Recombinant Mouse IL2 Protein

Name: Recombinant Mouse IL2 Protein
Brand: Beta LifeScience
SKU: BLPSN-2805
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Cytokines and growth factors, Interleukins and receptors, Recombinant interleukin-2 (il-2) proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Mouse
Accession	P04351
Synonym	Il-2
Background	Interleukin-2, also known as T-cell growth factor, TCGF, Aldesleukin and IL2, is a secreted protein which belongs to theIL-2 family. Interleukin-2 / IL-2 was the first interleukin molecule to be discovered. Interleukin-2 / IL-2 molecule was first purified to homogeneity by immunoaffinity chromatography by Kendall Smith and his team at Dartmouth Medical School. Interleukin-2 / IL-2 was also the first cytokine shown to mediate its effects via a specific IL-2 receptor, and it was also the first interleukin to be cloned and expressed from a complementary DNA (cDNA) library. Interleukin-2 / IL-2 was designated number 2 because Smith's data at the time indicated that IL-1, produced bymacrophages, facilitates IL-2 production by T lymphocytes (T cells). Interleukin-2 / IL-2 is produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Interleukin-2 / IL-2 is normally produced by the body during an immune response. When environmental substances (molecules or microbes) gain access to the body, these substances (termed antigens) are recognized as foreign by antigen receptors that are expressed on the surface of lymphocytes. Antigen binding to the T cell receptor (TCR) stimulates the secretion of Interleukin-2 / IL-2, and the expression of IL-2 receptors IL-2R. The IL-2 / IL-2R interaction then stimulates the growth, differentiation and survival of antigen-selected cytotoxic T cells via the activation of the expression of specific genes. Interleukin-2 / IL-2 can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells. The World Reference Standard for Interleukin-2 / IL-2 is produced by the National Institute of Biological Standards and Control in the UK. A recombinant form of Interleukin-2 / IL-2 for clinical use is manufactured by Chiron Corporation with the brand name Proleukin. It has been approved by the Food and Drug Administration (FDA) for the treatment of cancers (malignant melanoma, renal cell cancer), and is in clinical trials for the treatment of chronic viral infections, and as a booster (adjuvant) for vaccines. The use of Interleukin-2 / IL-2 in HIV therapy has been found to be ineffective.Immune CheckpointImmunotherapyCancer ImmunotherapyTargeted Therapy
Description	A DNA sequence encoding the soluble form of mouse IL2 (P04351) (Ala 21-Gln 169) was expressed, with an initial Met at the C-terminus.
Source	E.coli
Predicted N Terminal	Met
AA Sequence	Ala 21-Gln 169
Molecular Weight	The recombinant mouse IL2 consists of 150 a.a. and has a calculated molecular mass of 17.4KDa. It migrates as an approximately 19 kDa in SDS-PAGE under reducing conditions.
Purity	>92% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	1. Measured by its ability to bind recombinant human IL2Ra-Fc in a functional ELISA.2. Measured in a cell proliferation assay using CTLL2. The ED50 for this effect is typically 0.2-1.0 ng/mL.
Formulation	Lyophilized from sterile PBS, 2mM DTT, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the 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.

Target Details

Target Function	Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells.
Subcellular Location	Secreted.
Protein Families	IL-2 family
Database References	KEGG: mmu:16183 STRING: 10090.ENSMUSP00000029275 UniGene: Mm.14190

Gene Functions References

These studies demonstrate that Th1 CD4(+) T cells require IL-2 for lung T resident memory cell development. PMID: 28948612
Because IL-2 production was limited to cells receiving the strongest T cell receptor (TCR) signals, a direct link between TCR-signal strength, IL-2 production, and T cell fate determination has been established. PMID: 30213884
These data highlights the existence of IL-2 trans-presentation between NK cells in the local microenvironment where the availability of IL-2 is limited. PMID: 28074895
interleukin-2 (IL-2) is a non-pancreatic autoimmune target in type 1 diabetes PMID: 27708334
Each mutation decreased STAT5 binding and altered IL-2-induced Il2ra gene expression, revealing that individual elements within the superenhancer were not functionally redundant and that all were required for normal gene expression. PMID: 29078395
Deleting IL-2 in CD11c(high)MHCII(+) cells induces spontaneous colitis resembling human inflammatory bowel disease. PMID: 29549257
a significant increase in plasma levels of IL-2, IFN-g and TNF-g was revealed as assessed by ELISA. In conclusion, the results of the present study indicate that MENK has a cytotoxic effect on B16 melanoma cells in vitro and in vivo, and suggest a potential mechanism for these bioactivities. PMID: 28849104
WASp knockout mice controlled growth of A20 lymphoma cells that naturally produced IL-2. PMID: 27477778
Tumor growth delays observed by tumor irradiation combined with MVA-MUC1-IL-2 vaccine were significantly more prolonged than those observed by vaccine, radiation, or radiation with MVA empty vector. PMID: 28116088
IL-2 signalling is essential to prevent deletion of CD4SP CCR7+ Helios+ thymocytes at a later developmental stage than Card11 is required to prevent deletion. The deletion prevented by IL-2 signalling occurs in a Foxp3-independent manner. PMID: 28362433
in vivo targeting of the TNF superfamily receptor TNFRSF25 using the TL1A-Ig fusion protein, along with IL-2, resulted in transient but massive Treg expansion in donor mice; transplantation of Treg-expanded donor cells facilitated transplant tolerance without GVHD, with complete sparing of graft-versus-malignancy. PMID: 28219835
IL-2 and IL-6 work together to enhance influenza-specific CD8 T cell generation responding to live influenza virus in aged mice and humans PMID: 27322555
this report, we elucidated the unsolved mechanism of the anti-cancer effect of curcumin by identifying IL-2 as a direct molecular target. Curcumin, as a small molecule IL-2 modulator, has the potential to be used to treat IL-2 related pathologic conditions. PMID: 29127008
Data show that PTEN plays a key role in Th17 cell differentiation by blocking IL-2 expression. PMID: 29018045
AnxA6 regulates IL-2 homeostasis and sensitivity in T cells by sustaining a lipid raft-like membrane environment. PMID: 26853809
NOD Treg cells have an impaired responsiveness to IL-2 that reduces their ability to compete for a limited supply of IL-2. PMID: 26763864
Suppression of IL-12p70 formation by IL-2 or following macrophage depletion causes T-cell autoreactivity leading to CNS demyelination in HSV-1-infected mice. PMID: 28542613
At single cell level, IL-2 is binary (digital) and CD25 is graded expressed, whereas at population level both parameters show graded expression correlating with the antigen amount. PMID: 28035902
IL-2/anti-IL-2 complexes protected lupus-prone mice against lupus nephritis by expanding Tregs. PMID: 27914701
results show that IL-23 accounts for the main aspects of human and murine lupus including the expansion of double negative T cells, decreased IL-2, and increased IL-17 production PMID: 28646040
studies revealed a new epigenetic pathway in the control of IL-2 production in systemic lupus erythematosus whereby low levels of miR-200a-3p accumulate the binding of the ZEB1-CtBP2 complex to the IL-2 promoter and suppress IL-2 production PMID: 28438897
data suggest that the use of Golgi transport inhibitors results in an underestimation of the presence of type 2 cytokine-secreting cells and highlight IL-2 as a critical component in optimal cytokine production by Th2 and Th9 cells in vitro and in vivo PMID: 28468971
These results suggested that TSC-22 could counteract the protective effect of GILZ on IL-2-deprivation-induced apoptosis. PMID: 26752201
this study shows that IL-2 modulates the TCR signaling threshold for CD8 but not CD4 T cell Proliferation on a single-cell level PMID: 28159902
These data demonstrate an important synergetic role of TGF-beta and IL-2 in the generation, activation and stability of Treg cells, as well as their subsequent development into follicular regulatory T cells. PMID: 27787514
Mecamylamine, a nAChR inhibitor, suppressed not only these [Ca(2+)]i transients, but also IL-2 release and T cell proliferation PMID: 28025040
Flavonoid glycosides of Alchornea floribunda did not result in detectable Il2 secretion by treated splenic T-lymphocytes. PMID: 26974045
We also discuss the role of interleukin 2 (IL-2), which is decisive for the function of Treg and has been used therapeutically in preliminary trials in human SLE. The identification of novel Treg markers and the development of novel therapeutic approaches, which restore the balance between Treg and autoreactive Tcells are future goals for research in SLE. PMID: 26975190
Data show that after tumor necrosis factor alpha-induced protein 8 like-2 (TIPE2) gene was down-regulated, the expression of the CD69 antigen was increased, and the proliferation of T lymphocytes and the secretion of cytokines IL-2 and IFN-gamma were enhanced. PMID: 27363266
This study evaluated a chemical genetic toolkit that evaluated a biphasic requirement for JAK3 kinase activity in IL-2-driven T cell proliferation. PMID: 27018889
Dominance of regulatory T cells in carcinogen-induced fibrosarcomas is not T-bet or Il-2 dependent. PMID: 26433463
TCF1 is required for the T follicular helper cell response to viral infection functioning through negative feedback loops with IL-2 and Blimp1. PMID: 26365183
These results may provide an additional understanding of the characteristics of the various fractions of isolated Tregs based on phenotype and function and the role of varying levels of exogenous IL-2 on the suppressive activity of these cells. PMID: 26529512
findings demonstrate that distinct niches within the lymphoid organ T zone support distinct cell fate decisions, and they establish a function for dendritic-cell-derived CD25 in controlling IL-2 availability and T-cell differentiation PMID: 27147029
IL-2 signaling modulates TH1 cell, follicular helper T cell and central memory T cell gene expression. PMID: 26743592
Ndrg1 is a T-cell clonal anergy factor negatively regulated by IL-2. PMID: 26507712
Innate cell-derived IL-2 is a critical cofactor in regulating innate lymphoid cell function in pulmonary type 2 pathology PMID: 26025126
glucosamine interferes with N-glycosylation of CD25, and thereby attenuates IL-2 downstream signaling PMID: 26468284
Interleukin-2 critically regulates bone marrow erythropoiesis and prevents anemia development. PMID: 26404745
findings identified that autocrine IL-2 production operates in a dose-dependent fashion to facilitate the expansion potential of Ag-specific CD8(+) T cell populations, which may instigate ways to augment therapies depending on fit CD8(+) T cells. PMID: 26453748
IL-2-mediated activation of the Akt kinase and mTORc1 signaling was both necessary and sufficient to shift differentiation away from Tfh cells, instead promoting that of Th1 cells. PMID: 26410627
This study identified a novel long-range enhancer of the Il2 gene located 83 kb upstream of the transcription start site. PMID: 26351138
The amelioration by Gl-PS against the suppression of the production of IL-2, IFN-gamma and TNF-alpha in mononuclear lymphocytes by B16F10 cell culture supernatant might contribute to cancer control. PMID: 25585987
Late IL-2 promotes survival through acute downregulation of apoptotic pathways in effector T cells and by permanently upregulating their IL-7 receptor expression, enabling IL-7 to sustain them as memory T cells. PMID: 25369785
enhances anti-CD45RBmAb-induced immune tolerance to skin allograft via up-regulated T regulatory cells PMID: 25550088
Chronodependent effect of interleukin-2 on mouse spleen cells in the model of cyclophosphamide immunosuppression. PMID: 25708328
Peripherally Induced Tolerance Depends on Peripheral Regulatory T Cells That Require Hopx To Inhibit Intrinsic IL-2 Expression. PMID: 26170384
The morphologic changes and rapid cell death induced by dimeric IL-2 imply that cell death is mediated by disruption of membrane permeability and subsequent necrosis. PMID: 25019288
autocrine IL-2 signaling is functional in GM-CSF myeloid dendritic cells in an early time window after PAMPs stimulation PMID: 25652593
IL-2 produced by antigen-bearing dendritic cells (DCs) had a key role in Treg cell development and that existing Treg cells limited new development of Treg cells by competing for IL-2. PMID: 25939026

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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.

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