Background:

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]

Specificity:

natriuretic peptide receptor 1

Alternative names:

ANPa; ANPRA; GUC2A; GUCY2A; NPRA

Species reactivity:

Human, Mouse, Rat

Host:

Mouse

Ig type:

PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Immunogen:

Human recombinant protein fragment corresponding to amino acids 746-1006 of human NPR1 (NP_000897) produced in E.coli.

Purification & Purity:

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

Molecular weight:

118.7 kDa(Predicted)

Applications:

WB

Usage:

WB 1:2000

Storage:

PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Precautions:

For research use only, not for use in diagnostic procedure.

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