Recombinant Human MASP2 Protein Standard (His tag)
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Recombinant Human MASP2 Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.
View Alternative Names
Mannan-binding lectin serine protease 2, MBL-associated serine protease 2, Mannose-binding protein-associated serine protease 2, MASP-2, MASP2
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Human MASP2 Protein Standard (His tag) (AB316432)
Sandwich ELISA with the capture antibody dilution at 2 ug/mL and detector antibody dilution at 0.5 ug/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human MASP2 Protein Standard (His tag) (AB316432)
SDS-PAGE analysis of ab316432
Reactivity data
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.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
Specifications
Form
Liquid
General info
Function
Precursor of a serum protease that activates the lectin pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed : 11527969, PubMed : 22691502). The lectin complement system is activated following association of lectins, such as MBL2, FCN1, FCN2 or FCN3, to carbohydrates on the pathogen surface (PubMed : 22691502, PubMed : 22966085). MASP2 is cleaved and activated by MASP1 in response to lectin-binding to pathogen carbohydrates (PubMed : 10946292, PubMed : 22949645, PubMed : 22966085, PubMed : 9087411). Can activate prothrombin to thrombin (PubMed : 39924859).. Mannan-binding lectin serine protease 2 B chain. Serine protease component of the lectin complement pathway, which catalyzes cleavage and activation of C2 and C4, the next components of the complement pathway.
Sequence similarities
Belongs to the peptidase S1 family.
Post-translational modifications
Activated by cleavage after Arg-444 by MASP1. The uncleaved zymogen is inactive towards synthetic substrates, but has sufficient activity to effect autocatalytic cleavage.. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Target data
Product promise
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