SIRT5 (human, recombinant)
SIRT5 (human, recombinant)
Sirtuin 5 (SIRT5) is an enzyme that catalyzes the NAD-dependent removal of malonyl, succinyl, and glutaryl groups from target proteins.{55107,55108}...
€724.00
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€590.00 €501.50
€590.00 €501.50
STAT1, also known as STAT1?, is a transcription factor and member of the STAT protein family with roles in innate and adaptive immunity.{53705} It is composed of an N-terminal domain that is essential to protein-protein interactions and dimerization, a DNA binding domain that facilitates nuclear import and export, as well as DNA binding, a linker domain, tail segment, and a transactivation domain that facilitates transcription of target genes.{53706} STAT1? is an isoform of STAT1 that is formed by alternative splicing and lacks the 38-amino acid transactivation domain.{53707} Upon phosphorylation by JAKs, STAT1 dimerizes and is translocated to the nucleus to activate transcription of IFN-?-inducible genes.{53708} Because the C-terminal transactivation domain is required for STAT1 interaction with the transcriptional coactivator CREB-binding protein (CBP)/p300 and gene transcription, STAT1? is considered a dominant-negative regulator of STAT1 and overexpression of STAT1? inhibits IFN-?-induced gene expression in RAW 264.7 cells. STAT1? phosphorylation is increased and IFN-?-induced JAK1, JAK2, and STAT1 activation is decreased in RAW 264.6 cells infected with L. major and L. mexicana parasites, as well as M. avium bacteria.{53708,53709} STAT1? protein levels are reduced in patient-derived esophageal squamous cell carcinoma (ESCC) tumor samples and are positively correlated with lymph node metastasis, invasion, and shorter overall survival.{53707} Cayman’s STAT1? (human, recombinant) protein consists of 950 amino acids and has a calculated molecular weight of 111 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 150 mM sodium chloride |
| Purity | ≥92% 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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