Immunoglobulin-like receptor which plays an inhibitory role in degranulation of mast cells. Negatively regulates IgE-mediated mast cell activation and suppresses the type I immediate hypersensitivity reaction. Allergin-1 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 20.1 kDa and the accession number is Q3TB92.

MID1IP1 (MID1 Interacting Protein 1) is a Protein Coding gene. The encoded protein belongs to the SPOT14 family. It is a homodimer in the absence of THRSP. MID1IP1 interacts with ACACA and ACACB. Its interaction with THRSP interferes with ACACA binding. It up-regulates ACACA enzyme activity and plays a role in the regulation of lipogenesis in the liver. MID1IP1 is required for efficient lipid biosynthesis, including triacylglycerol, diacylglycerol, and phospholipid. MID1IP1 is involved in the stabilization of microtubules. It is widely expressed in bone marrow, fat, and other tissues. Diseases associated with MID1IP1 include Gluten Allergy and Scoliosis. Among its related pathways are the Import of palmitoyl-CoA into the mitochondrial matrix and Metabolism.

Interleukin-4, also known as IL4, is a secreted protein which belongs to the IL-4 / IL-13 family. Interleukin-4 / IL4 has many biological roles, including the stimulation of activated B-cell and T-cell proliferation.In the presence of IL-4 and IL-13, cytokines that are produced in a Th-2 type response, particularly during allergy and parasitic infections, macrophages become differentially activated, And this cytokine is a ligand for interleukin 4 receptor. . IL-4 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 17.8 kDa and the accession number is P05112.

Interleukin-4, also known as IL4, is a secreted protein which belongs to the IL-4 / IL-13 family. Interleukin-4 / IL4 has many biological roles, including the stimulation of activated B-cell and T-cell proliferation.In the presence of IL-4 and IL-13, cytokines that are produced in a Th-2 type response, particularly during allergy and parasitic infections, macrophages become differentially activated, And this cytokine is a ligand for interleukin 4 receptor. . IL-4 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 16.03 kDa and the accession number is P79339-1.

Interleukin-13 (IL-13) is a monomeric 17 kDa immunoregulatory cytokine that plays a key role in the pathogenesis of allergy, cancer, and tissue fibrosis. It is secreted by several helper T cell subsets, NK cells, mast cells, eosinophils, basophils, and visceral smooth muscle cells. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses. Positively regulates IL31RA expression in macrophages (By similarity).

Der p 23 is a new major allergen of D. pteronyssinus. The house dust mite (HDM) Dermatophagoides pteronyssinus is one of most important allergen sources and a major elicitor of allergic asthma. Der p 23 may be an essential component for diagnosis and specific immunotherapy of HDM allergy.

Has low chemotactic activity for eosinophils. May play a role in inflammation and allergy. Has no chitinase activity.

Interleukin-4, also known as IL4, is a secreted protein which belongs to the IL-4 / IL-13 family. Interleukin-4 / IL4 has many biological roles, including the stimulation of activated B-cell and T-cell proliferation.In the presence of IL-4 and IL-13, cytokines that are produced in a Th-2 type response, particularly during allergy and parasitic infections, macrophages become differentially activated, And this cytokine is a ligand for interleukin 4 receptor.

Dog dander is an important cause of respiratory allergy but its content of allergenic components is still incompletely known. The size and the amino acid composition of the ligand-binding pocket indicate that Can f 4 is capable of binding only relatively small hydrophobic molecules which are different from those that Can f 2 is able to bind. The crystal structure of Can f 4 contained both monomeric and dimeric forms of the allergen, suggesting that Can f 4 is able to form transient (weak) dimers. The existence of transient dimers in solution was confirmed by use of native mass spectrometry. The dimeric structure of Can f 4 is formed when the ends of four β-strands are packed against the same strands from the second monomer.