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Human SIGIRR Protein, Fc Tag (MALS verified)

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SIR-H5255-100ug
$295.00
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SIR-H5255-1mg
$2,040.00
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SIR-H5255
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Product Details
Performance Data
Reviews & Citations
Resources
  • Product Details
  • Performance Data
  • Reviews & Citations
  • Important Statement
  • Resources
Synonyms

Single Ig IL-1-related receptor, Single Ig IL-1R-related molecule, Single immunoglobulin domain-containing IL1R-related protein, Toll, interleukin-1 receptor 8, TIR8

Source

Human SIGIRR, Fc Tag (SIR-H5255) is expressed from human 293 cells (HEK293). It contains AA Met 1 - His 118 (Accession # Q6IA17-1).

Predicted N-terminus: Met 1

Molecular Characterization
Other Tags and Version Biotin & Other Labeled Version

This protein carries a human IgG1 Fc tag at the C-terminus.

The protein has a calculated MW of 39.0 kDa. The protein migrates as 50-60 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

Endotoxin

Less than 1.0 EU per μg by the LAL method / rFC method.

Purity

>95% as determined by SDS-PAGE.

>95% as determined by SEC-MALS.

Formulation

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

Contact us for customized product form or formulation.

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.
ACRO Quality Management System

Background

Single immunoglobulin IL-1-related receptor (SIGIRR), which is also known as Toll/interleukin-1 receptor 8, is a member of the interleukin-1 receptor (IL-1R) family. SIGIRR acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP.