Recombinant Human IL-1 alpha/IL1A protein

Specifications

Form

Lyophilized

General info

Function

Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed : 26439902). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex (PubMed : 17507369, PubMed : 2950091). Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4 (PubMed : 17507369). In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed : 14687581). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage (PubMed : 15679580). In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (PubMed : 26439902).

Sequence similarities

Belongs to the IL-1 family.

Post-translational modifications

Acetylated within its nuclear localization sequence, which impacts subcellular localization.. Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules.. Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A.