(+)-D-threo–PDMP (hydrochloride)
(+)-D-threo–PDMP (hydrochloride)
(+)-D-threo-PDMP is a ceramide analog and is one of the four possible stereoisomers of PDMP (Item No. 62595).{11392} (+)-D-threo-PDMP is...
€707.00
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€365.00 €310.25
€365.00 €310.25
Heat shock protein 70s (Hsp70s) are abundant and stress-inducible 70 kDa molecular chaperone proteins encoded by a highly conserved, multigene family.{15480} They are monomeric proteins that can be divided into two functional domains: an N-terminal ATPase domain and a substrate binding domain that contains a highly conserved EEVD motif at its C-terminus. Hsp70s are found in the cytosol, nuclei, endoplasmic reticulum, mitochondria, and chloroplasts of eukaryotes, as well as in bacteria. They function as molecular chaperones that assist in a wide range of cellular processes, including refolding of aggregated or misfolded proteins, co- and post-translational folding and assembly of nascent peptides, membrane translocation of secretory and organellar proteins, controlling activity of regulatory nuclear receptors, kinases and transcription factors, as well as acting cooperatively with the Hsp90 chaperone system in eukaryotes.{36132} The Hsp70 chaperone cycle is ATP-dependent and initiated by transient interaction of the Hsp70 substrate binding domain with hydrophobic regions within a peptide or protein. It consists of an alteration between the low-affinity ATP-bound state with fast rates of substrate exchange and the high-affinity ADP bound state with slow rates of substrate exchange. Hsp70s are subject to a variety of post-translational modifications and their expression is upregulated under conditions of cellular stress and in a variety of disease states.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 50 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Formulation | 50 mM HEPES pH 8.0, 150 mM sodium chloride, 1 mM DTT, 10% glycerol |
| Purity | ≥90% as 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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