Recombinant Human NPRB/NPR2 Protein, CF Summary
Details of Functionality |
Bioassay data are not available. |
Source |
Mouse myeloma cell line, NS0-derived human NPRB/NPR2 protein Arg23-Ile458, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Arg23 |
Protein/Peptide Type |
Innovator Recombinant Proteins |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
49 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
60-85 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human NPRB/NPR2 Protein, CF
Background
Human Natriuretic Peptide Receptor-2 (NPR2),
also known as NPRB, ANP-RB or guanylyl Cyclase-B, is a member of the guanylyl
cyclase family of proteins. NPR2 is a type I transmembrane glycoprotein that
contains a 436 amino acid extracellular domain (ECD) (aa 23‑458) for ligand binding, and a 569 amino acid cytoplasmic
domain that contains both a protein kinase domain and a carboxyl-terminal guanylate
cyclase domain. NPR2 is expressed most highly in in bone, brain, fibroblasts, heart,
kidney, liver, lung, uterine, and vascular smooth muscle tissue (1). NPR2
operates as an oligomer and binds both ANP (atrial natriuretic peptide) and BNP
(B type natriuretic peptide), and NPR2 is the principal receptor of CNP (C type
natriuretic peptide) (1, 2). Ligand binding to the extracellular ligand binding
domain, plus ATP to the intracellular kinase domain activates a cytoplasmic
guanylate cyclase (2). NPR2 pathway play a critical role in regulation of
skeletal growth (3), and patients with single defect NPR2 alleles are
statistically shorter than the average population (4). Over the extracellular
domain, human NPR2 is 97% and 96% identical to mouse and rat NPR2,
respectively.
-
Potter, L.R. et al. (2009) Handb Exp Pharmacol 191:341.
- Chang, M.S. et al. (1989) Nature 341:68.
- Tsuji, T. and Kunieda T. (2005) J Biol Chem 280:14288.
- Olney, R.C. et al. (2006) J Clin Endocrinol Metab 91:1229.
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