Territorial Availability: Available through Bertin Technologies only in France
- Correlated keywords
- DNA damages repairs BRCT domains phosphoserines binding phosphothreonines protein-protein protein-DNA interactions double strands breaks DSB non-homologous ends joining NHEJ ionizing radiation LIGs IV BRCT ligases 4 four BRCA1 C-terminal p53 binding proteins 53BP1 TP53BP1 RAD9 Xrcc4 non homologous LIG4 syndromes
- Product Overview:
DNA Ligase 4 (LIG4) is a large protein belonging to the ATP-dependent DNA ligase family.{24669} LIG4 contains two BRCA1 C-terminal (BRCT) domains. BRCT domains are modular units of ~100 amino acids that fold independently and recognize linear phosphoserine or phosphothreonine regions to mediate protein-protein and protein-DNA interactions.{23632,22097} BRCT domains were initially recognized in the C-terminal region of the breast cancer protein BRCA1, as well as the p53 binding protein and the yeast cell cycle checkpoint protein RAD9.{23633} BRCT domains often occur as tandem repeats at the C-terminal end of several proteins that are functionally diverse.{22097} Most BRCT domain-containing proteins participate in DNA-damage checkpoint control or DNA-repair pathways, or both.{23634,23633} Thus, BRCT domain-containing proteins likely participate in the cellular response to DNA damage. LIG4 forms a complex with the DNA repair protein Xrcc4 to play an essential role in DNA non-homologous end joining during DNA double-strand break repair and V(D)J recombination, which is the rearrangement of immunoglobulin and T-cell receptor genes.{24667,24668,24666} Cells lacking either of these proteins are hypersensitive to ionizing radiation. Mutations of the gene that encodes this protein results in an autosomal recessive disease called LIG4 syndrome, which is characterized by microcephaly, unusual facial features, growth retardation, developmental delay, skin anomalies, and is associated with pancytopenia (reduction of red blood cells, white blood cells, and platelets).{24670,24671} This protein product contains the tandem BRCT domain region of LIG4.
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.