STING1 Protein, Mouse (Cell-Free, His)

STING1 is a promoter of innate immune signaling, a key sensor of bacterial and viral cytoplasmic DNA, and promotes the production of type I interferons (IFN-α and IFN-β). This innate immune response is triggered in response to non-CpG double-stranded DNA delivered to the cytoplasm from various pathogens. STING1 Protein, Mouse (Cell-Free, His) is the recombinant mouse-derived STING1 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of STING1 Protein, Mouse (Cell-Free, His) is 378 a.a., with molecular weight of 48.9 kDa.

STING1, a facilitator of innate immune signaling, serves as a critical sensor for cytosolic DNA from bacteria and viruses, promoting the production of type I interferon (IFN-alpha and IFN-beta). This innate immune response is triggered in response to non-CpG double-stranded DNA delivered to the cytoplasm from various pathogens. STING1 acts by binding cyclic dinucleotides, recognizing and binding cyclic di-GMP (c-di-GMP), a bacterial second messenger, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA viruses in the cytosol. Upon binding, STING1 oligomerizes, translocates from the endoplasmic reticulum, and is phosphorylated by TBK1, leading to the recruitment and activation of the transcription factor IRF3. This induction results in the expression of type I interferon, establishing a potent anti-viral state. STING1's versatile role extends to direct participation in autophagy, where cGAMP-binding triggers its movement from the endoplasmic reticulum to COPII vesicles, forming the endoplasmic reticulum-Golgi intermediate compartment (ERGIC). The ERGIC serves as the membrane source for autophagosome formation, facilitating the degradation of cytosolic DNA or DNA viruses by the lysosome. The autophagy and interferon-inducing activities of STING1 can be uncoupled, with autophagy induction being independent of TBK1 phosphorylation. Furthermore, STING1 exhibits a preference for 2'-3'-cGAMP and may be involved in translocon function, influencing the induction of type I interferons. Additionally, its association with the major histocompatibility complex class II suggests a potential role in transducing apoptotic signals. STING1 is activated by the anticancer drug 5,6-dimethylxanthenone 4-acetic acid (DMXAA) and specifically inhibited by nitrofuran derivatives C-178 and C-176, preventing palmitoylation and subsequent activation of STING1. The multifaceted activities of STING1 highlight its pivotal role in orchestrating innate immune responses, autophagic processes, and potential contributions to apoptotic signaling and anticancer responses.

Mouse

E. coli Cell-free

N-10*His

Q3TBT3 (M1-I378)

72512

MPYSNLHPAIPRPRGHRSKYVALIFLVASLMILWVAKDPPNHTLKYLALHLASHELGLLLKNLCCLAEELCHVQSRYQGSYWKAVRACLGCPIHCMAMILLSSYFYFLQNTADIYLSWMFGLLVLYKSLSMLLGLQSLTPAEVSAVCEEKKLNVAHGLAWSYYIGYLRLILPGLQARIRMFNQLHNNMLSGAGSRRLYILFPLDCGVPDNLSVVDPNIRFRDMLPQQNIDRAGIKNRVYSNSVYEILENGQPAGVCILEYATPLQTLFAMSQDAKAGFSREDRLEQAKLFCRTLEEILEDVPESRNNCRLIVYQEPTDGNSFSLSQEVLRHIRQEEKEEVTMNAPMTSVAPPPSVLSQEPRLLISGMDQPLPLRTDLI

45 kDa

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized powder

Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 0.15 M NaCl, 0.05% FOS12, 6% Trehalose, pH 8.0.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.