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FEN1 (human, recombinant)

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    FEN1 (human, recombinant)
  • FEN1 (human, recombinant)
Cat No: 14199
Proteins - Enzymes
Cayman

Flap endonuclease 1 (FEN1), a RAD2 Class II nuclease, plays a crucial role in DNA repair, replication, and genomic stability.{28481} FEN1 removes the 5'-unannealed flap during Okazaki fragment processing in lagging strand DNA synthesis.{28483} Removal...

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: 100 µg

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • endonuclease nuclease DNA damage repair replication protein enzyme activity recombinant flap FEN-1 RAD2 class II 2 genomic stability 5’-unannealed flap Okazaki fragment lagging strand synthesis long-patch base excision regulation recombination yeast UV radiation ultraviolet chromosome segregation cell cycle arrest S phase haploinsufficiency haploinsufficient tumor progression overexpressed overexpression cancer lung gastric prostate pancreatic brain breast DNase IV DNaseIV structure specific 1 Maturation factor MF1
Product Overview:
Flap endonuclease 1 (FEN1), a RAD2 Class II nuclease, plays a crucial role in DNA repair, replication, and genomic stability.{28481} FEN1 removes the 5'-unannealed flap during Okazaki fragment processing in lagging strand DNA synthesis.{28483} Removal of the DNA flap is also critical in long-patch base excision repair and regulation of recombination.{22126} In yeast, FEN1 mutants display sensitivity to UV irradiation, deficient chromosome segregation, and cell cycle arrest in S phase.{28482} Furthermore, haploinsufficiency of FEN1 in mice leads to rapid tumor progression.{28482} FEN1 is overexpressed in many forms of cancer, including lung, gastric, prostate, pancreatic, brain, and breast.{22126}
Size 100 µg
Shipping dry ice
Formulation 50 mM Tris, pH 8.0, containing 1 mM DTT and 10% glycerol
Purity ≥85% estimated by SDS-PAGE
Custom Code 3504.00
UNSPSC code 12352204

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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