Recombinant Human PDE9A Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3702

Recombinant Human PDE9A Protein (His & GST Tag)

Beta LifeScience SKU/CAT #: BLPSN-3702
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His&GST
Host Species Human
Accession O76083
Synonym HSPDE9A2
Background High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A, also known as PDE9A, is a member of the cyclic nucleotide phosphodiesterase family and PDE9 subfamily. PDE9A is expressed in all tissues examined (testis, brain, small intestine, skeletal muscle, heart, lung, thymus, spleen, placenta, kidney, liver, pancreas, ovary and prostate) except blood. Highest levels of PDE9A is in brain, heart, kidney, spleen, prostate and colon. IsoformPDE9A12is found in prostate. PDE9A mRNA is widely distributed throughout the rat and mouse brain, with the highest expression observed in cerebellar Purkinje cells.PDE9A is the only cGMP-specific PDE with significant expression in the forebrain, and as such is likely to play an important role in NO-cGMP signaling. PDE9A is highly conserved between species and is widely distributed throughout the rodent brain. PDE9A is probably involved in maintenance of low cGMP levels in cells and might play an important role in a variety of brain functions involving cGMP-mediated signal transduction. PDE9A hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. PDE9A represents a novel drug target worthy of further study.
Description A DNA sequence encoding the full length of human PDE9A (O76083-2) (Met 1-Ala 533) was fused with the N-terminal His-tagged GST tag at the N-terminus.
Source Baculovirus-Insect Cells
Predicted N Terminal Met
AA Sequence Met 1-Ala 533
Molecular Weight The recombinant human PDE9A consisting of 770 a.a. and has a calculated molecular mass of 89.5 kDa. It migrates as an approximately 75 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile 20mM Tris, 500mM NaCl, 5mM GSH, pH 7.4, 10% gly.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart. Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory.
Subcellular Location [Isoform PDE9A1]: Cell projection, ruffle membrane. Cytoplasm, perinuclear region. Golgi apparatus. Endoplasmic reticulum. Cell membrane, sarcolemma.; [Isoform PDE9A2]: Cell projection, ruffle membrane. Cytoplasm, perinuclear region.; [Isoform PDE9A3]: Cytoplasm. Endoplasmic reticulum.; [Isoform PDE9A17]: Cytoplasm. Endoplasmic reticulum.
Protein Families Cyclic nucleotide phosphodiesterase family, PDE9 subfamily
Database References
Tissue Specificity Expressed in all tissues examined (testis, brain, small intestine, skeletal muscle, heart, lung, thymus, spleen, placenta, kidney, liver, pancreas, ovary and prostate) except blood. Highest levels in brain, heart, kidney, spleen, prostate and colon. Isofo

Gene Functions References

  1. PDE9A can regulate cGMP signalling independent of the nitric oxide pathway, and its role in stress-induced heart disease suggests potential as a therapeutic target. PMID: 25799991
  2. it is concluded that assessment of PDE5 and PDE9 expression may be useful in the differential diagnosis of benign and malignant breast disease and successful treatment of breast cancer PMID: 22960860
  3. In vivo effects of PDE9A inhibition included reversal of the respective disruptions of working memory. PMID: 22328573
  4. PDE9 is widely distributed in the urothelial epithelium of the human lower urinary tract and its potential roles may be different from those of PDE5. PMID: 21736695
  5. Data show that PDE9A inhibitor, BAY-73-6691, significantly reduced basal and sickle cell (SCA) neutrophil adhesion; this was accompanied by decreased SCA neutrophil surface expressions of the L-selectin and CD11b adhesion molecules. PMID: 21336703
  6. Identification and distribution of different variants produced by differential splicing of phosphodiesterase 9A mRNA. PMID: 12565835
  7. X ray crystallography with IBMX inhibitor binding PMID: 15210993
  8. The data suggests the utilization of two different start codons to produce a variety of different PDE9A proteins, allowing specific subcellular location of PDE9A splice variants. PMID: 17090334
  9. PDE9A, is unlikely to play an important role in antidepressant outcome in this sample PMID: 19214142

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed