Reactivity | MuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its binding ability in a functional ELISA. When recombinant Mouse Pentraxin/SAP His-tag (2558-SAB) is immobilized at 10 μg/mL (100
µL/well), the concentration of Biotinylated recombinant human FC gamma RIIA/CD32a (R167) Protein that
produces 50% of the optimal binding response is found to be
approximately 0.5-2.5 µg/mL. |
Source | Mouse myeloma cell line, NS0-derived mouse Pentraxin 2/SAP protein Gln21-Asp224, with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | No results obtained: Gln21 predicted. |
Protein/Peptide Type | Recombinant Proteins |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.10 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. |
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SDS-PAGE | 27-35 kDa, under reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl and CaCl2. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile water. |
Pentraxin 2 (also known as Serum Amyoid P Component or SAP) is a secreted glycoprotein that is a universal non-fibrillar component of amyloid deposits. Amyloid is an abnormal extracellular deposit of insoluble protein fibrils that can lead to tissue damage and disease (1-3). Pentraxin 2 belongs to the pentraxin (pentaxin) family, whose members have a characteristic pentagonal discoid arrangement of five non-covalently bound subunits (4). Pentraxin domains contain the consensus sequence, HxCx(S/T)WxS (x = any amino acid), a lectin fold, and two calcium-binding sites (1). They bind to a variety of unrelated molecules in a calcium-dependent lectin-like manner (1, 4, 5). Pentraxin 2 and C-reactive protein (CRP) are members of the classical or short pentraxin subfamily and share 46% amino acid (aa) identity (1). Mouse Pentraxin 2 is the major acute-phase protein whose expression is dependent on complement activation, IL-6 and/or IL-1 beta , while in humans, CRP is the major acute-phase protein (2, 5, 9). Both are produced and secreted by liver hepatocytes and circulate in plasma. The 204 aa mature mouse Pentraxin 2 shares 79% aa identity with rat Pentraxin 2 and 63-68% aa identity with human, guinea pig, golden hamster, porcine, and bovine Pentraxin 2 (2, 5). Amyloid deposits containing Pentraxin 2 are implicated in a diverse range of diseases including Alzheimer’s, prion diseases, type 2 diabetes and various systemic amyloidoses (3, 6, 7). Pentraxin 2 regulates the solubility of amyloid fibrils and protects them from degradation. In addition to its pathogenic role, Pentraxin 2 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 neutrophil phagocytosis (8). Pentraxin 2 has been proposed to bind and sequester a variety of ligands including auto-antigens, apoptotic cells, chromatin, DNA, and micro-organisms (1-3). Pentraxin 2 is also a normal component of basement membranes (1).
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