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...
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From €469.00 €398.65
Hsp90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more co-chaperones.{15726} One class of Hsp90-binding co-chaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an Hsp90 binding site. Among the TRP co-chaperones of Hsp90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins.{15727} FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex.{15728} The N-terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPlase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TRP repeats involved in protein-protein interactions with Hsp40.{15729} Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by the glucocorticoid receptor in opposing manners and have different Hsp90-binding characteristics.{15728,15730} Also, whereas FKBP51 typically has a role with the progesterone receptor, FKBP52 has been found to be linked to the progesterone, androgen, and glucocorticoid receptors.{15730}
Territorial Availability: Available through Bertin Technologies only in France
| Size | 100 µg, 25 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 52 |
| Antigen | synthetic peptide corresponding to the residues of human FKBP52 |
| Host | Mouse |
| Clone | clone Hi52c |
| Isotype | IgG1 |
| Custom code | 3822.19 |
| Application(s) | IHC (paraffin embeded sections), IP, WB |
| Formulation | Protein G-purified IgG at a concentration of 1 mg/ml in PBS buffer, containing 0.09% sodium azide and 50% glycerol |
| 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.
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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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