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The recombinant Human NPR2 was expressed with the amino acid range of 23-458. This NPR2 protein is theoretically predicted to have a molecular weight of 64.5 kDa. The NPR2 protein was expressed in e.coli. The NPR2 coding gene included the N-terminal 6xHis-SUMO tag, which simplifies the detection and purification processes of the recombinant NPR2 protein in following stages of expression and purification.Atrial natriuretic peptide receptor 2 (NPR2) is a membrane-bound guanylate cyclase receptor that plays a crucial role in cardiovascular regulation. Also known as natriuretic peptide receptor B (NPR-B), it primarily binds atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Upon binding, NPR2 activates the synthesis of cyclic GMP (cGMP), a second messenger that regulates various physiological processes. NPR2 is particularly important in the regulation of blood pressure, fluid homeostasis, and cardiovascular development. Mutations in the NPR2 gene are associated with certain skeletal dysplasias. Research on NPR2 extends into cardiovascular biology, endocrinology, and the development of therapeutic strategies targeting the natriuretic peptide pathway.
The recombinant Human NPR2 was expressed with the amino acid range of 23-458. This NPR2 protein is theoretically predicted to have a molecular weight of 64.5 kDa. The NPR2 protein was expressed in e.coli. The NPR2 coding gene included the N-terminal 6xHis-SUMO tag, which simplifies the detection and purification processes of the recombinant NPR2 protein in following stages of expression and purification.Atrial natriuretic peptide receptor 2 (NPR2) is a membrane-bound guanylate cyclase receptor that plays a crucial role in cardiovascular regulation. Also known as natriuretic peptide receptor B (NPR-B), it primarily binds atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP). Upon binding, NPR2 activates the synthesis of cyclic GMP (cGMP), a second messenger that regulates various physiological processes. NPR2 is particularly important in the regulation of blood pressure, fluid homeostasis, and cardiovascular development. Mutations in the NPR2 gene are associated with certain skeletal dysplasias. Research on NPR2 extends into cardiovascular biology, endocrinology, and the development of therapeutic strategies targeting the natriuretic peptide pathway.
| Cat.No | ACP04030 | Target Name | NPR2 |
|---|---|---|---|
| Form | Liquid or Lyophilized powder | Expression System | E.coli |
| Expression Range | 23-458aa | Mol Weight | 64.5kDa |
| Protein Length | Extracellular Domain | Purity | Greater than 90% as determined by SDS-PAGE. |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | P20594 |
|---|
Uniprot Id
P20594
Target Species
Human
Target Name
NPR2
Target Full Name
Atrial natriuretic peptide receptor 2
Target Function
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.
Target Involvement
Acromesomelic dysplasia, Maroteaux type (AMDM); Epiphyseal chondrodysplasia, Miura type (ECDM); Short stature with non-specific skeletal abnormalities (SNSK)
Target Subcellular Location
Cell membrane; Single-pass type I membrane protein.
Target Protein Families
Adenylyl cyclase class-4/guanylyl cyclase family
Target Research Area
Cancer, Cardiovascular
Target Synonyms
AMDM; ANP-B; ANPB; ANPR-B; ANPRB; ANPRB_HUMAN; Atrial natriuretic peptide B type receptor; Atrial natriuretic peptide receptor 2; Atrial natriuretic peptide receptor type B; Atrionatriuretic peptide receptor B; GC-B; GCB; Guanylate cyclase B; GUC 2B; GUC2B; GUCY2B; Natriuretic peptide receptor B; Natriuretic peptide receptor B/guanylate cyclase B; NPR-B; Npr2; NPRB; NPRBi
Target Background
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.
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