proBNP Positive Control is synthetically produced from the sequence and is suitable for use in western blot applications.
Applications
WB
Note
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Product Properties
Dilution Range
WB: 1:500
Formulation
Provided as 100 uL ready-to-use, in SDS-PAGE sample buffer (Laemelli's buffer) containing Tris, pH 6.8, 1 % SDS, Glycerol and Bromophenolblue blue as tracking dye. The sample is reduced by adding 2% beta mercaptoethanol. The protein concentration is
Storage Instruction
Store at-20°C for long term storage. Avoid freeze-thaw cycles.
Brain natriuretic peptide 32: Detected in the cardiac atria (at protein level). Detected in the kidney distal tubular cells (at protein level).
Post Translational Modifications
The precursor molecule is proteolytically cleaved by the endoproteases FURIN or CORIN at Arg-102 to produce brain natriuretic peptide 32 and NT-proBNP. This likely occurs after it has been secreted into the blood, either during circulation or in the target cells. CORIN also cleaves the precursor molecule at additional residues including Arg-99 and possibly Lys-105. In patients with heart failure, processing and degradation of natriuretic peptides B occurs but is delayed, possibly due to a decrease in enzyme level or activity of CORIN and DPP4. Brain natriuretic peptide 32: Undergoes further proteolytic cleavage by various proteases such as DPP4, MME and possibly FAP, to give rise to a variety of shorter peptides. Cleaved at Pro-104 by the prolyl endopeptidase FAP (seprase) activity (in vitro). Degraded by IDE. During IDE degradation, the resulting products initially increase the activation of NPR1 and can also stimulate NPR2 to produce cGMP before the fragments are completely degraded and inactivated by IDE (in vitro). O-glycosylated on at least seven residues. In cardiomyocytes, glycosylation at Thr-97 is essential for the stability and processing of the extracellular natriuretic peptides B. Glycosylation, especially at Thr-97, may also be important for brain natriuretic peptide 32 stability and/or extracellular distribution. Glycosylation at Thr-97 appears to inhibit FURIN- or CORIN-mediated proteolytic processing, at least in HEK293 cells.
Function
Brain natriuretic peptide 32: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis. May also function as a paracrine antifibrotic factor in the heart. Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses. Involved in regulating the extracellular fluid volume and maintaining the fluid-electrolyte balance through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. Binds the clearance receptor NPR3. NT-proBNP: May affect cardio-renal homeostasis. Able to promote the production of cGMP although its potency is very low compared to brain natriuretic peptide 32. BNP(3-32): May have a role in cardio-renal homeostasis. Able to promote the production of cGMP.
