protein

Recombinant Human Atrial natriuretic peptide receptor 1

MBS963032

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Atrial natriuretic peptide receptor 1

Atrial natriuretic peptide receptor 1

Atrial natriuretic peptide receptor type A; ANP-A; ANPR-A; NPR-A; Guanylate cyclase A; GC-A

atrial natriuretic peptide receptor 1; Atrial natriuretic peptide receptor 1; atrial natriuretic peptide receptor 1; natriuretic peptide receptor 1; Atrial natriuretic peptide receptor type A; ANP-A; ANPR-A; NPR-A; Guanylate cyclase A; GC-A

NPR1

NPR1; NPR1; ANPa; NPRA; ANPRA; GUC2A; GUCY2A; ANPRA; ANP-A; ANPR-A; NPR-A; GC-A

ANPRA_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

33-473

1061

GNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPD
LLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNP
AVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVK
DEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAY
RPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSH
YTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGE
DYVFFHLDIFGQSLQGGQGPA

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cardiovascular

Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand.

Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction.Lowe D.G., Chang M.S., Hellmiss R., Chen E., Singh S., Garbers D.L., Goeddel D.V.EMBO J. 8:1377-1384(1989) Organization of the human natriuretic peptide receptor A gene.Takahashi Y., Nakayama T., Soma M., Izumi Y., Kanmatsuse K.Biochem. Biophys. Res. Commun. 246:736-739(1998) Identification of functional polymorphisms in noncoding regions of the human natriuretic peptide receptor A gene.Maeda N., Knowles J.W.NHLBI resequencing and genotyping service (RS&G) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006)

167830411

NP_000897.3

NM_000906.3

P16066

64.9kD

Aldosterone Synthesis And Secretion Pathway (1272485); Aldosterone Synthesis And Secretion Pathway (1285075); Cardiac Conduction Pathway (1339115); Muscle Contraction Pathway (1269868); Oxytocin Signaling Pathway (952859); Oxytocin Signaling Pathway (960764); Physiological Factors Pathway (1339122); Purine Metabolism Pathway (82944); Purine Metabolism Pathway (307); Regulation Of Lipolysis In Adipocytes Pathway (1222950)

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]

ANPA: natriuretic peptide receptor A, which mediates natriuretic, diuretic, and vasorelaxing actions of the natriuretic peptides. Contains five functional domains: an extracellular ligand-binding domain, a single membrane-spanning region, and intracellularly a protein kinase homology domain, a helical hinge region involved in oligomerization, and a carboxyl-terminal guanylyl cyclase catalytic domain. Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. Has guanylate cyclase activity on binding of ANF. Hypertensive SHR Rat has polymorphism at the locus. Human non-coding polymorphisms can alter expression up to two-fold, and have been associated with hypertension. A coding SNP is associated with hypertension and myocardial infarction. Protein type: Protein kinase, RGC; Guanylyl cyclase; Lyase; Membrane protein, integral; Nucleotide Metabolism - purine; EC 4.6.1.2; Protein kinase, dual-specificity (receptor); Receptor, misc.; Kinase, protein; RGC group; RGC family. Chromosomal Location of Human Ortholog: 1q21-q22. Cellular Component: guanylate cyclase complex, soluble; integral to plasma membrane; plasma membrane; receptor complex. Molecular Function: adenylate cyclase activity; ATP binding; GTP binding; guanylate cyclase activity; hormone binding; natriuretic peptide receptor activity; peptide hormone binding; peptide receptor activity, G-protein coupled; protein kinase activity; protein kinase binding. Biological Process: body fluid secretion; cell surface receptor linked signal transduction; cGMP biosynthetic process; dopamine metabolic process; G-protein coupled receptor protein signaling pathway; negative regulation of angiogenesis; negative regulation of cell growth; negative regulation of smooth muscle cell proliferation; positive regulation of cGMP biosynthetic process; protein amino acid phosphorylation; receptor guanylyl cyclase signaling pathway; regulation of blood pressure; regulation of vascular permeability; regulation of vasodilation

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750