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.
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".
(tested or 100% immunogen sequence identity)
Protein A/G purified
Performing IHC? See our complete line of Immunohistochemistry Reagents including antigen retrieval solutions, blocking agents
ABC Detection Kits and polymers, biotinylated secondary antibodies, substrates and more.
PAPPA / PAPP-A antibody was raised against purified human PAPP-A.
Specific for native human PAPP-A. Heat and SDS denatured PAPP-A is also recognized, but not acid-treated PAPP-A. The epitope is different from those of clones 6F172 and 6F174 and is located on the PAPP-A subunit of the heterotetramer. In sandwich ELISA the optimal combination was clone 6F174 as coating and biotinylated clone 6F173 as detection. This product detects only unreduced PAPP-A in Western Blot. It gives the strongest signal in Immunohistochemistry compared to clone 6F172 and clone 6F174.
Suitable for use in ELISA, Western Blot, and Immunohistochemistry. ELISA: 1:8000. In sandwich ELISA the optimal combination was clone 6F174 as coating and biotinylated clone 6F173 as detection. Western Blot: Detects only unreduced PAPP-A. Immunohistochemistry: Gives the strongest signal compared to clone 6F172 and clone 6F174.
PBS, pH 7.2, 15 mM Sodium Azide
Short term: 4°C; Long term: Add glycerol (40-50%) -20°C.
Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF.