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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€505.00 €429.25
€505.00 €429.25
Kelch-like ECH-associated protein 1 (Keap1) is a substrate adapter protein in the Kelch-like (KLHL) family of proteins.{55226} It contains an N-terminal region, a BTB/POZ domain that facilitates protein binding and Keap1 dimerization, a central intervening region (IVR), a double glycine repeat (DGR)/Kelch repeat domain, a BACK that binds to other proteins, and a C-terminal region.{55226,53741,53742} KEAP1 is ubiquitously expressed and localized to the perinuclear region of the cytosol and bound to the actin skeleton via its DGR region.{53743,53744,53745} Under homeostatic conditions, it associates with Nrf2, preventing its nuclear translocation and promoting its ubiquitination and proteasomal degradation.{53741,53745} In the presence of electrophiles or oxidants, Keap1 releases Nrf2, which translocates to the nucleus to induce the expression of cytoprotective genes.{53745} Somatic mutations in Keap1 have been found in various cancers and human cancer cell lines and are associated with loss of Keap1 function and constitutive activation of Nrf2, which contributes to tumor growth and chemoresistance.{53742} Cayman’s Keap1 (human, recombinant) protein is comprised of Keap1 (amino acids 2-264) fused to His and GST tags at its N-terminus, consists of 860 amino acids, and has a calculated molecular weight of 97.37 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of this protein is approximately 109 kDa.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Formulation | Lyophilized from sterile 20 mM Tris, pH 7.4, with 500 mM sodium chloride and 10% glycerol |
| Purity | ≥85% estimated by SDS-PAGE |
| Custom code | 3504.00 |
| 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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