The present application relates to antibodies that bind to small molecules such as cyclophosphamide, ifosfamide, and analogs thereof, and immunological assays for determining the presence and/or quantifying the amount of cyclophosphamide and/or ifosfamide in a sample. By way of example, such immunological assays can be used for environmental testing.

The present disclosure provides modified proteins that are capable of being cleaved by the protease OmpT1. The proteins can be modified in an exposed surface motif to incorporate OmpT1 cleavage sites. Also provided are nucleic acids encoding the modified proteins, bacterial cells that express the modified proteins, and cell free synthesis systems containing modified RF1. The disclosure further provides methods for reducing the deleterious activity of a modified protein in a cell free synthesis system by contacting the modified protein with OmpT1. Also provided are methods for reducing RF1 competition at an amber codon in the cell free synthesis system, and methods for expressing a protein in the cell free synthesis system. The modified proteins of the invention can be used to increase the yield of proteins having non-natural amino acids incorporated at an amber codon.

Provided herein are high affinity antibodies or antigen binding fragments thereof that specifically bind to human tau-pS413. Also provided are compositions, kits, methods, and uses involving such antibodies or antigen binding fragments thereof.

The present invention provides a method for treating human immunodeficiency virus (HIV)-associated enteropathy in subjects who have been on antiretroviral therapy by orally administering immunoglobulin/protein isolate.

The present invention provides a method for treating human immunodeficiency virus (HIV)-associated enteropathy in subjects who have been on antiretroviral therapy by orally administering immunoglobulin/protein isolate.

The invention provides a process of purification of antibody or fusion protein from protein mixture comprising product and process related impurities. The process provides the use of hydroxyapatite chromatography for the separation of low molecular weight impurities and basic variants. In addition, invention further provides a scalable purification process to remove product and process related impurities.

A process for purification of antibody or fusion protein through anion exchange chromatography to produce an antibody or fusion protein which is substantially free of at least one of the product-related impurities.

A process for purification of antibody or fusion protein by affinity chromatography wherein the elution is performed with high salt concentration which reduce turbidity in protein mixture during neutralization steps. The present invention provides an improved process of purifying antibodies through affinity chromatography using high salt-based elution.

The present invention relates to compositions comprising erenumab and one or more erenumab variants, including isomerization variants, deamidation variants, acidic variants, and HMW species. Pharmaceutical formulations comprising the erenumab compositions and methods of using and characterizing the compositions are also described.

In certain embodiments, the invention provides a method of purifying a protein of interest from a mixture which comprises the protein of interest and one or more contaminants, comprising: a) subjecting the mixture to a first chromatography step; b) recovering the protein of interest in an elution solution; c) adding caprylic acid to the elution solution to form a contaminant precipitate; d) removing the contaminant precipitate from the elution solution; and e) subjecting the post-precipitated elution solution to a second chromatography column, thereby purifying the protein of interest.