€615.00 €522.75
Eukaryotic translation initiation factor 4E (eIF4E) is a component of the eIF4 complex that specifically binds to the methyl-7-guanosine cap structure at the 5’ end of eukaryotic mRNA to initiate translation.{25357,25363,41706} It is composed of an ?/? domain containing one short and three long ?-helices and an antiparallel ?-sheet.{25357} eIF4E is ubiquitously expressed and localized to the nucleus and cytoplasm.{62504} Nuclear eIF4E promotes export of mRNAs that contain the eIF4E sensitivity element (4E-SE) to the cytosol while cytosolic eIF4E, in a complex with eIF4A and eIF4G1/eIF4G3, mediates recruitment of mRNAs to the ribosome to initiate cap-dependent translation.{25357,41706} eIF14E activity is regulated by eIF4E-binding proteins (4E-BPs), which bind eIF4E to prevent eIF4 complex assembly and subsequent translation.{41706} Overexpression of eIF4E is observed in approximately 30% of human malignancies, including breast, colon, and head and neck carcinomas and acute myeloid leukemias, particularly myelomonocytic M4 and monocytic M5 subtypes, as well as prostate cancers.{41706,25358,25362} Increased eIF4E expression leads to increased translation of oncogenic mRNAs, such as those encoding VEGF and cyclin D1, and contributes to cancer cell survival and proliferation. Phosphorylation of eIF4E at serine 209 (Ser209) is associated with tumor progression and reduced survival in patients with malignant melanoma, and pharmacologic inhibition of eIF4E phosphorylation is selectively cytotoxic to cancer cells.{55659,55660} Cayman’s eIF4E (Phospho-Ser209) Rabbit Monoclonal Antibody can be used for Western blot (WB) applications.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µl |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Host | Rabbit |
| Antigen | Peptide corresponding to human eIF4E (phospho-Ser209) |
| Clone | RM452 |
| Isotype | IgG |
| Application(s) | WB |
| Formulation | 100 µl of protein A-affinity 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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