Recombinant human IL12RB1 protein with C-terminal human Fc tag
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Amount : | 50 µg |
Purification : | The purity of the protein is greater than 95% as determined by SDS-PAGE and Coomassie blue staining. |
Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
Alternative Name : | CD212,IL-12R-BETA1,IL12RB,IMD30 |
Expression Host : HEK293
The protein has a predicted molecular mass of 82.94 kDa after removal of the signal peptide.
The protein encoded by this gene is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukine 12 (IL12) with a low affinity, and is thought to be a part of IL12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL12 binding activity. The coexpression of this and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. Mutations in this gene impair the development of interleukin-17-producing T lymphocytes and result in increased susceptibility to mycobacterial and Salmonella infections. Alternative splicing results in multiple transcript variants.
The protein has a predicted molecular mass of 82.94 kDa after removal of the signal peptide.
The protein encoded by this gene is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. This protein binds to interleukine 12 (IL12) with a low affinity, and is thought to be a part of IL12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL12 binding activity. The coexpression of this and IL12RB2 proteins was shown to lead to the formation of high-affinity IL12 binding sites and reconstitution of IL12 dependent signaling. Mutations in this gene impair the development of interleukin-17-producing T lymphocytes and result in increased susceptibility to mycobacterial and Salmonella infections. Alternative splicing results in multiple transcript variants.
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