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Rat Anti-MASP1 Recombinant Antibody (CBFYM-1738) (CBMAB-M1905-FY)


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Summary

Host Animal
Rat
Specificity
Human
Clone
CBFYM-1738
Antibody Isotype
IgG2a
Application
Immunoassay, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG2a
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
Mannan Binding Lectin Serine Peptidase 1
Introduction
This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants.
Entrez Gene ID
5648
UniProt ID
P48740
Alternative Names
Mannan Binding Lectin Serine Peptidase 1; Complement-Activating Component Of Ra-Reactive Factor; Mannose-Binding Lectin-Associated Serine Protease 1; Mannose-Binding Protein-Associated Serine Protease; C4/C2 Activating Component Of Ra-Reactive Factor; Ra-Reactive Factor Serine Protease P100; Complement Factor MASP-3; Serine Protease 5; CRARF1; CRARF; PRSS5; RaRF; Mannan-Binding Lectin Serine Peptidase 1 (C4/C2 Activating Component Of Ra-Reactive Factor)
Function
Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development (PubMed:21258343).
Biological Process
Cell surface pattern recognition receptor signaling pathway Source: ComplexPortal
Complement activation, lectin pathway Source: ComplexPortal
Negative regulation of complement activation Source: UniProtKB
Positive regulation of opsonization Source: ComplexPortal
Proteolysis Source: ComplexPortal
Cellular Location
Secreted
Involvement in disease
3MC syndrome 1 (3MC1):
A form of 3MC syndrome, an autosomal recessive disorder characterized by facial dysmorphism, craniosynostosis, learning disability, and genital, limb and vesicorenal anomalies. Facial features include hypertelorism, blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli, Malpuech, and Michels syndromes.
PTM
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
N-glycosylated. Some N-linked glycan are of the complex-type (By similarity).
Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing.
More Infomation

Liu, X., Tan, S., Liu, H., Jiang, J., Wang, X., Li, L., & Wu, B. (2023). Hepatocyte‐derived MASP1‐enriched small extracellular vesicles activate HSCs to promote liver fibrosis. Hepatology, 77(4), 1181-1197.

Hurler, L., Toonen, E. J., Kajdácsi, E., van Bree, B., Brandwijk, R. J., de Bruin, W., ... & Yong, C. (2022). Distinction of early complement classical and lectin pathway activation via quantification of C1s/C1-INH and MASP-1/C1-INH complexes using novel ELISAs. Frontiers in Immunology, 13, 1039765.

Golomingi, M., Kohler, J., Jenny, L., Hardy, E. T., Dobó, J., Gál, P., ... & Schroeder, V. (2022). Complement lectin pathway components MBL and MASP-1 promote haemostasis upon vessel injury in a microvascular bleeding model. Frontiers in immunology, 13, 948190.

Rosbjerg, A., Würzner, R., Garred, P., & Skjoedt, M. O. (2021). Masp-1 and masp-3 bind directly to aspergillus fumigatus and promote complement activation and phagocytosis. Journal of Innate Immunity, 13(4), 211-224.

Norheim, K. B., Imgenberg-Kreuz, J., Alexsson, A., Johnsen, S. J. A., Bårdsen, K., Brun, J. G., ... & Omdal, R. (2021). Genetic variants at the RTP4/MASP1 locus are associated with fatigue in Scandinavian patients with primary Sjögren’s syndrome. RMD open, 7(3), e001832.

Gajek, G., Świerzko, A. S., & Cedzyński, M. (2020). Association of polymorphisms of MASP1/3, COLEC10, and COLEC11 genes with 3MC syndrome. International journal of molecular sciences, 21(15), 5483.

Alberts, A., Klingberg, A., Wessig, A. K., Combes, C., Witte, T., Brand, K., ... & Neumann, K. (2020). C-reactive protein (CRP) recognizes uric acid crystals and recruits proteases C1 and MASP1. Scientific Reports, 10(1), 6391.

Jenny, L., Noser, D., Larsen, J. B., Dobó, J., Gál, P., Pál, G., & Schroeder, V. (2019). MASP-1 of the complement system alters fibrinolytic behaviour of blood clots. Molecular immunology, 114, 1-9.

Debreczeni, M. L., Németh, Z., Kajdácsi, E., Schwaner, E., Makó, V., Masszi, A., ... & Cervenak, L. (2019). MASP-1 increases endothelial permeability. Frontiers in immunology, 10, 991.

Angus, D., Linde-Zwirble, W., Lidicker, J., Clermont, G., Carcillo, J., Pinsky, M., ... & Taylor, R. (2019). Reduced mannose-binding lectin-associated serine protease (MASP)-1 is associated with disturbed coagulation in septic shock. Thrombosis and Haemostasis, 119(06), 952-961.

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

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