Recombinant Human IL-2 Protein, Active

Beta LifeScience SKU/CAT #: BEP-0040

Recombinant Human IL-2 Protein, Active

Beta LifeScience SKU/CAT #: BEP-0040
Regular price $311.00
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Product Overview

Product Name Recombinant Human IL-2 Protein
Target Symbol IL2
Alternative Names Interleukin 2, IL2, T Cell Growth Factor, TCGF, Aldesleukin, Lymphokine
Accession Number P60568
Expression System E.Coli.
Purity Determined by SDS-PAGE and quantitative densitometry by Coomassie® Blue staining
Activity Determined by in-house activity assay
Formulation Lyophilized from sterile PBS with Trehalose, pH 7.4
Endotoxin Level Available Upon Request
Shipping Shipped at ambient temperature.
Stability & Storage 12 months from date of receipt at -20°C to -70°C, lyophilized powder. 3 months at -20°C to -70°C under sterile conditions after reconstitution. Avoid repeated freeze-thaw cycles.
Reconstitution Reconstitute at 100 ug/mL in sterile PBS.
Target Function Interleukin-2 (IL-2) is a cytokine primarily produced by T cells and plays a critical role in the proliferation of T cells through paracrine and autocrine activity. It further regulates immune response through promoting the differentiation of T cells into various subsets such as effector Th17 cells or regulatory T (Treg) cells. IL-2 also promotes the differentiation and stimulation of B cell and NK cell populations. The receptor for IL-2 is a heterotrimeric complex composed of IL-2 R alpha (CD25), IL-2 R beta (CD122) and IL-2 R gamma (also named, common gamma chain or CD132). IL-2 has garnered interest in cancer immunotherapy and adoptive cell therapy (ACT) where research techniques in cell culture have included IL-2 to support the expansion and survival of modified T cells in chimeric antigen receptor (CAR) T cell therapy, tumor-infiltrating lymphocyte (TIL) therapy and NK cells.
Tissue Specificity IL-2 expression has been identified in lymph node, spleen, and brain.
Cellular Localization Secreted protein
Involvement In Disease IL-2 dysregulation is implicated in autoimmune disorders (rheumatoid arthritis, multiple sclerosis, and type 1 diabetes), allergic asthma, allergic rhinitis, and inflammatory bowel disease (IBD).

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.

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