Confirm delete?

Bertin Bioreagent
logo
All categories
Contact Us
You are here :

PDE9A2 (human, recombinant)

  • Zoom
    PDE9A2 (human, recombinant)
  • PDE9A2 (human, recombinant)
Cat No: 32039
Proteins - Enzymes
Cayman

Phosphodiesterase 9A (PDE9A) is a high-affinity cGMP-specific cyclic nucleotide phosphodiesterase.{53752} Alternative splicing in the 5' region of PDE9A mRNA results in a variety of PDE9A isoforms, including PDE9A2, whereas the 3' region encoding the ...

More
: 100 µg

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • PDE-9A 9 A2 9A2 COS1 HSPDE9A2 HSPDE9A2
Product Overview:
Phosphodiesterase 9A (PDE9A) is a high-affinity cGMP-specific cyclic nucleotide phosphodiesterase.{53752} Alternative splicing in the 5' region of PDE9A mRNA results in a variety of PDE9A isoforms, including PDE9A2, whereas the 3' region encoding the catalytic PDE domain does not vary between isoforms.{53750,53753} PDE9A2 mRNA is expressed in colon, prostate, spleen, peripheral blood leukocytes, small intestine, thymus, testis, and ovary.{53750} PDE9A2 localizes to membrane ruffles, the perinuclear region, and other membrane regions when transiently overexpressed in HeLa and COS-1 cells.{53753} PDE9A expression is elevated in reticulocytes and neutrophils isolated from patients with sickle cell disease compared with healthy individuals.{53751} Cayman's PDE9A2 (human, recombinant) protein consists of 770 amino acids and has a calculated molecular weight of 89.5 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 75 kDa.
Size 100 µg
Shipping dry ice
Formulation Lyophilized from sterile 20 mM Tris, pH 7.4, with 500 mM sodium chloride, 5 mM GSH, and 10% glycerol
Purity ≥90% estimated by SDS-PAGE
Custom Code 3504.00
UNSPSC code 12352204

Click here to ask for your quote and get 15% off Cayman's products.

 

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.

Search