IL-1 alpha is a member of the interleukin 1 cytokine family. Cytokines are proteinaceous signaling compounds that are major mediators of the immune response. They control many different cellular functions including proliferation, differentiation, and cell survival/apoptosis but are also involved in several pathophysiological processes including viral infections and autoimmune diseases. Cytokines are synthesized under various stimuli by a variety of cells of both the innate (monocytes, macrophages, dendritic cells) and adaptive (T- and B-cells) immune systems. Cytokines can be classified into two groups: pro- and anti-inflammatory. Pro-inflammatory cytokines, including IFNgamma, IL-1, IL-6, and TNF-alpha, are predominantly derived from the innate immune cells and Th1 cells. Anti-inflammatory cytokines, including IL-10, IL-4, IL-13, and IL-5, are synthesized from Th2 immune cells. IL-1 alpha is a pleiotropic cytokine involved in various immune responses, inflammatory processes, and hematopoiesis. It is produced by monocytes and macrophages as a proprotein, which is proteolytically processed and released in response to cell injury, and thus induces apoptosis. IL-1 alpha stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity.

The interleukin (IL)-1 family of cytokines is currently comprised of 11 members that have pleiotropic functions in inflammation and cancer. IL-1α and IL-1β were the first members of the IL-1 family to be described, and both signal via the same receptor, IL-1R. Over the last decade, much progress has been made in our understanding of biogenesis of IL-1β and its functions in human diseases.

IL-36 alpha/IL-1F6 Protein, Mouse, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 18 kDa and the accession number is Q9JLA2-1.

IL-1 beta/IL-1F2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 32.3 kDa and the accession number is P01584.

IL-1F8 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 19.3 kDa and the accession number is Q9NZH7-2.

IL-1F8 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.7 kDa and the accession number is Q9NZH7-2.

IL-36 alpha/IL-1F6 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 19.2 kDa and the accession number is Q9UHA7.

IL-1F10 Protein, Human, Recombinant (His) is expressed in yeast with His tag. The predicted molecular weight is 18.4 kDa and the accession number is AAK68048.1.

IL-1 alpha/IL-1A Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 18 kDa and the accession number is P01583.

IL-36 alpha/IL-1F6 Protein, Human, Recombinant (aa 6-158) is expressed in E. coli expression system. The predicted molecular weight is 17.2 kDa and the accession number is Q9UHA7.

IL-1 beta/IL-1F2 Protein, Rabbit, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17.5 kDa and the accession number is P14628.

Interleukin-1 receptor antagonist protein (Il1rn), also known as IL-1ra, IRAP or IL1 inhibitor, is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1 alpha (IL1A) and interleukin 1 beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. The mouse Il1rn gene encodes a 178 amino acids (aa) protein with a 26 aa signal peptide. Mouse Il1rn protein shares 26% and 19% identity with its homologues IL-1 beta and IL-1 alpha, respectively. Il1rn can Inhibits the activity of interleukin-1 by binding to receptor IL1R1 and preventing its association with the coreceptor IL1RAP for signaling, but has no interleukin-1 like activity. Recently, an recombinant human Il1rn protein is used in the treatment of rheumatoid arthritis, an autoimmune disease in which IL-1 plays a key role.

IL-1 beta/IL-1F2 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 17 kDa and the accession number is P01584.

IL-25/IL17E Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 20 kDa and the accession number is Q8VHH8.

IL-25/IL17E Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 45 kDa and the accession number is Q9H293-1.

Receptor for interleukin-12. This subunit is the signaling component coupling to the JAK2/STAT4 pathway. Promotes the proliferation of T-cells as well as NK cells. Induces the promotion of T-cells towards the Th1 phenotype by strongly enhancing IFN-gamma production. IL12RB2 Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 69.7 kDa and the accession number is Q99665.

Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1 alpha/IL1A Protein, Rhesus macaque, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 34.1 kDa and the accession number is P48089.

IL12A & IL12B Heterodimer Protein, Human, Recombinant (Flag & His) is expressed in HEK293 mammalian cells with C-10xHis and C-Flag tag. The predicted molecular weight is 39.7 kDa and 27.2 kDa and the accession number is P29460 P29459.

Interleukin 25 (IL-25) belongs to the Interleukin 17 (IL-17) family of proteins, which is comprised of six members (IL-17, IL-17B through IL-17F). These proteins are secreted and are structurally related by sharing a conserved cysteine-knot fold near the C-terminus, but have considerable sequence divergence at the N-terminus. With the exception of IL-17B, which exists as a non-covalently linked dimer, all IL-17 family members are disulfide-linked dimers. IL-17 family proteins are pro-inflammatory cytokines that induce local cytokine production and are involved in the regulation of immune functions. Human interleukin-17E (IL17E), also referred to as Interleukin-25 (IL25), is a distinct member of the IL17 cytokine family comprised of at least six members sharing a conserved cysteine-knot structure but divergent at the N-terminus. IL25 is a glycoprotein secreted as dimers by innate effector eosinophils and basophils, and present at very low levels in various peripheral tissues. IL25, together with IL17B, are ligands for the cytokine receptor IL17BR, and the cross-linking induces NF-κB activation and production of the proinflammatory chemokine IL-8, as well as ERK, JNK, and p38 activation. Overexpression of IL25 gene in transgenic mice suggested that this cytokine can regulate hematopoietic and immune functions, and additionally is identified as a proinflammatory cytokine favoring Th2-type immune responses possibly by enhancing the maintenance and functions of adaptive Th2 memory cells.

NEIL1 is a member of DNA glycosylases. DNA glycosylases are a family homologous to the bacterial Fpg/Nei family. They play a role in base excision repair which is the mechanism by which damaged bases in DNA are removed and replaced. The first step of this process is catalyzed by DNA glycosylases. They remove the damaged nitrogenous base while leaving the sugar-phosphate backbone intact, creating an apurinic/apyrimidinic site, commonly referred to as an AP site. NEIL1 functions in base excision repair of DNA damaged by oxidation or by mutagenic agents. It acts as a DNA glycosylase that recognizes and removes damaged bases. NEIL1 prefers to oxidized pyrimidines, such as thymine glycol, Formamidopyrimidine (Fapy), and 5-hydroxyuracil. Has marginal activity towards 8-oxoguanine. It has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand and cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.

PPIL1 is a member of the cyclophilin family. Cyclophilins are well conserved and ubiquitous. Members of cyclophilin family take a significant part in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. PPIL1 is a peptidylprolyl isomerase(PPIase). It increases the folding of proteins and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIL1 is involved in proliferation of cancer cells through modulation of phosphorylation of stathmin. It is a novel molecular target for colon-cancer therapy.

IL-25/IL17E Protein, Canine, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 46.2 kDa and the accession number is A0A8I3MRV2.

IL-25/IL17E Protein, Rat, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 46.1 kDa and the accession number is D3ZLB1.

Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains. The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1. Regulates the IL1-mediated translocation of NCOR1 out of the nucleus. Involved in heart development.