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

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

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

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of NPR2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.

Cardiovascular

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

64.5kD

natriuretic peptide receptor 2

atrial natriuretic peptide receptor 2

Atrial natriuretic peptide receptor 2

ANPRB; ANP-B; ANPR-B; NPR-B; GC-B??[Similar Products]

ANPRB_HUMAN

This gene encodes natriuretic peptide receptor B, one of two integral membrane receptors for natriuretic peptides. Both NPR1 and NPR2 contain 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. The protein is the primary receptor for C-type natriuretic peptide (CNP), which upon ligand binding exhibits greatly increased guanylyl cyclase activity. Mutations in this gene are the cause of acromesomelic dysplasia Maroteaux type. [provided by RefSeq, Jul 2008]

ANPB: natriuretic peptide receptor B, one of two integral membrane receptors for 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. Is the primary receptor for C-type natriuretic peptide (CNP), which upon ligand binding exhibits greatly increased guanylyl cyclase activity. 21 mutations linked to acromesomelic dysplasia (skeletal malformation). 3 isoforms of the human protein are produced by alternative splicing.

Protein type: Kinase, protein; EC 4.6.1.2; Receptor, misc.; Protein kinase, dual-specificity (receptor); Nucleotide Metabolism - purine; Protein kinase, RGC; Lyase; Guanylyl cyclase; Membrane protein, integral; RGC group; RGC family

Chromosomal Location of Human Ortholog: 9p21-p12

Cellular Component: guanylate cyclase complex, soluble; integral to membrane; plasma membrane

Molecular Function: adenylate cyclase activity; ATP binding; GTP binding; guanylate cyclase activity; hormone binding; identical protein binding; natriuretic peptide receptor activity; peptide hormone binding; protein kinase activity; receptor activity; transmembrane receptor activity

Biological Process: cell surface receptor linked signal transduction; cGMP biosynthetic process; negative regulation of meiotic cell cycle; ossification; protein amino acid phosphorylation; receptor guanylyl cyclase signaling pathway; regulation of blood pressure; signal transduction

Disease: Acromesomelic Dysplasia, Maroteaux Type; Epiphyseal Chondrodysplasia, Miura Type; Short Stature With Nonspecific Skeletal Abnormalities

Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases.Chang M.S., Lowe D.G., Lewis M., Hellmiss R., Chen E., Goeddel D.V.Nature 341:68-72(1989) Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension.Rehemudula D., Nakayama T., Soma M., Takahashi Y., Uwabo J., Sato M., Izumi Y., Kanmatsuse K., Ozawa Y.Circ. Res. 84:605-610(1999) cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides molecular and functional studies in human proximal tubule cells.Hirsch J.R., Meyer M., Maegert H.-J., Forssmann W.-G., Mollerup S., Herter P., Weber G., Cermak R., Ankorina-Stark I., Schlatter E., Kruhoffer M.J. Am. Soc. Nephrol. 10:472-480(1999) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)

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