Commercially available Temperature Response Protein A resins:  Nomadic Byzen Pro

In General

Koguma (US13/996385; see also US application No. 14/408,458) discloses antibody purification using a temperature responsive protein A medium such that low pH treatment is avoided in the elution or any virus invactivation. This is disclosed as advantageous because damage to the antibody can be avoided and the antibody will have better binding affinity that conducting the protein A affinity using low pH treatment. (Koguma (j of chromatoraphy A1305 (2013) 149-153 disclsoes taht a mutant protein A (thermo-repsoive protein A) bound IgG at 5C and rlease it at 40C and that IgG was purified mainly as a monomer; the TRPA column showed almost a single monomer peak and a small shoulder peak. On the other hand, IgG purifed by a coventional column had several molecules species, possibly corresponding to aggregated IgG1. 

Sato (US2010/0168395 and WO2008/143199) discloses mutatns of Protein A based on the B domain of Protein A whose binding properties change based on temperature which enables immunoglobulines to be bound and washed in a low temperature range and then released in a higher tmerpature range due to the change in the structure on the Protein A. This is advantageous because it enables the antibody to be extracted while the pH is kept at neutral. In other words, one does not need to use a low pH to elute the antibody, a change in temperature can accomplish this goal. 

Conditions:

Elution additives:

Kawooya (US 16/093,994, published as US 2019/0127418) disclsoes a method of purifying an IgG-svFv binding protein using a temrpature senstive Protein A resin where the elution buffer contained /75M NaCL, 0.5 M argine, 05 M proline, 2.2 M sorbitol and 4M urea at pH 7.2

Linkers/Spacers/Graft Chains for Temperature Sensitive Mutants

Kazuo (US 14/410616) discloses a temeprature sensitive mutant based on the B domain derived from protein A which includes a linker sequence having an amino acid sequence that does not comprise a Val-Pro-Arg sequence and is composed of 7-12 amino acid residues. In one embodiment the linker is Ser-Ser-Gly-(Xaa)-Met wherein n represent and interger 3-8 and an n number of Xaa each independently represents a glycine, serine, histidine, leucine or arginine. In another emobdiment the linker is Ser-Ser-Gly-Leu-(Xbb)m-His-Met wherein m represents an interger 1-6 and and an m number of Xbb each idenpendently represents a glycine, serine or arginine residue.