NPPA Human
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
Greater than 95.0% as determined by SDS-PAGE.
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Description
NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).
Product Specs
Natriuretic Peptide A (NPPA) belongs to the natriuretic peptide family and plays a crucial role in maintaining cardiovascular balance. It achieves this by regulating processes such as natriuresis (sodium excretion), diuresis (urine production), and vasodilation (widening of blood vessels). NPPA is initially synthesized as a large precursor molecule. This precursor undergoes cleavage to release two peptides: one from the N-terminus, resembling vasoactive peptide and cardiodilatin, and another from the C-terminus, exhibiting natriuretic and diuretic properties. During pregnancy, NPPA contributes to the proper development of the placenta by facilitating trophoblast invasion and the remodeling of spiral arteries within the uterus.
Recombinant human NPPA, expressed in E. coli, is a single-chain polypeptide without any glycosylation modifications. It consists of 106 amino acids, encompassing the sequence from position 26 to 123, and includes an 8-amino acid histidine tag attached to the N-terminus. The calculated molecular weight of this protein is 11.7 kDa.
The NPPA protein undergoes filtration (using a 0.4 μm filter) and is subsequently lyophilized. The lyophilization process starts with a protein concentration of 0.5 mg/ml in a buffer solution containing 20 mM Tris, 50 mM NaCl, and 5% w/v trehalose, at a pH of 7.5.
To prepare a working solution, it is advised to add deionized water to the lyophilized powder, aiming for a final concentration of about 0.5 mg/ml. Ensure complete dissolution of the pellet before use. It is important to note that this NPPA product is not sterile. Prior to any cell culture applications, it is mandatory to filter the reconstituted protein through a sterile filter with an appropriate pore size.
The purity of this protein is determined to be greater than 95.0% based on SDS-PAGE analysis.
Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.
MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.
Product Science Overview
Natriuretic Peptide A, also known as Atrial Natriuretic Peptide (ANP), is a member of the natriuretic peptide family, which plays a crucial role in cardiovascular homeostasis. ANP is primarily synthesized and secreted by the cardiac atria in response to atrial stretch and increased blood volume. The peptide exerts its effects by binding to specific receptors, leading to natriuresis, diuresis, and vasodilation, thereby regulating blood pressure and fluid balance .
ANP was first discovered in the early 1980s when researchers identified a peptide with potent natriuretic and diuretic properties in the atrial tissue of rats. The human form of ANP is a 28-amino acid peptide derived from a larger precursor molecule, pro-ANP. The active peptide is generated through proteolytic cleavage of the precursor .
ANP plays a significant role in the regulation of blood pressure and fluid homeostasis. It promotes the excretion of sodium and water by the kidneys, reduces blood volume, and causes vasodilation. These actions collectively help to lower blood pressure and reduce the workload on the heart. ANP also inhibits the renin-angiotensin-aldosterone system (RAAS) and sympathetic nervous system, further contributing to its antihypertensive effects .
Due to its therapeutic potential, recombinant human ANP has been developed for clinical use. Recombinant ANP is produced using genetic engineering techniques, where the gene encoding human ANP is inserted into a suitable expression system, such as bacteria or yeast. The recombinant peptide is then purified and formulated for therapeutic applications .
Recombinant human ANP has been investigated for its potential use in treating various cardiovascular conditions, including heart failure and hypertension. Clinical studies have shown that ANP can improve hemodynamic parameters, enhance renal function, and reduce symptoms in patients with acute decompensated heart failure. Additionally, ANP has been explored as a biomarker for diagnosing and monitoring heart failure .
Despite its promising therapeutic potential, the clinical use of recombinant ANP faces several challenges. One major issue is its short half-life, which necessitates continuous infusion for sustained therapeutic effects. Researchers are exploring various strategies to overcome this limitation, including the development of ANP analogs with longer half-lives and the use of drug delivery systems to enhance its stability and bioavailability .
In conclusion, Natriuretic Peptide A (Human Recombinant) represents a significant advancement in the field of cardiovascular therapeutics. Its ability to regulate blood pressure and fluid balance makes it a valuable tool in the management of heart failure and hypertension. Ongoing research and development efforts aim to optimize its clinical use and expand its therapeutic applications.
