Recombinant Human IL-2 Protein, CF

Catalog #: BT-002 Datasheet / COA / SDS

Contains the Cysteine to Serine substitution found in Proleukin® (aldesleukin)

Catalog #	Availability	Size / Price	Qty
BT-002-010
BT-002-050
BT-002-100
BT-002-500
BT-002-01M

Recombinant Human IL‑2 Protein Bioactivity.

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human IL-2 Protein, CF Summary

Product Specifications

Purity

>97%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Endotoxin Level

<0.01 EU per 1 μg of the protein by the LAL method.

Activity

Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. Gearing, A.J.H. and C.B. Bird (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 295. The ED50 for this effect is 0.0300-0.250 ng/mL.

Source

E. coli-derived human IL-2 protein
Ala21-Thr153 (Cys145Ser), with and without an N-terminal Met

Accession #

P60568.1

N-terminal Sequence
Analysis

Ala21 & Met

Predicted Molecular Mass

15.5 kDa

SDS-PAGE

13 kDa, under reducing conditions.

Product Datasheets

BT-002

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

BT-002

Formulation	Lyophilized from a 0.2 μm filtered solution in Sodium Acetate with Trehalose.
Reconstitution	Reconstitute the 10 μg size at 100 μg/mL in sterile deionized water. Reconstitute all other sizes at 500 μg/mL in sterile deionized water.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70 °C as supplied. 1 month, 2 to 8 °C under sterile conditions after reconstitution. 3 months, -20 to -70 °C under sterile conditions after reconstitution.

Scientific Data

Bioactivity

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Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. The ED₅₀ for this effect is 0.0300-0.250 ng/mL.

Bioactivity

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Equivalent bioactivity of GMP (BT-002-GMP), Animal-Free (BT-002-AFL) and RUO (Catalog # BT-002) grades of Recombinant Human IL-2 as measured in a cell proliferation assay using CTLL-2 mouse cytotoxic T cells (orange, green, red, respectively).

SDS-PAGE

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2 μg/lane of Recombinant Human IL‑2 Protein (Catalog # BT-002) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 13 kDa.

Reconstitution Calculator

Background: IL-2

Recombinant Interleukin-2 (IL-2) is expressed in E. coli and has been engineered to contain the serine for cysteine substitution found in Proleukin^® (aldesleukin). Recombinant IL-2 is widely used in cell culture for the expansion of T cells. IL-2 is expressed by CD4+ and CD8+ T cells, gamma δ T cells, B cells, dendritic cells, and eosinophils (1-3). Mature human IL-2 shares 56% and 66% amino acid (aa) sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit cross-species activity (4). The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes (5-7). The 55 kDa IL-2 R alpha is specific for IL-2 and binds with low affinity. The 75 kDa IL-2 R beta, which is also a component of the IL-15 receptor, binds IL-2 with intermediate affinity. The 64 kDa common gamma chain gamma c/IL-2 R gamma, which is shared with the receptors for IL-4, -7, -9, -15, and -21, does not independently interact with IL-2. Upon ligand binding, signal transduction is performed by both IL-2 R beta and gamma c.

IL-2 is best known for its autocrine and paracrine activity on T cells. It drives resting T cells to proliferate and induces IL-2 and IL-2 R alpha synthesis (1, 2). It contributes to T cell homeostasis by promoting the Fas-induced death of naïve CD4+ T cells but not activated CD4+ memory lymphocytes (8). IL-2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17 polarized cells (9-11). Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity (12, 13).

IL-2 expression and concentration can have either immunostimulatory effects at high doses or immunosuppressive effects at low doses due to its preferential binding to different receptor subunits expressed by various immune cell types. This has led to the generation of recombinant IL-2 variants aimed at modifying IL-2 receptor binding for increased antitumor efficacy (14, 15). These variants are typically used in combination with immune checkpoint inhibitors instead of as a monotherapy (14). IL-2 can be genetically engineered to express in NK cells for CAR T cell therapies, and in combination with other cytokines like IL-15, can increase cell viability and proliferation (16). In addition to adoptive cell transfer and checkpoint blockade inhibitors, cancer vaccines that boost immune responses have been combined with IL-2 treatment with promising results in recent studies (15).

In cell culture, IL-2 is a frequently used cytokine for the proliferation, differentiation, and increased antibody secretion of B cells as they transform into plasma cells in vitro (17). IL-2 is also a classically used cytokine for the expansion of NK cells, early differentiated T cells and effector memory Treg cells for adoptive cell transfer cancer immunotherapy (16, 18). GMP IL-2 is a commonly used supplement for the expansion of these cell types for cellular therapies.

References

Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
Gaffen, S.L. and K.D. Liu (2004) Cytokine 28:109.
Taniguchi, T. et al. (1983) Nature 302:305.
Mosmann, T.R. et al. (1987) J. Immunol. 138:1813.
Liparoto, S.F. et al. (2002) Biochemistry 41:2543.
Wang, X. et al. (2005) Science 310:1159.
Bodnar, A. et al. (2008) Immunol. Lett. 116:117.
Jaleco, S. et al. (2003) J. Immunol. 171:61.
Malek, T.R. (2003) J. Leukoc. Biol. 74:961.
Laurence, A. et al. (2007) Immunity 26:371.
Kryczek, I. et al. (2007) J. Immunol. 178:6730.
Afzali, B. et al. (2007) Clin. Exp. Immunol. 148:32.
Fehervari, Z.et al. (2006) Trends Immunol. 27:109.
Xue, D. et al. (2021) Antib Ther. 4:123.
Wolfarth, A.A. et al. (2022) Immune Netw. 22:e5.
Koehl, U. et al. (2015) Oncoimmunology. 5:e1115178.
Marsman, C. et al. (2022) Front. In Immunol. 13:815449.
Chamucero-Millares, J.A. et al. (2021) Cellular Immunol. 360:104257.

Long Name

Interleukin 2

Entrez Gene IDs

3558 (Human); 16183 (Mouse); 116562 (Rat); 396868 (Porcine); 280822 (Bovine); 403989 (Canine); 100034204 (Equine); 751114 (Feline); 100302458 (Rabbit)

Alternate Names

Aldesleukin; IL2; IL-2; IL-2lymphokine; interleukin 2; interleukin-2; involved in regulation of T-cell clonal expansion; Proleukin; T cell growth factor; T-cell growth factor; TCGF