Compositions, methods, articles of manufacture, and kits are provided for storage and delivery of proteins.

Provided herein are methods for refolding denatured protein (e.g., from inclusion bodies) that do not require the use of a denaturing agent. Exemplary methods use a high pH for solubilizing denatured protein, followed by a decrease in pH for refolding the proteins.

Processes are provided for recovering and purifying refolded recombinant proteins produced in heterologous host cells, which includes the step of refolding the protein in a high pH buffer.

Provided is a method of refolding of recombinant GCSF that minimizes the generation of oxidized forms of GCSF by optimizing the refolding of inclusion bodies containing recombinant GCSF.

One subject of the present invention is the use of a combination of a polyol (i) consisting of 12 carbon atoms and of a polyol (ii) consisting of 4 to 6 carbon atoms, as protein stabilizer. Another subject of the present invention is protein compositions comprising such a combination. A final subject of the present invention is a process for preparing protein compositions using such a combination.

The present invention provides method of increasing the percentage of monomer in a composition of recombinantly expressed antibody molecules characterised in that the antibody molecule comprises at least one Fv with specificity for an antigen of interest comprising one VH and one VL wherein said VH and VL are connected directly or indirectly via one or more linkers and are stabilised by a disulfide bond therebetween, said method comprises: a) a conversion step of treating the composition with a denaturant selected from urea and/or Guanidine hydrochloride; b) wherein step a) is performed in the presence of a reducing agent or after treatment with a reducing agent.

Provided is a method of treating a protein to be renatured, including: (1) mixing the protein to be renatured with a denaturing solution containing a denaturing reagent; (2) incubating a resulting mixture at such a low temperature that the denaturing agent is gradually precipitated from the denaturing solution, resulting in a decreasing concentration gradient of the denaturing agent and an increasing concentration of a renatured protein or its precursor in the denaturing solution with a decreasing volume; and (3) obtaining at least one of the renatured protein and its precursor.

A preparing a purified population of single chain Mycobacterium smegmatis porins.

Provided herein are charge complementary peptides that can be optionally coupled to a cargo polypeptide that are capable of self-assembling under stimulating conditions. The charge complementary peptides can be capable of forming supramolecular structures. Also provided herein are methods of using the charge complementary peptides provided herein.

The present invention provides methods of preparing active immunoconjugates, including anti-CD22 immunoconjugates. Suitably, the methods include a fed-batch refolding process and/or column stripping process that result in an increase in yield of the immunoconjugate over other processes that do not utilize the methods.