Sign in or Register   Sign in or Register
  |  

Mouse Anti-CPB2 Recombinant Antibody (CBYJT-1143) (CBMAB-T0156-YJ)

Provided herein is a Mouse monoclonal antibody, which binds to CPB2 (Carboxypeptidase B2). The antibody can be used for immunoassay techniques, such as ELISA, WB.
See all CPB2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYJT-1143
Antibody Isotype
IgG1
Application
ELISA, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
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!]

Buffer
PBS, pH 7.2
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 related to 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 CPB2 include metallocarboxypeptidase activity and carboxypeptidase activity. An important paralog of CPB2 is CPB1.
Entrez Gene ID
UniProt ID
Alternative Names
Carboxypeptidase B2; Carboxypeptidase B2 (Plasma, Carboxypeptidase U); Thrombin-Activatable Fibrinolysis Inhibitor; Thrombin-Activable Fibrinolysis Inhibitor; Carboxypeptidase B2 (Plasma); Plasma Carboxypeptidase B; Carboxypeptidase U; Carboxypeptidase R
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).

Ask a question We look forward to hearing from you.
0 reviews or Q&As
Loading...
Have you used Mouse Anti-CPB2 Recombinant Antibody (CBYJT-1143)?
Submit a review and get a Coupon or an Amazon gift card. 20% off Coupon $30 eGift Card
Submit a review
Loading...
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.).

Online Inquiry

Documents

Contact us

  • Tel: (USA)
  • (UK)
  • Fax:
  • Email:

Submit A Review

Go to
Compare