protein

IL-1 alpha Protein, Human (HEK293, Fc)

HY-P700290

10 μg;50 μg

150;420 USD

IL-1 alpha Protein, Human (HEK293, Fc)

proteins

HEK293

10 μg;50 μg

150;420 USD

IL-1 alpha protein is located in cells and is a key cytokine connecting innate immunity and adaptive immunity. After binding to IL1R1 through IL1RAP, it forms a high-affinity receptor complex, initiates a signaling cascade with adapter molecules such as MYD88, IRAK1 or IRAK4, and activates the NF-kappa-B and MAPK pathways. IL-1 alpha Protein, Human (HEK293, Fc) is the recombinant human-derived IL-1 alpha protein, expressed by HEK293 , with C-hFc labeled tag. The total length of IL-1 alpha Protein, Human (HEK293, Fc) is 159 a.a., with molecular weight of 54 kDa.

Human

Interleukin-1 alpha (IL-1 alpha), a cytokine consistently found intracellularly in nearly all quiescent non-hematopoietic cells, plays a pivotal role in inflammation and serves as a crucial link between the innate and adaptive immune systems. Upon binding to its receptor IL1R1, in conjunction with its accessory protein IL1RAP, IL-1 alpha forms the high-affinity interleukin-1 receptor complex. This complex initiates signaling cascades involving the recruitment of adapter molecules such as MYD88, IRAK1, or IRAK4, subsequently leading to the activation of NF-kappa-B and the three MAPK pathways—p38, p42/p44, and JNK pathways. Intracellularly, IL-1 alpha acts as an alarmin, and its release into the extracellular space upon cell death, following cell membrane disruption, induces inflammation and signals the host response to injury or damage. Beyond its role as a danger signal released during cell necrosis, IL-1 alpha also directly senses DNA damage, serving as a signal for genotoxic stress without compromising cell integrity. Moreover, IL-1 alpha's interactions with proteins such as TMED10, IL1R1, and S100A13 contribute to its regulatory mechanisms, mediating translocation, secretion, and export processes.

Interleukin-1 Alpha; IL-1 Alpha; Hematopoietin-1; IL1A; IL1F1;

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, pH 7.5.

Room temperature in continental US;may vary elsewhere.