Artikelnummer: PKSH031479_100μg-ES

Recombinant Human CD122/IL-2RB Protein (Fc Tag), 100 μg

Interleukin-2 receptor (IL-2R) also known as High affinity IL-2 receptor subunit beta, IL-2 receptor subunit beta, and IL-2RB, is involved in T cell-mediated immune responses. CD122/IL-2RB is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit and is not involved in signal transduction. The intermediate affinity form consists of an alpha/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of CD122/IL-2RB are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. CD122/IL-2RB expression was restricted to the earliest B220+ cells (CD43+CD24-; prepro B cells; fraction A) that proliferate vigorously to IL-2 in the absence of any stromal cells, but not to IL-15. The high-affinity form of this receptor is expressed on activated T lymphocytes, activated B lymphocytes, and activated macrophages. CD122/IL-2RB plays a role in regulating normal lymphocyte development.

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Grundlegende Informationen

Marken: Elabscience

Versand: This product is provided as lyophilized powder which is shipped with ice packs.

Speicher: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

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Herkunftsort: China

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Calculated Molecular Weight:51.6 kDa

Observed Molecular Weight:60-65 kDa

Purity: > 90 % as determined by reducing SDS-PAGE.

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Storage:Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

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Calculated Molecular Weight:51.6 kDa

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Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.

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Reinheit: > 90 % as determined by reducing SDS-PAGE.

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