IL-12 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 60.13 kDa and the accession number is P29459-1&NP_002178.2.

IL-12 Protein, Human, Recombinant (His), Biotinylated is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 60.13 kDa and the accession number is P29459.2&NP_002178.2.

IL-12 Protein, Mouse, Recombinant (hFc) is expressed in HEK293 mammalian cells with hFc tag. The predicted molecular weight is 111.5 kDa and the accession number is P43431&P43432.

IL-12 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 60.3 kDa and the accession number is P43431&P43432.

IL-12 Protein, Rhesus, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 60.2 kDa and the accession number is NP_001038199.1&NP_001038190.1.

IL-12RB1 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 57.11 kDa and the accession number is NP_005526.1.

IL-12RB2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 70 kDa and the accession number is P97378.

Interleukin12 receptor subunit beta 1 (IL12RB1) is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily. IL12RB1 can spontaneously form homodimers and -oligomers, which are able to bind IL12 with only low affinity. IL12 high affinity receptor complex is composed of two subunits designated IL12RB1 and IL12RB2. While IL12RB1 interacts with the IL-12p40 subunit, IL-12p35 is mainly connecting with IL12RB2. This receptor chain is also responsible for transmitting the IL12 signal into the cell. IL12RB1, to the contrary, is also part of the IL23R, where it interacts with the p40 subunit of IL23. IL12RB1 is expressed in activated T cells, NK cells and B cells.

IL-12RB1 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 58.5 kDa and the accession number is P42701-1.

IL-12B Protein, Mesocricetus auratus, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 39.8 kDa and the accession number is Q8CJE6.

Interleukin-12 subunit beta (IL-12B) belongs to the type I cytokine receptor family. It contains 1 fibronectin type-III domain and 1 Ig-like C2-type domain. IL-12B is a cytokine that acts on T and natural killer cells, and has a broad array of biological activities. IL-12 is a disulfide-linked heterodimer composed of the 40 kD cytokine receptor encoded by IL12B and a 35 kD subunit encoded by IL12A. IL12 is expressed by activated macrophages that serve as an essential inducer of Th1 cells development. It has been found to be important for sustaining a sufficient number of memory/effector Th1 cells to mediate long-term protection to an intracellular pathogen.

The IL12 receptor complex, formed by IL12RB1 and IL12RB2, mediates the type I immune responses of various types of lymphocytes. Its ligand, IL12, is a heterodimeric cytokine composed of IL-12p35 and IL-12p40 subunits that are linked via disulfide bonds. Ligation of IL-12 to its receptor involves the binding of IL-12p35 to IL12RB1 and IL-12p40 to IL12RB2. This will result in the activation of tyrosine kinase 2 (TYK2), which is associated with the IL12RB1 chain and Janus kinase 2 (JAK2), which is associated with the IL12RB2 chain. Activated TYK2 and JAK2 direct the phosphorylation of STAT4. IL12RB1 is present on all lymphocytes, while the expression of IL12RB2 is tightly regulated. It has shown that the expression of IL12RB2 is limited to Th2 cells. IL12RB2 subunit plays an important role in Th1 cell differentiation, since its absence leads to an abortive Th1 differentiation that has dysfunctional production of Th1 effector molecules.

Interleukin (IL)‑12B, which encodes the p40 subunit common to IL‑12 and IL‑23, as one of the genes for which expression in fibroblast‑like synoviocytes from patients with rheumatoid arthritis (RA‑FLS) is induced by DcR3.Decoy receptor 3 (DcR3) competitively binds to three ligands, Fas ligand, lymphotoxin‑related inducible ligand that competes for glycoprotein D binding to herpesvirus entry mediator on T cells and tumor necrosis factor‑like ligand 1A (TL1A), to prevent their effects. Recent studies have suggested that DcR3 directly affects cells as a ligand.

IL-12 Protein, Mouse, Recombinant (His & hFc) is expressed in HEK293 mammalian cells with His and hFc tag. The predicted molecular weight is 85.9 kDa and the accession number is P43431&P43432.

IL-12 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 57.2 kDa and the accession number is P29459-1&NP_002178.2.

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Macrophage Metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein that belongs to the peptidase M1A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type I I-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.

Interleukin-18 (IL-18) is a member of the interleukin-1 family of cytokines produced constitutively by different cell types and by adipose tissue. Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation. IL-18R alpha Protein, Cynomolgus, Recombinant (aa 22-329, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 36.45 kDa and the accession number is A0A2K5V3J9.

Interleukin-18 (IL-18) is a member of the interleukin-1 family of cytokines produced constitutively by different cell types and by adipose tissue. Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation. IL-18R alpha Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 38.8 kDa and the accession number is Q13478.

Interleukin-18 (IL-18）is a protein which belongs to the IL-1 family. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. Mature mouse IL-18 shares 63% and 91% amino acid sequence identity with mouse and rat IL-18, respectively. IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex. Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs. It augments natural killer cell activity in spleen cells and stimulates interferon gamma production in T-helper type I cells. In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells. In the absence of IL-12 or IL-15, however, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils.

Siglecs are sialic acid specific I‑type lectins that are characterized by an extracellular domain (ECD) with an N‑terminal Ig‑like V‑set domain followed by varying numbers of Ig‑like C2‑set domains. Mouse Siglec‑E, also known as Myeloid Inhibitory Siglec (MIS), is an 80 ‑ 85 kDa member of the CD33‑related subfamily of Siglecs. Rodent and primate Siglec gene families have significantly diverged, and Siglec‑9 is the most likely human ortholog of mouse Siglec‑E. Siglec‑E is expressed as a heavily N‑glycosylated disulfide‑linked homodimer and shows binding preference for disialic acids in the alpha 2‑8 linkage. Siglec‑E is up‑regulated and additionally phosphorylated following cellular stimulation by a variety of TLR agonists. Siglec‑E signaling negatively regulates the LPS‑induced production of TNF‑ alpha and IL‑6 by macrophages. Its up‑regulation in macrophages parallels the development of endotoxin tolerance. Siglec‑E recognition of sialylated determinants on virulent T. cruzi contributes to the suppression of dendritic cell IL‑12 p40 production.

Interleukin-18 (IL-18) is a member of the interleukin-1 family of cytokines produced constitutively by different cell types and by adipose tissue. Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation. IL-18R alpha Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 38.8 kDa and the accession number is Q13478.

Interleukin 1 family member 7, or interleukin 37 (IL1F7 / IL37 / IL-1H4) is a secretory protein belonging to the Interleukin 1 family. IL-1F7 was localized in human peripheral monocytic cells. It has been localized the expression of IL-1F7b protein in discrete cell populations including plasma cells and tumor cells. These data suggest that IL-1F7 may be involved in immune response, inflammatory diseases, and/or cancer. Through constructing an adenoviral vector that allows high-level expression in murine and human cells, it has been demonstrated that the ability of adenovirus-mediated gene transfer of IL1F7 to induce an IL-12- and Fas ligand-dependent anti-tumor response. Complete inhibition of tumor growth was observed following multiple injections of IL1F7 in most animals. These results suggest that IL1F7 could play a role in both innate and adaptive immune responses, similar to IL-18. Moreover, IL1F7 could be useful for cancer gene therapy.

Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation.