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NPR1
Anti-NPR1 Recombinant Antibody Products
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- Target: NPR1
- Host Animal: Human
- Application: ELISA, FC, Cell-uptake
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For Research Use Only. Not For Clinical Use.
Guanylyl cyclases, catalyzing the production of cGMP from GTP, are classified as soluble and membrane forms (Garbers and Lowe, 1994 [PubMed 7982997]). The membrane guanylyl cyclases, often termed guanylyl cyclases A through F, form a family of cell-surface receptors with a similar topographic structure: an extracellular ligand-binding domain, a single membrane-spanning domain, and an intracellular region that contains a protein kinase-like domain and a cyclase catalytic domain. GC-A and GC-B function as receptors for natriuretic peptides; they are also referred to as atrial natriuretic peptide receptor A (NPR1) and type B (NPR2; MIM 108961). Also see NPR3 (MIM 108962), which encodes a protein with only the ligand-binding transmembrane and 37-amino acid cytoplasmic domains. NPR1 is a membrane-bound guanylate cyclase that serves as the receptor for both atrial and brain natriuretic peptides (ANP (MIM 108780) and BNP (MIM 600295), respectively).[supplied by OMIM, May 2009]
Protein class
Enzymes, FDA approved drug targets, Metabolic proteins, Transporters
Predicted location
Membrane
Single cell type specificity
Group enriched (Hepatic stellate cells, Adipocytes, Endothelial cells)
Immune cell specificity
Not detected in immune cells
Cell line specificity
Cell line enriched (ASC diff)
Interaction
Homodimer.
Molecular function
Lyase, Receptor, Vasoactive
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