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Rabbit Anti-CPB2 Recombinant Antibody (CBFYC-2151) (CBMAB-C2219-FY)

This product is rabbit antibody that recognizes CPB2. The antibody CBFYC-2151 can be used for immunoassay techniques such as: ELISA.
See all CPB2 antibodies

Summary

Host Animal
Rabbit
Specificity
Mouse
Clone
CBFYC-2151
Antibody Isotype
IgG
Application
ELISA

Basic Information

Immunogen
Recombinant Mouse Carboxypeptidase B2CPB2 protein
Specificity
Mouse
Antibody Isotype
IgG
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
Liquid
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
Carboxypeptidase B2
Introduction
CPB2 (Carboxypeptidase B2) is a Protein Coding gene. Diseases associated with CPB2 include Factor Xiii Deficiency and Factor Xi Deficiency. Among its related pathways are Peptide hormone metabolism and Complement and coagulation cascades. Gene Ontology (GO) annotations related to this gene include metallocarboxypeptidase activity and carboxypeptidase activity. An important paralog of this gene is CPB1.
Entrez Gene ID
56373
UniProt ID
Q9JHH6
Alternative Names
carboxypeptidase B2; carboxypeptidase R; carboxypeptidase U; thrombin-activable fibrinolysis inhibitor; thrombin-activatable fibrinolysis inhibitor; EC 3.4.17.20
Function
Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.
Biological Process
Blood coagulation Source: UniProtKB-KW
Cellular response to glucose stimulus Source: Ensembl
Fibrinolysis Source: GO_Central
Liver regeneration Source: Ensembl
Negative regulation of fibrinolysis Source: Ensembl
Negative regulation of hepatocyte proliferation Source: Ensembl
Negative regulation of plasminogen activation Source: Ensembl
Positive regulation of extracellular matrix constituent secretion Source: Ensembl
Proteolysis Source: GO_Central
Regulation of complement activation Source: Reactome
Response to drug Source: Ensembl
Response to heat Source: Ensembl
Cellular Location
Secreted
PTM
N-glycosylated. N-glycan at Asn-108: Hex5HexNAc4.

Zhou, Q., Zhao, L., Shao, Z., Declerck, P., Leung, L. L., & Morser, J. (2022). Both plasma basic carboxypeptidases, carboxypeptidase B2 and carboxypeptidase N, regulate vascular leakage activity in mice. Journal of Thrombosis and Haemostasis, 20(1), 238-244.

Claesen, K., Mertens, J. C., Basir, S., De Belder, S., Maes, J., Bosmans, J., ... & Hendriks, D. (2021). Effect of Statin Therapy on the Carboxypeptidase U (CPU, TAFIa, CPB2) System in Patients With Hyperlipidemia: A Proof-of-Concept Observational Study. Clinical Therapeutics, 43(5), 908-916.

Claesen, K., Mertens, J. C., Leenaerts, D., & Hendriks, D. (2021). Carboxypeptidase U (CPU, TAFIa, CPB2) in thromboembolic disease: what do we know three decades after its discovery?. International journal of molecular sciences, 22(2), 883.

Claesen, K., Roth, L., Mertens, J. C., Hermans, K., Sim, Y., & Hendriks, D. (2021). Pleiotropic Effects of Atorvastatin Result in a Downregulation of the Carboxypeptidase U System (CPU, TAFIa, CPB2) in a Mouse Model of Advanced Atherosclerosis. Pharmaceutics, 13(10), 1731.

Khamsehnejad, M. I., Djadid, N. D., & Raz, A. (2019). Identification, molecular characterization, and in silico structural analysis of carboxypeptidase B2 of Anopheles stephensi. Journal of Medical Entomology, 56(1), 72-85.

Leenaerts, D., Loyau, S., Mertens, J. C., Boisseau, W., Michel, J. B., Lambeir, A. M., ... & Hendriks, D. (2018). Carboxypeptidase U (CPU, carboxypeptidase B2, activated thrombin‐activatable fibrinolysis inhibitor) inhibition stimulates the fibrinolytic rate in different in vitro models. Journal of Thrombosis and Haemostasis, 16(10), 2057-2069.

Leung, L. L. K., & Morser, J. (2018). Carboxypeptidase B2 and carboxypeptidase N in the crosstalk between coagulation, thrombosis, inflammation, and innate immunity. Journal of Thrombosis and Haemostasis, 16(8), 1474-1486.

Morser, J., Shao, Z., Nishimura, T., Zhou, Q., Zhao, L., Higgins, J., & Leung, L. L. K. (2018). Carboxypeptidase B2 and N play different roles in regulation of activated complements C3a and C5a in mice. Journal of Thrombosis and Haemostasis, 16(5), 991-1002.

Mohamed, H. T., El-Husseiny, N., El-Ghonaimy, E. A., Ibrahim, S. A., Bazzi, Z. A., Cavallo-Medved, D., ... & Mohamed, M. M. (2018). IL-10 correlates with the expression of carboxypeptidase B2 and lymphovascular invasion in inflammatory breast cancer: the potential role of tumor infiltrated macrophages. Current Problems in Cancer, 42(2), 215-230.

Oguntona, T. S. (2018). The potential role of a carboxypeptidase B2 inhibitor in renal fibrosis (Doctoral dissertation, University of Sheffield).

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

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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