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".
AMBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (20-203) and having a molecular mass of 23.1 kDa.AMBP is fused to a 21 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Greater than 90% by SDS-PAGE
20 mM Tris-HCl, pH 8.0, 20 mM DTT, 20 mM NaCl, 10% glycerol.
Store lyophilized at 4°C. Once reconstituted, aliquot and store at -20°C. Avoid freeze-thaw cycles.
AMBP Protein, A1M Protein, Alpha-1-microglobulin Protein, Bikunin Protein, HCP Protein, IATIL Protein, ITIL Protein, HI30 Protein, ITI Protein, ITILC Protein, Protein AMBP Protein, Uronic-acid-rich protein Protein, UTI Protein, Trypstatin Protein, Uristatin Protein, EDC1 Protein, Growth-inhibiting protein 19 Protein, Protein HC Protein
Bikunin / AMBP is a complex glycoprotein secreted in plasma. The precursor is proteolytically processed into distinct functioning proteins: alpha-1-microglobulin, which belongs to the superfamily of lipocalin transport proteins and may play a role in the regulation of inflammatory processes, and bikunin, which is a urinary trypsin inhibitor belonging to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes.