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Formalin-fixed, paraffin-embedded human Brain stained with Serum Amyloid P Mouse Monoclonal Antibody (APCS/3240).
SDS-PAGE Analysis of Purified PSA Mouse Monoclonal Antibody (APCS/3240). Confirmation of Integrity and Purity of Antibody.
Analysis of Protein Array containing more than 19,000 full-length human proteins using Serum Amyloid P Mouse Monoclonal Antibody (APCS/3240). Z- and S- Score: The Z-score represents the strength of a signal that a monoclonal antibody (Monoclonal Antibody) (in combination with a fluorescently-tagged anti-IgG secondary antibody) produces when binding to a particular protein on the HuProtTM array. Z-scores are described in units of standard deviations (SD’s) above the mean value of all signals generated on that array. If targets on HuProtTM are arranged in descending order of the Z-score, the S-score is the difference (also in units of SD’s) between the Z-score. S-score therefore represents the relative target specificity of a Monoclonal Antibody to its intended target. A Monoclonal Antibody is considered to specific to its intended target, if the Monoclonal Antibody has an S-score of at least 2.5. For example, if a Monoclonal Antibody binds to protein X with a Z-score of 43 and to protein Y with a Z-score of 14, then the S-score for the binding of that Monoclonal Antibody to protein X is equal to 29.
Serum amyloid P (SAP) is a glycoprotein belonging to the pentraxin family of proteins, which has a characteristic pentameric organization and calciumdependent ligand binding. Secreted by liver epithelial cells, SAP is found in serum and urine. Although the function of SAP has not been clearly established, it has been shown to interact with DNA and histones and is thought to play a role in scavenging nuclear material released from damaged circulating cells. Also designated PTX2, SAP is a precursor of the protein amyloid P component (AP), which is universally associated with the amyloid deposits in all forms of amyloidoses, including Alzheimer s disease. SAP is a decamer of ten identical, noncovalently linked subunits, each of which may be post-translationally modified by glycosylation.
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