Recombinant Cynomolgus CTLA-4 Protein (His Tag)

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Co-inhibitory receptors, Featured immune checkpoint protein molecules, Immune checkpoint proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Cynomolgus
Accession	Q9BDC4
Synonym	GSE, CD152, IDDM12, CELIAC3, CTLA-4.
Background	CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.
Description	A DNA sequence encoding the cynomolgus CTLA4 (Q9BDC4) (Met1-Asp161) was produced with a His tag at the C-terminus.
Source	HEK293
Predicted N Terminal	Ala 37
AA Sequence	Met1-Asp161
Molecular Weight	The recombinant cynomolgus CTLA4 comprises 136 amino acids and has a calculated molecular mass of 14.9 KDa. The apparent molecular mass of it is approximately 24 and 21 KDa respectively in SDS-PAGE.
Purity	(73.4+23.7)% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Immobilized Cynomolgus CTLA4-His at 10 ug/ml (100 ul/well) can bind Cynomolgus CD80-Fc, The EC50 of Cynomolgus CD80-Fc is 0.02-0.04 ug/ml.
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	Recombinnat Proteins are stable for up to 1 year from date of receipt at -70°C
Usage	For Research Use Only
Storage	Store recombinant protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.