IL2RA
Origine: Humain
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
ELISA
IL2RA
Origine: Souris
Hôte: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
IL2RA
Origine: Humain
Hôte: Human Cells
Recombinant
> 95 % as determined by reducing SDS-PAGE.
Active
Restrictions
For Research Use only
Format
Lyophilized
Buffer
Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization.
Stock
-20 °C,-80 °C
Stockage commentaire
Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.
The interleukin 2 (IL2) receptor alpha (IL2RA) and beta (IL2RB) chains, together with the common gamma chain (IL2RG), constitute the high-affinity IL2 receptor. Homodimeric alpha chains (IL2RA) result in low-affinity receptor, while homodimeric beta (IL2RB) chains produce a medium-affinity receptor. Normally an integral-membrane protein, soluble IL2RA has been isolated and determined to result from extracellular proteolyisis. Alternately-spliced IL2RA mRNAs have been isolated, but the significance of each is presently unknown. Mutations in this gene are associated with interleukin 2 receptor alpha deficiency.
Poids moléculaire
predicted molecular mass of 22.6 kDa after removal of the signal peptide.The apparent molecular mass of IL2RA-His is 35-55 kDa due to glycosylation.