Recombinant Anti-IL2 Antibody, Rabbit Monoclonal

EliteRmab®, manufactured by recombinant technology
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Recombinant Anti-IL2 Antibody, Rabbit Monoclonal General Information

Product name
Recombinant Anti-IL2 Antibody, Rabbit Monoclonal
Validated applications
ELISA
Species reactivity
Reacts with: Canine
Specificity
Canine IL2
Immunogen
Recombinant Canine IL-2 Protein (Catalog#70014-DNAE)
Preparation
This antibody was obtained from a rabbit immunized with purified, recombinant Canine IL-2 (Catalog#70014-DNAE; Q29416; Ala21-Thr155,147Cys/Ser).
Source
Monoclonal Rabbit IgG Clone #001
Purification
Protein A
Formulation
0.2 μm filtered solution in PBS
Conjugate
Unconjugated
Form
Liquid
Shipping
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Storage
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Recombinant Anti-IL2 Antibody, Rabbit Monoclonal Validated Applications

Application Dilution
ELISA 1:5000-1:10000
Please Note: Optimal concentrations/dilutions should be determined by the end user.

IL2 Background Information

Interleukin-2, also known as a T-cell growth factor, TCGF, Aldesleukin, and IL2, is a secreted protein that belongs to the IL-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 by macrophages, 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 is ineffective.
Full Name
interleukin 2
Research Areas
Related Pathways
  • Common G-Chain signaling pathway
    Common G-Chain signaling pathway
References
  • Smith KA, et al.,1980,  J. Exp. Med.151 (6): 1551-6. 
  • Smith KA, et al.,1980, Nature. 287 (5785): 853-5.
  • Taniguchi T, et al.,1983, Nature. 302 (5906): 305.
  • Cantrell DA, et al.,1984, Science. 224 (4655): 1312-6. 
  • Smith KA, et al.,1988, Science. 240 (4856): 1169-76.
  • Wang X. et al., 2005, Science 310:1159-63.
  • Stauber D.J. et al., 2006, Proc. Natl. Acad. Sci. USA. 103: 2788-93.

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