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".
Rat, Human, Monkey, Mouse, Bovine, Dog, Guinea pig, Hamster, Pig, Rabbit (tested or 100% immunogen sequence identity)
Protein A purified
IHC - Paraffin (10 µg/ml)
Western blot (1:1000)
Specificity and Use
PDIA3 / ERp57 antibody was raised against native rat liver Grp58 protein.
Immunohistochemistry: LS-B3699 was validated for use in immunohistochemistry on a panel of 21 formalin-fixed, paraffin-embedded (FFPE) human tissues after heat induced antigen retrieval in pH 6.0 citrate buffer. After incubation with the primary antibody, slides were incubated with biotinylated secondary antibody, followed by alkaline phosphatase-streptavidin and chromogen. The stained slides were evaluated by a pathologist to confirm staining specificity. The optimal working concentration for LS-B3699 was determined to be 10 ug/ml
PDIA3 Antibody, 58 kDa microsomal protein Antibody, ER protein 57 Antibody, ERp60 Antibody, ERp61 Antibody, Disulfide isomerase ER-60 Antibody, Endoplasmic reticulum P58 Antibody, GRP58 Antibody, HsT17083 Antibody, p58 Antibody, Phospholipase C-alpha Antibody, PI-PLC Antibody, ER protein 60 Antibody, ER60 Antibody, ERp57 Antibody, GRP57 Antibody, Protein disulfide-isomerase A3 Antibody
PDIA3 / ERp57 encodes a protein of the endoplasmic reticulum that interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. The protein was once thought to be a phospholipase; however, it has been demonstrated that the protein actually has protein disulfide isomerase activity. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.