Reactivity | RtSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. Immobilized rrPTX2 at 2 µg/mL (100 µL/well) can bind rhCD32a with a linear range of 0.08-5 µg/mL. |
Source | Mouse myeloma cell line, NS0-derived rat Pentraxin 2/SAP protein Gln21-Ser228 with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | No results obtained: Gln21 predicted |
Structure / Form | Noncovalently-linked homopentamer |
Protein/Peptide Type | Recombinant Proteins |
Gene | Apcs |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 25 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE | 29-35 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CaCl2. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Pentraxin 2 (PTX2), also known as Serum Amyloid P Component (SAP), is a secreted serum glycoprotein that is a universal non-fibrillar component of amyloid deposits. These extracellular deposits of insoluble protein fibrils are the result of protein misfolding and can lead to tissue damage and disease (1, 2). PTX2 belongs to the pentaxin superfamily, whose members have the characteristic pentagonal discoid arrangement of five non-covalently bound subunits. Pentaxins bind to a variety of molecules in a calcium-dependent lectin-like manner through a pattern-recognition-binding site (1, 4, 5). Two subfamilies of pentaxins, the classical or short pentaxin subfamily that includes the serum C-reactive protein (CRP) and PTX2, and the fusion or long pentaxin subfamily whose members contain pentaxin-related carboxyl-terminal halves, are known (1).
PTX2 and CRP share approximately 50% amino acid sequence identity (2, 5). They are produced and secreted by liver hepatocytes and circulates in plasma. Rat and mouse PTX2 are major acute-phase proteins whose plasma concentrations increase dramatically during an acute phase response (2). In human where CRP is the major acute-phase protein, the plasma concentration of human PTX2 remains relatively constant in response to tissue-damage (2, 5). The gene for PTX2 has been localized to rat chromosome 13 of 23 where it is closely linked to the gene for CRP.
PTX2 associates ubiquitously with all amyloid deposits that are implicated in a diverse range of diseases including Alzheimer’s and prion diseases, type 2 diabetes and various systemic amyloidoses (3, 6, 7). As a non-fibrillar component, PTX2 regulates the solubility of amyloid fibrils and protects them from degradation by proteolytic enzymes and phagocytic cells. In addition to its role in the pathogenesis of amyloidoses, PTX2 also has an important physiological function in innate immunity (8). It is an opsonin that interacts with all three types of human Fc gamma receptors that mediate phagocytosis by polymorphonuclear leukocytes. It has been proposed that PTX2 may function as an opsonin for a variety of ligands including autoantigens, apoptotic cells, chromatin, DNA, and micro-organisms.
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