Amyloid-? (1-8, A2V) Peptide
Amyloid-? (1-8, A2V) Peptide
Amyloid-? (1-8, A2V) is a truncated form of amyloid-? (A?) that contains a valine to alanine substitution at position 2...
€114.00
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€166.00 €141.10
€166.00 €141.10
FMS-related tyrosine kinase 3 ligand (FLT3L) is a type I transmembrane protein that regulates hematopoietic stem and progenitor cell proliferation, differentiation, and survival.{52578} It is composed of an N-terminal signaling peptide and extracellular cytokine domain, a transmembrane domain, and a cytosolic tail.{52579} Soluble FLT3L is formed by proteolytic cleavage of membrane-bound FLT3L at the transmembrane domain or alternative splicing. Both membrane-bound and soluble FLT3L homodimerize and bind to FLT3 to induce ligand-dependent intracellular signaling and are expressed mainly by bone marrow stroma cells.{52579,52578} FLT3L synergizes with IL-7 to enhance B-lymphopoiesis and promotes IL-12-induced T cell production.{52577} It also acts on myeloid progenitor cells to induce proliferation of granulocytes and monocytes and increases the number of functional dendritic cells in a manner dependent on the presence of other growth factors such as GM-CSF (Item No. 32044), M-CSF, and IL-3. Flt3l knockdown induces hematopoietic developmental defects in mice. FLT3L induces proliferation and prevents apoptosis of acute myeloid leukemia cells in vitro. Cayman’s Soluble FLT3 Ligand (human, recombinant) protein can be used for cell-based assay applications. This protein consists of 175 amino acids and has a calculated molecular weight of 20.2 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is 27 kDa due to glycosylation.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 1 mg, 10 µg, 50 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | |
| Custom code | 3504.00 |
| Formulation | Lyophilized from sterile 20 mM Tris, 500 mM sodium chloride, pH 7.4 |
| Purity | ≥95% as determined by SDS-PAGE |
| UNSPSC code | 12352204 |
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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