Work with LifeSpan to design a custom immunohistochemistry to address your specific biological question. Outsource the entire localization process without having to
worry about finding and characterizing target specific antibodies, sourcing and validating difficult-to-find tissues, and having the ability to interpret the resulting
immunostaining in relation to complex human pathologies.
TCR Screening Services
Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding.
Our non-GLP TCR services are designed on the FDA recommendation outlined in their "Points to Consider in the Manufacture and Testing of Monoclonal Antibody Products for Human Use".
Rabbit Polyclonal (IgG) to Human APCS / Serum Amyloid P / SAP
IHC, Western blot, ELISA
Mouse Monoclonal [clone 5.4A] (IgG1) to Human APCS / Serum Amyloid P / SAP
Human APCS / Serum Amyloid P / SAP
Human (tested or 100% immunogen sequence identity)
IgG1 Monoclonal [5.4A]
Protein A purified
Specificity and Use
Human serum amyloid P.
Specific for Amyloid P from human serum. Amyloid consists mainly of rigid, non-branching protein fibrils, together with rod-like aggregates of a pentagonal-shaped glycoprotein called amyloid P protein. Amyloid P protein comprises 10 per cent of amyloid tissue and is present in all but the central nervous system forms of amyloid. Amyloid P protein is a constituent of normal basement membranes and the microfibrillaryelastic fiber network.
APCS Antibody, 9.5S alpha-1-glycoprotein Antibody, Amyloid P component, serum Antibody, Pentaxin-related Antibody, PTX2 Antibody, Serum Amyloid P Antibody, Serum amyloid P-component Antibody, SAP Antibody
APCS / Serum Amyloid P / SAP is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. 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.