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Recombinant Mouse SIGIRR Fc Chimera Protein, CF  100 UG图1

Recombinant Mouse SIGIRR Fc Chimera Protein, CF 100 UG

2024-11-24 19:55IP属地 广东省东莞市 电信00留言

992-SG

 

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.


Reconstitution Reconstitute at 100 μg/mL in sterile PBS.



Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.


Stability & Storage:       Use a manual defrost freezer and avoid repeated freeze-thaw cycles.      

  • 12 months from date of receipt, -20 to -70 °C as supplied.

  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.

  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.


Background: SIGIRR

The Interleukin 1 receptor family (IL-1 R) comprises at least eleven members including IL-1 RI (IL-1 R1), IL-1 RII (IL-1 R2), IL-1 RAcP (IL‑1 R3), ST2 (T1/IL-1 R4), IL-18 Ra (IL-1 Rrp/IL-1 R5), IL-1 Rrp2 (IL-1 RL2/IL-1 R6), IL-18 Rb (AcPL/IL-1 R7), IL-1RAPL‑1 (TIGIRR‑2/IL‑1 R8), and TIGIRR-1 (IL-1 R9) (1). All family members possess three immunoglobulin (Ig)-like domains in their extracellular region. Most members have an intracellular TIR (Toll-like receptor/IL-1 receptor signaling) domain that is also conserved in the Toll-like receptor family. Five of the IL-1 R family members (1, 2, 4, 5, and 6) are clustered and localized to chromosome 2. SIGIRR (single Ig domain containing IL-1 receptor-related molecule) is a subtype of the IL-1 R family that differs from the other nine members by having only one Ig domain in its extracellular region. The sequence of mouse SIGIRR predicts a 409 amino acid (aa) residue transmembrane glycoprotein that lacks signal peptide and contains a 117 aa single Ig extracellular domain, a transmembrane region and a 268 aa cytoplasmic tail with a TIR domain. The cytoplasmic tail of SIGIRR contains a C-terminal extention beyond the TIR domain which is also found in IL-1 R8, IL-1 R9, and Toll-like receptor family members but absent in other IL-1 receptor family members. SIGIRR is widely expressed and is present in all cells and tissues examined. Mouse and human SIGIRR share 82% amino acid sequence identity. The ligand and signaling mechanism for SIGIRR has not been identified.

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