MASP1 Antibody Cat

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MASP1 Antibody Cat. No.: 19-799 MASP1 Antibody Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids 20-300 IMMUNOGEN: of human MASP1 (NP_001870.3). TESTED APPLICATIONS: WB APPLICATIONS: WB: ,1:500 - 1:2000 POSITIVE CONTROL: 1) HeLa PREDICTED MOLECULAR Observed: 60kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid September 24, 2021 1 https://www.prosci-inc.com/masp1-antibody-19-799.html BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: MASP1 Mannan-binding lectin serine protease 1, 3421-, Complement factor MASP-3, Complement-activating component of Ra-reactive factor, Mannose-binding lectin- associated serine protease 1, MASP-1, Mannose-binding protein-associated serine ALTERNATE NAMES: protease, Ra-reactive factor serine protease p100, RaRF, Serine protease 5, Mannan- binding lectin serine protease 1 heavy chain, Mannan-binding lectin serine protease 1 light chain, MASP1, CRARF, CRARF1, PRSS5 GENE ID: 5648 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References 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 BACKGROUND: 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. ANTIBODIES FOR RESEARCH USE ONLY. For additional information, visit ProSci's Terms & Conditions Page. September 24, 2021 2 https://www.prosci-inc.com/masp1-antibody-19-799.html.

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MASP-1, a Promiscuous Complement Protease: Structure of Its Catalytic Region Reveals the Basis of Its Broad Specificity 1
MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity 1 József Dobó 2,3* , Veronika Harmat 3† , László Beinrohr *, Edina Sebestyén *, Péter Závodszky *, Péter Gál 2* * Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina út 29, H-1113, Budapest, Hungary † Protein Modeling Group, Hungarian Academy of Sciences, and Laboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University , Pázmány Péter sétány 1A, H-1117, Budapest, Hungary Running title: Structure of MASP-1 CCP1-CCP2-SP Keywords (not in the title): lectin pathway; innate immunity; modular serine protease; mannan-binding lectin; MBL-associated serine protease; MASP-2; C1r; C1s; thrombin; trypsin; factor D 1 Abstract Mannose-binding lectin (MBL)-associated serine protease-1 (MASP-1) is an abundant component of the lectin pathway of complement. The related enzyme, MASP-2 is capable of activating the complement cascade alone. Though the concentration of MASP-1 far exceeds that of MASP-2 only a supporting role of MASP-1 has been identified regarding lectin pathway activation. Several non-complement substrates, like fibrinogen and factor XIII, have also been reported. MASP-1 belongs to the C1r/C1s/MASP family of modular serine proteases, however its serine protease domain is evolutionary different. We have determined the crystal structure of the catalytic region of active MASP-1 and refined it to 2.55 Å resolution. Unusual features of the structure are: an internal salt bridge (similar to one in factor D) between the S1 Asp189 and Arg224, and a very long 60-loop.
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