17 件の結果
UniHRV 3C Protease
カタログ番号:
パッケージ:500 U / Customized package
説明:UniHRV 3C Protease is a recombinant form of the 3C protease derived from human rhinovirus 14 expressed in E. coli (specific activity 1800-2000 U/mg). This product is a highly purified recombinant 6XHis-fusion protein and requires neither metal nor cofactors for activity. UniHRV 3C Protease recognizes the cleavage site: Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP). UniHRV 3C Protease demonstrate excellent cleavage efficiency in a variety of fusion proteins.
発現系:Escherichia coli
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Glycerol-free
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Carrier-free
HRV 3C Protease
カタログ番号:
パッケージ:1,000 U / 10,000 U / Customized package
説明:HRV 3C Protease is a recombinant form of the 3C protease derived from human rhinovirus 14 expressed in E. coli (specific activity 1800-2000 U/mg). This product is a highly purified recombinant 6XHis-fusion protein. This protease requires neither metal nor cofactors for activity. HRV 3C Protease recognizes the cleavage site: Leu-Glu-Val-Leu-Phe-Gln↓Gly-Pro (LEVLFQ↓GP).
発現系:Escherichia coli
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Glycerol-free
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Carrier-free
LeadGMP® PNGase F
カタログ番号:
パッケージ:15 KU / 75 KU / Customized package
説明:PNGase F is an enzyme used in biochemistry and molecular biology to remove N-linked glycans from glycoproteins. By using PNGase F, researchers can enzymatically cleave between these sugar chains and asparagine residues of glycoproteins, allowing for the study of protein structure and function, particularly in glycosylation research.
発現系:Escherichia coli
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Animal-free
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Glycerol-free
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Carrier-free
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Low Endotoxin
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GMP-grade
LeadGMP® T7 RNA Polymerase
カタログ番号:
パッケージ:25,000 U / 200,000 U / 2,000,000 U / Customized package
説明:Bacteriophage T7 RNA Polymerase is a DNA-dependent RNA polymerase with high specificity for the T7 promoter. This enzyme catalyzes the 5’→3’ synthesis of RNA from DNA downstream from its promoter.
発現系:Escherichia coli
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Carrier-free
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GMP-grade
PNGase F
カタログ番号:
パッケージ:15 KU / 75 KU / Customized package
説明:PNGase F is an enzyme used in biochemistry and molecular biology to remove N-linked glycans from glycoproteins. By using PNGase F, researchers can enzymatically cleave between these sugar chains and asparagine residues of glycoproteins, allowing for the study of protein structure and function, particularly in glycosylation research.
発現系:Escherichia coli
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Glycerol-free
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Carrier-free
SUMO-Specific Protease 2 (SENP2)
カタログ番号:
パッケージ:100 μg / 1 mg / Customized package
説明:SENP2 is an enzyme that belongs to the protease family C48. Structurally, SENP2 harbors the C48 catalytic domain which is typically located close to the C terminus and has been reported to engage two SUMO pathways. The first is cleavage processing of small ubiquitin-like modifiers (SUMO1, SUMO2, and SUMO3) propeptides, subsequently leading to protein maturation. The second is the cleavage processing of SUMO1, SUMO2, and SUMO3 from targeted proteins. SENP2 protease has a His-tag for easy removal from a cleavage reaction by using nickel affinity resins.
発現系:Escherichia coli
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Glycerol-free
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Carrier-free
LEADSPHERE® Proteinase K
カタログ番号:
パッケージ:50 tablets / Customized package
説明:Proteinase K is a non-specific serine protease that belongs to the subtilisin family with an active site catalytic triad Asp39-His69-Ser224. It is useful for the general digestion of peptide bonds, consequently used in broad applications in the biology experiments such as isolation of genomic DNA and plasmid, isolation of RNA, inactivation of RNases, DNases, and enzymes in reactions. LEADSPHERE® Proteinase K sphere is competent in the digestion of samples in 300-400 μL, such as saliva. In addition, LEADSPHERE® Proteinase K is generated with an ISO13485 quality management system specifically for medical devices.
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Glycerol-free
SUMO Protease (ULP1) (Active)
カタログ番号:
パッケージ:2,500 U / Customized package
説明:SUMO Protease (ULP1, Ubiquitin-like-specific protease 1) is a highly active cysteine protease derived from Saccharomyces cerevisiae. It has often been used as a biotechnological tool for cleavage affinity purification tags such as ubiquitinlike (UBL) protein, and SUMO from fusion proteins. ULP1 protease specifically recognizes the tertiary structure of SUMO rather than an amino acid sequence. ULP1 protease has a His-tag for easy removal from a cleavage reaction by using nickel affinity resins. Notably, the cleavage reactions are available in a buffer containing 2 M urea.
発現系:Escherichia coli
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Glycerol-free
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Carrier-free

