Human NPR1 protein
Recombinant protein from the full-length sequence of homo sapiens natriuretic peptide receptor 1 (NPR1) (NM_000906), with a His tag.
ANPa; ANPRA; GUC2A; GUCY2A; NPRA
>90% by SDS-PAGE gel and Coomassie Blue staining
Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only!
Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives
Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg)
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]
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