€604.00 €513.40
Protein arginine deiminase 6 (PAD6) is a homodimeric guanidine-modifying enzyme belonging to the amidinotransferase superfamily.{34555} It is a calcium-dependent enzyme that catalyzes the post-translational modification of target proteins by converting arginine to citrulline. PAD6 is expressed in mammalian oocytes, sperm cells, and early embryos.{39678} In mammalian oocytes and early embryo cytoplasm, its expression is localized to cytoskeletal sheets, dynamic structures containing various keratins, which are major targets for citrullination. PAD6-/- oocytes exhibit reduced microtubule acetylation and defective organelle positioning and redistribution, suggesting a role for PAD6 in regulating microtubule-mediated organelle movement and positioning.{39677} PAD6-/- female, but not male, mice are infertile due to a reduction of de novo protein synthesis, cytoskeletal sheet formation, and ribosomal RNA which induces arrest of zygote development at the two-cell stage.{39678,39679} PAD6 is regulated by newborn ovary homeobox (Nobox), as its promoter contains a Nobox DNA-binding element (NBE) and expression and activity of PAD6 are decreased in Nobox-/- mouse ovaries.{39676} In human females, homozygous nonsense mutations and compound-heterozygous mutations in PAD6 induce early embryonic arrest following in vitro fertilization (IVF) or intracytoplasmic sperm injection (ICSI).{39680} Cayman’s PAD6 monoclonal antibody (Clone 4B7) can be used for Western blot and ELISA applications. The antibody recognizes PAD6 at ~77 kDa from human samples.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Host | Mouse |
| Antigen | Full-length human recombinant PAD6 protein |
| Clone | 4B7 |
| Isotype | IgG1 |
| Application(s) | ELISA, WB |
| Formulation | 100 µg of protein G-purified monoclonal antibody |
| Custom code | 3822.19 |
| UNSPSC code | 12352203 |
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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