FABP3 Blocking Peptide
FABP3 Blocking Peptide
To be used in conjunction with Cayman’s FABP3 polyclonal antibody (Catalog No. 10233) to block protein-antibody complex formation during immunochemical...
€199.00
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€615.00 €522.75
€615.00 €522.75
SMAD4, also known as deleted in pancreatic carcinoma locus 4 (DPC4), is a tumor suppressor and a signal transduction protein that functions as a central mediator of the TGF-? and bone morphogenic protein (BMP) signaling pathways.{59633,59634} It is comprised of an N-terminal MH1 domain that binds DNA, a linker region containing a C-terminal SMAD activation domain essential to SMAD4 transcriptional activity, and a C-terminal MH2 domain that interacts with the MH1 domain of other SMAD proteins to facilitate homo- and heterodimerization.{59634} SMAD4 is ubiquitously expressed and localized to both the nucleus and cytosol.{59633} Upon TGF-? or BMP receptor activation, SMAD4 forms complexes with phosphorylated SMAD2 and SMAD3 or SMAD1, SMAD5, and SMAD8, respectively, which are translocated to the nucleus to induce cell cycle arrest and apoptosis.{59634} Homozygous deletion of, or intragenic inactivation mutations in, SMAD4 have been found in pancreatic and colorectal cancers. Heterozygous mutations in SMAD4 have been found in approximately 20% of patients with juvenile polyposis syndrome and are positively correlated with manifestation of hereditary hemorrhagic telangiectasia.{59635} Cayman’s SMAD4 (C-Term) Rabbit Monoclonal Antibody can be used for immunohistochemistry (IHC) and 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 from the C-terminal region of human SMAD4 |
| Clone | RM277 |
| Isotype | IgG |
| Application(s) | IHC, 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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