxidative stress.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A680)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyse small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumours. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A555)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11676R-A647)
Supplier: Bioss
Description: UCH-L1 is a member of a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to generate the ubiquitin monomer. Expression of UCH-L1 is highly specific to neurons and to cells of the diffuse neuroendocrine system and their tumors. UCH-L1 is expressed in brain neurons. Examination of specific brain regions reveals expression in all areas tested, particularly in the substantia nigra. UCH-L1 represents 1 to 2% of total soluble brain protein. Its occurrence in Lewy bodies and its function in the proteasome pathway make it a compelling candidate gene in Parkinson disease. The gene which encodes UCH-L1 maps to human chromosome 4p14. The 230 amino acid human UCH-L3 protein is 54% identical to that of UCH-L1. UCH-L3 is the predominant thiol protease and has high-affinity binding sites for ubiquitin.
UOM: 1 * 100 µl


Supplier: Apollo Scientific
Description: Diethylene glycol monobenzyl ether 98%

Catalog Number: (BOSSBS-8300R-A647)
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.
UOM: 1 * 100 µl


Supplier: Thermo Fisher Scientific
Description: An azido containing reagent with PEG spacer and sulfhydryl reactivity. The compound is not stable upon prolonged storage and is sold as a kit.
Catalog Number: (BOSSBS-8300R-A680)
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 oxidised 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 oxidised 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 oxidised Prx can be reduced back to the active form during recovery after oxidative stress.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8300R-A488)
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.
UOM: 1 * 100 µl


Catalog Number: (8.14037.0025)
Supplier: Merck
Description: 4,6-Diaminopyrimidine-2-thiol for synthesis, Sigma-Aldrich®
UOM: 1 * 25 g

MSDS


Supplier: ENZO LIFE SCIENCES
Description: The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins involved in the processing and maturation of secretory proteins in the ER by catalyzing the rearrangement of disulphide bonds. PDI, an abundant protein of the ER (>400uM), contains a carboxy-terminal retention signal sequence, KDEL, similar to that of BiP and Grp94. The PDI proteins are characterized by the presence of one or more domains of ~95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing - and one domain lacking - a redox-active-Cys-X-X-Cys-tetrapeptide. In addition to roles as redox catalysts and isomerases, PDI proteins perform such functions as peptide binding and cell adhesion, and may conduct chaperone activities. Platelet surface thiols and disulphides play an important role in platelet responses. Catalytically active PDI resides on platelet surfaces where it mediates platelet aggregation and secretion by reducing disulfide bonds, thus exposing fibrinogen receptors in platelets.

Supplier: AAT BIOQUEST
Description: Psoralen-PEG3-Biotin is a photoactivatable reagent for biotinylating DNA or RNA.

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