Human IL-1 RAcP / IL-1 R3 Protein, His Tag, low endotoxin (MALS verified)

Related Products: Cell line CHEK-ATF202 and CHEK-ATF244
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ILP-H52H4-100ug
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ILP-H52H4
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Synonyms

IL1RAP, IL-1RAcP, C3orf13, IL1R3

Source

Human IL-1 RAcP Protein, His Tag (ILP-H52H4) is expressed from human 293 cells (HEK293). It contains AA Ser 21 - Thr 367 (Accession # Q9NPH3-1).

Predicted N-terminus: Ser 21

Molecular Characterization

This protein carries a polyhistidine tag at the C-terminus.

The protein has a calculated MW of 41.7 kDa. The protein migrates as 55-70 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 0.01 EU per μg by the LAL method / rFC method.

Purity

>90% as determined by SDS-PAGE.

>90% as determined by SEC-MALS.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.

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Reconstitution

Please see Certificate of Analysis for specific instructions.

For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

Shipping and Storage

This product is shipped at ambient temperature.

For long term storage, the product should be stored at lyophilized state at -20°C or lower.

Please avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • -20°C to -70°C for 12 months in lyophilized state;
  • -70°C for 3 months under sterile conditions after reconstitution.

Background

Interleukin-1 receptor accessory protein (IL1RAP or IL-1RAcP) is also known as Interleukin-1 receptor 3 (IL-1R-3 or IL-1R3), C3orf13, which belongs to the interleukin-1 receptor family. IL1RAP contains three Ig-like C2-type (immunoglobulin-like) domains and one TIR domain. IL1RAP is detected in liver, skin, placenta, thymus and lung. IL-1R3 / IL1RAP is coreceptor with IL1R1, associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways.