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Rat Anti-CORIN Recombinant Antibody (CBFYC-2102) (CBMAB-C2168-FY)

This product is rat antibody that recognizes CORIN. The antibody CBFYC-2102 can be used for immunoassay techniques such as: WB, ICC.
See all CORIN antibodies

Summary

Host Animal
Rat
Specificity
Human
Clone
CBFYC-2102
Antibody Isotype
IgG2a
Application
WB, ICC

Basic Information

Immunogen
Mouse myeloma cell line NS0-derived recombinant human Corin, Ser67-Asn1042
Specificity
Human
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Lyophilized
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
corin, serine peptidase
Introduction
CORIN (Corin, Serine Peptidase) is a Protein Coding gene. Diseases associated with CORIN include Preeclampsia/Eclampsia 5 and Pre-Eclampsia. Among its related pathways are Cardiac conduction and Myometrial Relaxation and Contraction Pathways. Gene Ontology (GO) annotations related to this gene include serine-type endopeptidase activity and serine-type exopeptidase activity. An important paralog of this gene is ST14.
Entrez Gene ID
10699
UniProt ID
Q9Y5Q5
Alternative Names
Corin, Serine Peptidase; Heart-Specific Serine Proteinase ATC2; Transmembrane Protease Serine 10; Pro-ANP-Converting Enzyme; TMPRSS10; CRN; Atrial Natriuretic Peptide-Converting Enzyme; Corin, Serine Protease
Function
Serine-type endopeptidase involved in atrial natriuretic peptide (NPPA) and brain natriuretic peptide (NPPB) processing (PubMed:10880574, PubMed:21288900, PubMed:20489134, PubMed:21763278).

Converts through proteolytic cleavage the non-functional propeptides NPPA and NPPB into their active hormones, ANP and BNP(1-32) respectively, thereby regulating blood pressure in the heart and promoting natriuresis, diuresis and vasodilation (PubMed:10880574, PubMed:21288900, PubMed:20489134, PubMed:21763278).

Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus (PubMed:22437503).

Also acts as a regulator of sodium reabsorption in kidney (By similarity).

Isoform 2:
has weaker endopeptidase activity compared to isoform 1.
Biological Process
Female pregnancy Source: UniProtKB
Peptide hormone processing Source: UniProtKB
Regulation of blood pressure Source: UniProtKB
Regulation of cardiac conduction Source: Reactome
Regulation of renal sodium excretion Source: UniProtKB
Regulation of systemic arterial blood pressure by atrial natriuretic peptide Source: UniProtKB
Cellular Location
Cell membrane. May easily detached from the endothelial cell membrane.
Isoform 2: Cell membrane. Less efficiently targeted to the cell membrane compared to isoform 1.
Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment: Secreted. Soluble form produced following cleavage by ADAM10.
Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment: Secreted. Soluble form produced following autocatalytic cleavage.
Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment: Secreted. Soluble form produced following autocatalytic cleavage.
Involvement in disease
Pre-eclampsia/eclampsia 5 (PEE5):
A hypertensive disorder of pregnancy characterized by new hypertension (blood pressure 140/90 or greater) presenting after 20 weeks' gestation with clinically relevant proteinuria. It impacts 2 individuals, the mother and her child, both of whom can be severely affected. Preeclampsia is one of the causes of maternal mortality and morbidity worldwide.
Topology
Cytoplasmic: 1-45
Helical: 46-66
Extracellular: 67-1042
PTM
N-glycosylated; required for processing and activation.
Activated through proteolytic processing by a trypsin-like protease; cleaved into a N-terminal propeptide and an activated corin protease fragment. Different soluble forms are produced by cleavage and autocatalytic cleavage: Atrial natriuretic peptide-converting enzyme, 180 kDa soluble fragment is produced by cleavage by ADAM10, while 160 kDa and 100 kDa soluble fragments are produced by autocatalytic cleavage. Cleavage by ADAM10 to produce soluble 180 kDa soluble fragment takes place after the transmembrane region and before FZ 1.
A disulfide bond links the activated corin protease fragment and the N-terminal propeptide. The disulfide bond also links the activated corin protease fragment with soluble fragments (100 kDa, 160 kDa and 180 kDa fragments).

Zou, T., Yao, S., Du, M. F., Mu, J. J., Chu, C., Hu, G. L., ... & Wang, Y. (2021). Associations of corin genetic polymorphisms with salt sensitivity, blood pressure changes, and hypertension incidence in Chinese adults. The Journal of Clinical Hypertension, 23(12), 2115-2123.

Dong, N., Niu, Y., Chen, Y., Sun, S., & Wu, Q. (2020). Function and regulation of corin in physiology and disease. Biochemical Society Transactions, 48(5), 1905-1916.

He, M., Zhang, Y., Li, H., Liu, M., Dong, N., & Wu, Q. (2020). A common CORIN variant in hypertension reduces corin intracellular trafficking by exposing an inhibitory N-terminus. Biochemical and Biophysical Research Communications, 530(1), 35-41.

Celik, S., Karbalaei-Sadegh, M., Rådegran, G., Smith, J. G., & Gidlöf, O. (2019). Functional screening identifies microRNA regulators of corin activity and atrial natriuretic peptide biogenesis. Molecular and cellular biology, 39(23), e00271-19.

Utikal, J., Maherali, N., Kulalert, W., & Hochedlinger, K. (2019). The serine protease activity of corin is required for normal pigment type switching. Journal of Investigative Dermatology, 139, 257e259.

Yu, R., Han, X., Zhang, X., Wang, Y., & Wang, T. (2018). Circulating soluble corin as a potential biomarker for cardiovascular diseases: a translational review. Clinica Chimica Acta, 485, 106-112.

Chen, S., Wang, H., Li, H., Zhang, Y., & Wu, Q. (2018). Functional analysis of corin protein domains required for PCSK6-mediated activation. The international journal of biochemistry & cell biology, 94, 31-39.

Zhang, Y., Zhou, T., Niu, Y., He, M., Wang, C., Liu, M., ... & Wu, Q. (2017). Identification and functional analysis of CORIN variants in hypertensive patients. Human mutation, 38(12), 1700-1710.

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For research use only. Not intended for any clinical use.

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