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

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

Mouse

Clone

CBFYM-1744

Application

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.

More Infomation

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.

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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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.

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