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Mouse Anti-MASP2 Recombinant Antibody (CBFYM-1744) (CBMAB-M1912-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYM-1744
Antibody Isotype
IgG2b
Application
WB

Basic Information

Immunogen
Synthetic peptide
Specificity
Human
Antibody Isotype
IgG2b
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
Buffer
TBS, pH 7.4, 1% BSA, 40% glycerol
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
Mannan Binding Lectin Serine Peptidase 2
Introduction
This gene encodes a member of the peptidase S1 family of serine proteases. The encoded preproprotein is proteolytically processed to generate A and B chains that heterodimerize to form the mature protease. This protease cleaves complement components C2 and C4 in order to generate C3 convertase in the lectin pathway of the complement system. The encoded protease also plays a role in the coagulation cascade through cleavage of prothrombin to form thrombin. Myocardial infarction and acute stroke patients exhibit reduced serum concentrations of the encoded protein. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed.
Entrez Gene ID
10747
UniProt ID
O00187
Alternative Names
Mannan Binding Lectin Serine Peptidase 2; Mannan-Binding Lectin Serine Peptidase 1 Pseudogene 1; Mannan-Binding Lectin Serine Protease 1 Pseudogene 1; Mannose-Binding Protein-Associated Serine Protease 2; Mannan-Binding Lectin Serine Protease 2; MBL-Associated Serine Protease 2; MASP-2; MBL-Associated Plasma Protein Of 19 KD
Function
Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase.
Biological Process
Cell surface pattern recognition receptor signaling pathway Source: ComplexPortal
Complement activation, classical pathway Source: UniProtKB-KW
Complement activation, lectin pathway Source: ComplexPortal
Positive regulation of opsonization Source: ComplexPortal
Proteolysis Source: ComplexPortal
Cellular Location
Secreted
Involvement in disease
MASP2 deficiency (MASPD):
A disorder that results in autoimmune manifestations, recurrent severe infections, and chronic inflammatory disease.
PTM
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Activated by cleavage after Arg-444. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.
More Infomation

Götz, M. P., Skjoedt, M. O., Bayarri-Olmos, R., Hansen, C. B., Pérez-Alós, L., Jarlhelt, I., ... & Garred, P. (2023). Lectin pathway enzyme MASP-2 and downstream complement activation in COVID-19. Journal of Innate Immunity, 15(1), 122-135.

Mulinti, P., Diekjürgen, D., Kurtzeborn, K., Balasubramanian, N., Stafslien, S. J., Grainger, D. W., & Brooks, A. E. (2022). Anti-coagulant and antimicrobial recombinant heparin-binding major ampullate spidroin 2 (MaSp2) silk protein. Bioengineering, 9(2), 46.

Gao, T., Zhu, L., Liu, H., Zhang, X., Wang, T., Fu, Y., ... & Cao, C. (2022). Highly pathogenic coronavirus N protein aggravates inflammation by MASP-2-mediated lectin complement pathway overactivation. Signal Transduction and Targeted Therapy, 7(1), 318.

Damoah, C. E., Snir, O., Hindberg, K., Garred, P., Ludviksen, J. K., Brækkan, S. K., ... & INVENT Consortium. (2022). High levels of complement activating enzyme MASP-2 are associated with the risk of future incident venous thromboembolism. Arteriosclerosis, Thrombosis, and Vascular Biology, 42(9), 1186-1197.

Elhadad, S., Chapin, J., Copertino, D., Van Besien, K., Ahamed, J., & Laurence, J. (2021). MASP2 levels are elevated in thrombotic microangiopathies: association with microvascular endothelial cell injury and suppression by anti-MASP2 antibody narsoplimab. Clinical & Experimental Immunology, 203(1), 96-104.

Lafayette, R. A., Rovin, B. H., Reich, H. N., Tumlin, J. A., Floege, J., & Barratt, J. (2020). Safety, tolerability and efficacy of narsoplimab, a novel MASP-2 inhibitor for the treatment of IgA nephropathy. Kidney international reports, 5(11), 2032-2041.

Gao, T., Hu, M., Zhang, X., Li, H., Zhu, L., Liu, H., ... & Cao, C. (2020). Highly pathogenic coronavirus N protein aggravates lung injury by MASP-2-mediated complement over-activation. MedRxiv, 2020-03.

García-Laorden, M. I., Hernández-Brito, E., Muñoz-Almagro, C., Pavlovic-Nesic, S., Rúa-Figueroa, I., Briones, M. L., ... & Rodríguez-Gallego, C. (2020). Should MASP-2 deficiency be considered a primary immunodeficiency? Relevance of the lectin pathway. Journal of clinical immunology, 40, 203-210.

Bibert, S., Piret, J., Quinodoz, M., Collinet, E., Zoete, V., Michielin, O., ... & Bochud, P. Y. (2019). Herpes simplex encephalitis in adult patients with MASP-2 deficiency. PLoS pathogens, 15(12), e1008168.

Meijides-Mejías, C., Castillo-González, W., Rodríguez-Pérez, J. A., Lombillo-Alfonso, F., Mirabal-Viel, A., Pérez-del-Vallín, V., & Dorta-Contreras, A. J. (2019). MASP-2: New evaluating parameters. Revista Cubana de Investigaciones Biomédicas, 38(1).

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

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