IL-1 alpha Protein, Cynomolgus (HEK293, His)

IL-1 alpha, found in non-hematopoietic cells, connects innate and adaptive immunity. Binding to IL1R1, it activates signaling pathways involving MYD88, IRAK1, and IRAK4, leading to NF-kappa-B and MAPK pathway activation. Released during cell death, IL-1 alpha induces inflammation, senses DNA damage, and interacts with TMED10, IL1R1, and S100A13 for secretion and plasma membrane translocation. IL-1 alpha Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived IL-1 alpha protein, expressed by HEK293 , with C-His labeled tag.

IL-1 alpha, a cytokine consistently present intracellularly in nearly all quiescent non-hematopoietic cells, serves a crucial role in inflammation and acts as a nexus between the innate and adaptive immune systems. Upon binding to its receptor IL1R1, accompanied by its accessory protein IL1RAP, IL-1 alpha forms the high-affinity interleukin-1 receptor complex, initiating signaling cascades that recruit adapter molecules like MYD88, IRAK1, or IRAK4. Consequently, it mediates the activation of NF-kappa-B and three MAPK pathways—p38, p42/p44, and JNK pathways. Functioning as an alarmin within the cell, IL-1 alpha is liberated into the extracellular space upon cell death, induced by disruption of the cell membrane, thereby triggering inflammation and alerting the host to injury or damage. Beyond its role as a danger signal during passive release through cell necrosis, IL-1 alpha directly senses DNA damage, acting as a signal for genotoxic stress without compromising cell integrity. Present as a monomer, IL-1 alpha interacts with TMED10, facilitating its translocation from the cytoplasm into the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) for secretion. It also interacts with IL1R1 and S100A13, the latter marking the initial step in IL-1 alpha export, followed by the direct translocation of this complex across the plasma membrane.

Cynomolgus

HEK293

C-8*His

P79340 (S113-A271)

101926546  [NCBI]

Full Length of Mature Protein

SAPFSFLSNMTYHFIRIIKHEFILNDTLNQTIIRANDQYLTAAAIHNLDEAVKFDMGAYTSSKDDTKVPVILRISKTQLYVSAQDEDQPVLLKEMPEIPKTITGSETNFLFFWETHGTKNYFISVAHPNLFIATKHDNWVCLAKGLPSITDFQILENQA

Approximately 25-35 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.

<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 from date of receipt. 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.