Abcam, ab213888, Mouse SAP ELISA Kit (PTX2)

Size: 1 x 96Tests
Mouse SAP ELISA Kit (PTX2) is a Sandwich (quantitative) ELISA for the measurement of Mouse SAP (PTX2) in Mouse in Cell/Tissue Extracts, Cell Culture Media, Biofluids samples.
Key facts
Detection method:Colorimetric,
Sample types:Cell Lysate, Cell culture supernatant, EDTA Plasma, Heparin Plasma, Serum,
Reacts with:Mouse,
Assay type:Sandwich (quantitative),
Sensitivity:< 50 pg/mL,
Range:1.56 - 100 ng/mL,
Assay time:3h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
The Mouse SAP Enzyme-Linked Immunosorbent Assay (ELISA) kit (ab213888) is designed for the quantitative measurement of Mouse SAP in cell culture supernatants, cell lysates, serum and plasma (heparin, EDTA).
The ELISA kit is based on standard sandwich enzyme-linked immunosorbent assay technology. A monoclonal antibody from rat specific for SAP has been pre-coated onto 96-well plates. Standards (Expression system for standard: NSO; Immunogen sequence: Q21- D224) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for SAP is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex was added and unbound conjugates were washed away with PBS or TBS buffer. HRP substrate TMB was used to visualize HRP enzymatic reaction. TMB was catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Mouse Serum Amyloid P / SAP amount of sample captured in plate.
SAP also known as PTX2 or APCS, is the identical serum form of amyloid P component (AP), a 25kDa pentameric protein first identified as the pentagonal constituent of
in vivo
pathological deposits called "amyloid". It belongs to the pentraxins family, characterized by calcium dependent ligand binding and distinctive flattened beta-jellyroll structure similar to that of the legume lectins. This gene is mapped to 1q23.2. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that this protein binds to apoptotic cells at an early stage, which raises the possibility that it is involved in dealing with apoptotic cells
in vivo

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Serum Amyloid P component also known as SAP P-SAP or APCS protein is a pentraxin family member. It has a molecular mass of approximately 25 kDa. SAP expresses mainly in the liver and circulates in blood plasma. The protein consists of five identical subunits which form a homopentameric structure. This structure enables SAP to bind to amyloid fibrils a defining mechanical action of this protein.
Biological function summary
SAP plays a role in the immune system by recognizing damaged cells and pathogens. It acts as an opsonin marking these cellular targets for phagocytosis. As part of a complex SAP stabilizes extracellular matrix and amyloid deposits. It binds specifically to amyloid fibrils found in various tissues potentially facilitating their removal by immune cells. The protein's binding actions are important for its role in maintaining tissue and fluid homeostasis.
Pathways
SAP is actively involved in the innate immune response and amyloidogenic pathways. It interacts with the complement system to enhance the clearance of cell debris and amyloid fibrils. The complement system is an important component of innate immunity where SAP can engage with complement proteins like C1q. This interaction suggests that SAP plays roles in modulating both inflammation and tissue repair processes.
SAP has significant connections. SAP is related to systemic amyloidosis where it binds to amyloid deposits affecting multiple organs. Moreover SAP has been implicated in Alzheimer's disease due to its interaction with beta-amyloid protein plaques. In these disorders the involvement of SAP aids researchers in understanding the pathological mechanisms and could open avenues for targeted therapies aimed at modulating SAP functions.