Mouse Pentraxin 2/SAP Alexa Fluor® 405-conjugated Antibody
R&D Systems, part of Bio-Techne | Catalog # FAB2558V
Key Product Details
Species Reactivity
Applications
Label
Antibody Source
Product Specifications
Immunogen
Gln21-Asp224
Accession # P12246
Specificity
Clonality
Host
Isotype
Applications
Western Blot
Formulation, Preparation, and Storage
Purification
Formulation
Shipping
Stability & Storage
Background: Pentraxin 2/SAP
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).
Long Name
Alternate Names
Gene Symbol
UniProt
Additional Pentraxin 2/SAP Products
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
For research use only