SMN tudor domain (human recombin

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SMN tudor domain (human recombinant)

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Cat No: 14136

Proteins - More Proteins

Tudor domains are small protein structural motifs of ~50 amino acids related to the “Royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains.{22297,22331} Tudor domains occur either alone, in tandem, or with oth...

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Territorial Availability: Available through Bertin Technologies only in France

Correlated keywords:

methyl readers royal families post-translational modifications epigenetics cancers proteins tudors recombinant SMNs chromo MBT PWWP agenet-like exon 7 muscular atrophy SMN1 SMN-1 SMN2 SMN-2 SMNC SMN-C SMNT SMN-T

Product Overview:
Tudor domains are small protein structural motifs of ~50 amino acids related to the “Royal family” of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains.{22297,22331} Tudor domains occur either alone, in tandem, or with other domains and are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification and chromatin remodeling.{22332} The tudor domains recognize symmetric methylated arginine or methylated lysine residues.{18035,22333,22334,22335} The Survival of Motor Neurons (SMN) protein participates in RNA splicing. The Tudor domain of SMN recognizes and binds methylated Sm proteins, which bind small nuclear RNA.{22324} SMN is encoded in humans by two separate genes, SMN1 and SMN2, which differ by one base in exon 7. In motor neuron cells, approximately 90% of the SMN2 transcripts are spliced to exclude exon 7.{22322} The SMN2 transcripts without exon 7 are less stable than SMN1 transcripts.{22418} Consequently, defects in human SMN1 result in the death of motor neuron cells and spinal muscular atrophy, which is the leading genetic cause of infantile death. This protein product contains the tudor domain region of SMN. The sequence of this region is identical in both the SMN1 and the SMN2 genes.

Size	100 µg
Shipping	dry ice
Formulation	50 mM Tris-HCl, with 150 mM sodium chloride, pH 8.0, containing 20% glycerol
Purity	≥90% estimated by SDS-PAGE
Custom Code	3504.00
UNSPSC code	12352204

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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/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.