Rabbit Anti-CPB2 Recombinant Antibody (173) (V2LY-1206-LY933)

Name: Rabbit Anti-CPB2 Recombinant Antibody (173)
SKU: V2LY-1206-LY933
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Rabbit

Clone

173

Application

ELISA

Immunogen

Recombinant Mouse Carboxypeptidase B2 / CPB2 protein.

Host Species

Rabbit

Specificity

Mouse

Antibody Isotype

IgG

Clonality

Monoclonal Antibody

Application Notes

Application	Note
ELISA	1:5,000-1:10,000

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

Format

Liquid

Buffer

PBS

Preservative

None

Concentration

Batch dependent

Purity

>95% as determined by analysis by SDS-PAGE

Storage

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

More Infomation

Target

Full Name

Carboxypeptidase B2

Entrez Gene ID

56373

UniProt ID

Q9JHH6

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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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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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