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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.
Catalog Number: BOSSBS-11676R-HRP
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-11676R-A488
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-11676R-A750
UOM: 1 * 100 µl
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: BOSSBS-8300R-A555
UOM: 1 * 100 µl
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: BOSSBS-8300R-FITC
UOM: 1 * 100 µl
Supplier: Bioss


Description: Azido-PEG3-sulphorhodamine 101 conjugate
Catalog Number: J65476.X0
UOM: 1 * 5 mg
Supplier: Thermo Fisher Scientific

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

MSDS


Description: Psoralen-PEG3-Biotin is a photoactivatable reagent for biotinylating DNA or RNA.
Catalog Number: AATB39051
UOM: 1 * 5 mg
Supplier: AAT BIOQUEST

New Product


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.
Catalog Number: BOSSBS-11676R-A680
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-11676R-A555
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-11676R-A647
UOM: 1 * 100 µl
Supplier: Bioss


Description: The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. Through the use of a wide range of enzymes that can add or remove ubiquitin, the Ub pathway controls many intracellular processes such as signal transduction, transcriptional activation and cell cycle progression. USP3 (ubiquitin specific peptidase 3), also known as UBP or SIH003, is a 520 amino acid protein that contains one UBP-type zinc finger and belongs to the peptidase C19 family. Expressed ubiquitously with highest levels present in pancreas, USP3 catalyzes the conversion of a ubiquitin C-terminal thioester to a free ubiquitin and a thiol. The gene encoding USP3 maps to human chromosome 15, which houses over 700 genes and comprises nearly 3% of the human genome.
Catalog Number: BOSSBS-4806R-HRP
UOM: 1 * 100 µl
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.
Catalog Number: BOSSBS-8300R-A680
UOM: 1 * 100 µl
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: BOSSBS-8300R-A488
UOM: 1 * 100 µl
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: BOSSBS-8300R-A647
UOM: 1 * 100 µl
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: BOSSBS-8300R-HRP
UOM: 1 * 100 µl
Supplier: Bioss


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