Other Proteins

OX40 (also known as CD134, TNF receptor superfamily member 4, or TNFRSF4) is an immune checkpoint and a co-stimulatory receptor of the TNF (tumor necrosis factor) receptor family, expressed on the surface of T cells. Binding of OX40 to its ligand, OX40L (also known as CD252), potentiates T cell activation, differentiation, proliferation, survival, and T cell effector function. OX40L is present in NK cells, participating in their activation and cytotoxicity profile, and dendritic cells. OX40 can bind to members of the TRAF (TNFR associated factor) family of proteins, which can then regulate the NF-κF (nuclear factor kappa-light chain enhancer of activated B cells) signaling pathway. OX40 and OX40L can be found in cancer cells, such as AML (acute myeloid leukemia) and breast cancer cells. Studies have shown that OX40 agonists can increase anti-tumor immunity and improve tumor-free survival in pre-clinical studies. Alternatively, OX40 antagonists offer potential as therapeutics for inflam

CD155 (also known as PVR cell adhesion molecule) is a transmembrane glycoprotein receptor of the immunoglobulin superfamily of proteins. It is highly expressed in dendritic cells, fibroblasts, endothelial cells, and multiple tumor cells including ovarian carcinoma, non-small cell lung, glioblastoma, and colorectal carcinoma. It has a high affinity for a T cell regulatory transmembrane surface protein called TIGIT (T cell immunoglobulin and ITIM domains) and plays a key role in tumor cell invasion and migration. Interaction between CD155 and TIGIT causes immunosuppressive effects on CD4⁺ and CD8⁺ T cells, which hinders T cell proliferation and function. CD155 also interacts with the regulatory receptors CD226 (expressed on natural killer (NK) cells, monocytes and CD4⁺ T cells) and CD96. While CD155-CD226 engagement activates NK cell cytotoxicity and T cell response, CD155-CD96 interaction inhibits NK cell function. Due to these opposing regulatory effect

CD155 (also known as PVR cell adhesion molecule) is a transmembrane glycoprotein receptor of the immunoglobulin superfamily of proteins. It is highly expressed in dendritic cells, fibroblasts, endothelial cells, and multiple tumor cells including ovarian carcinoma, non-small cell lung, glioblastoma, and colorectal carcinoma. It has a high affinity for a T cell regulatory transmembrane surface protein called TIGIT (T cell immunoglobulin and ITIM domains) and plays a key role in tumor cell invasion and migration. Interaction between CD155 and TIGIT causes immunosuppressive effects on CD4⁺ and CD8⁺ T cells, which hinders T cell proliferation and function. CD155 also interacts with the regulatory receptors CD226 (expressed on natural killer (NK) cells, monocytes and CD4⁺ T cells) and CD96. While CD155-CD226 engagement activates NK cell cytotoxicity and T cell response, CD155-CD96 interaction inhibits NK cell function. Due to these opposing regulatory effect

Fibroblast growth factor 19 (FGF-19) is a secreted protein which belongs to the FGFs family. FGF-19 is expressed in fetal brain, cartilage, retina, and adult gall bladder. FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity. FGFRs can be important for regulation of glucose and lipid homeostasis. FGF19 has important roles as a hormone produced in the ileum in response to bile acid absorption. It has been shown to cause resistance to diet-induced obesity and insulin desensitization and to improve insulin, glucose, and lipid profiles in diabetic rodents. FGF-19 can be considered as a regulator of energy expenditure.

FGF-10 is a member of the large and diverse fibroblast growth factor (FGF) family of peptide growth factors. FGF-10 functions as a signaling molecule that is involved in many important processes.The proteins of this family play a core role in the prenatal development, postpartum growth, and regeneration processes of various tissues by promoting cell proliferation and differentiation. FGF-10 is most correlated with KGF/FGF-7 and is expressed during development, with a preference for expression in adult lungs. It binds to receptor FGFR2b and is essential as a signaling growth factor for mesenchymal-to-epithelial transition.

At least 23 different variants of IFN-α are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-α subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-α subtypes only differ in their sequences by one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. IFNA2 (Interferon Alpha 2) is a Protein Coding gene. This gene is a member of the alpha interferon gene cluster on chromosome 9. The encoded protein is a cytokine produced in response to viral infection. Type I Interferons (IFNs) are well-known cytokines that exert antiviral activity, antitumor activity, and immunomodulatory effects.