Abcam, ab316432, Recombinant Human MASP2 Protein Standard (His tag)

Size: 10µg
Recombinant Human MASP2 Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.
Key facts
Purity:>80% SDS-PAGE,
Expression system:HEK 293 cells,
Tags:His tag N-Terminus,
Applications:sELISA, SDS-PAGESee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:O00187,
Animal free:Yes,
Carrier free:No,
Species:Human,
Storage buffer:pH: 7.3 - 7.5Constituents: 2.922% Sodium chloride, 0.64107% disodium;hydrogen phosphate;dodecahydrate, 0.02858% Potassium phosphate monobasic

Product details:
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
MASP-2 also known as Mannan-binding lectin serine protease 2 is an important component of the innate immune system. This protein has a molecular mass of approximately 76 kDa and is expressed in the liver before being released into the bloodstream. MASP-2 primarily acts during the lectin pathway of the complement system where it plays an essential role in immune defense. The protein activates the complement cascade upon binding with carbohydrate molecules on pathogen surfaces contributing to opsonization and direct lysis of pathogens.
Biological function summary
MASP-2 associates with MBL (Mannose-binding lectin) and forms a complex critical for the lectin pathway's function. In this complex MASP-2 initiates the cleavage of complement proteins C4 and C2 forming the C3 convertase. This action enhances the immune response by promoting the clearance of pathogens. MASP-1 is another protease that works closely with MASP-2 in this pathway although the two have distinct roles—MASP-2 is primarily responsible for the activation of the downstream components of the cascade.
Pathways
MASP-2 plays an integral role in the complement system and particularly in the lectin pathway which is one of the three pathways of complement activation. It connects with both the classical and alternative pathways through the formation of C3 convertase a critical step in the complement cascade. The interactions with other proteins like MASP-1 and MBL are significant; MASP-1 has an additional role in the activation sequence by further augmenting MASP-2's activity and facilitating efficient pathogen clearance.
MASP-2 is connected to conditions like autoimmune diseases and recurrent infections due to its involvement in the complement system. For instance MASP-2 deficiency can lead to increased susceptibility to infections reflecting its role in pathogen clearance. The protein has been studied in relation to systemic lupus erythematosus where dysregulation of the complement pathway can exacerbate disease symptoms. Proteins such as MBL and MASP-1 which interact closely with MASP-2 also have roles in these disease states and further illustrate the importance of proper complement system functioning in disease prevention and control.