CD86 (P2) (human)-muIg Fusion Protein (Biotin) Reference: ANC-579-030 Human CD86 (B7-2) is a costimulating ligand for CD28 and CD152 (CTLA-4). CD86 is expressed on activated B cells and blood monocytes.
Asprosin (human) (rec.) (His) Reference: AG-40B-0174 Asprosin is a new fasting-induced protein hormone that targets the liver to increase plasma glucose levels. Asprosin is the C-terminal cleavage product of the protein pro-Fibrillin-1. Asprosin is secreted from white adipose tissue and increases hepatic glucose production by using cAMP as a second messenger, leading to activation of protein Kinase A. Reduction of Asprosin levels protects against metabolic syndrome-associated hyperinsulinism. Asprosin may act as a circulating hunger signal. Indeed, peripherally injected recombinant asprosin can cross the blood-brain barrier and intracerebroventricular (i.c.v.) injection of recombinant asprosin stimulated appetite in wild-type mice, indicating a central mechanism of action. Loss of Asprosin in mice and human leads to decreased fat mass and body weight, and hypophagia. Mice are also completely protected from the development of diet-induced obesity. Asprosin works by stimulating the orexigenic AgRP+ (Agouti related neuropeptide) neurons via a cAMP-dependent pathway and by inhibiting the anorexigenic neurons POMC+ (pro-opiomelanocortin) neurons in a GABA-dependent manner. Mutation in Asprosin in human leads to the pattern of metabolic dysregulation, including partial lipodystrophy, accompanied by reduced plasma insulin. Due to its key role in food regulation, Asprosin function could serve as a potentially unique therapeutic target against obesity, diabetes or metabolic diseases. Endogenous asprosin runs on SDS-PAGE at ~30kDa, while bacterially expressed recombinant asprosin runs at 18kDa. The difference of migration is probably due to predicted three N-linked glycosylation sites and potentially other post-translational modifications that are lacking in bacteria. Bacterially expressed recombinant asprosin retains the biological activity displayed by its endogenously expressed counterpart.
IL-38 (human) (rec.) (His) Reference: AG-40A-0191Y IL-38 (IL-1F10) mRNA is expressed in heart, placenta, fetal liver, spleen, thymus and tonsil. The expression in a variety of immune tissues and similarity to IL-1Ra suggest a role of IL-1F10 in the inflammatory response. It has been reported that removal of the N-terminus domain of the interleukins of the IL-1F family such as IL-1F5 / 6 / 8 or 9 (also called IL-36Ra, IL-36alpha, IL-36beta or IL-36gamma) is important to increase their biological activity. Recently it has been shown that IL-38 is N-terminally processed and secreted by apoptotic cells. Released processed IL-38 (20-152) binds to the receptor Interleukin-1 receptor accessory protein-like 1 (IL1RAPL1; TIGIRR-2) at the surface of macrophages. Processed IL-38-activated IL1RAPL1 reduces the production of IL-6 leading to inflammation attenuation.
IL-7 (human) (monomeric):Fc (LALA-PG)-KIH (human) (rec.) Reference: AG-40B-0247 Interleukin-7 (IL-7) is a hematopoietic growth factor and a member of the IL-7/IL-9 family, which is produced by fetal liver cells, stromal cells in the bone marrow (BM), thymus and other epithelial cells, including keratinocytes and enterocytes. The receptor of IL-7, IL-7R, is a heterodimeric complex consisting of the alpha-chain (CD127) and the common cytokine receptor gamma-chain, shared with the receptors for IL-2, IL-4, IL-7, IL-9, IL-15 and IL-21, and expressed in a variety of cells. IL-7 has a critical developmental function at every stage of T cell development, for both alphabeta and gammadelta lineages, and for the development and survival of naive T cells as well as generation and maintenance of CD4 and CD8 memory. IL-7 is also essential for the development and maintenance of the new ILCs. IL-7 is important throughout hematopoiesis, facilitating key lineage fate decisions. IL-7 is thought to support aberrant immune activity in autoimmune diseases such as diabetes and multiple sclerosis and in chronic inflammatory diseases such as rheumatoid arthritis, ankylosing spondylitis and inflammatory bowel disease. IL-7 contributes to leukemia development in vivo and also stimulates multiple immune-mediated mechanisms that contribute to the eradication of tumors. The protein IL-7 (human) (monomeric):Fc (LALA-PG)-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-7 (human):Fc (LALA-PG) Knobs sequence (synthesizing a protein of 60kDa) and one encoding for the Fc (LALA-PG) Holes sequence (synthesizing a protein of 28kDa). Both vectors transfected into HEK293 cells produce both Fc molecules (Knobs-into-Holes technology; J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)) required for dimerization of the Fc moieties and for secretion of the final protein IL-7 (human) (monomeric):Fc-KIH (human) (rec.). The LALA-PG mutations inhibit binding to FcgammaRs and C1q while FcRn binding and Fc stability remain unaffected. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
IL-21 (mouse) (monomeric):Fc (LALA-PG)-KIH (human) (rec.) Reference: AG-40B-0250 IL-21 is a monomeric 15 kDa cytokine, identified as a multifunctional cytokine principally produced by follicular helper T (Tfh), T helper 17 (Th17) and natural killer (NK) cells, but also by CD8+ T cells. As a receptor for IL-21, IL-21R, a class I cytokine heterodimeric receptor, shares a common cytokine receptor gamma chain with other cytokine families, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21 receptor (IL-21R) is heterodimeric (composed of an alpha and ɣ-chain) and physiologically expressed on immune cells (T and B cells, macrophages, DCs, thymocytes and splenocytes). Upon binding to its receptor, IL-21 induces strong and sustained activation of STAT3, which is critical for its effects on B cell and T cell differentiation. IL-21 produced by follicular helper CD4 T cells (TFH) acts directly on B cells to generate high-affinity, class-switched antibodies. IL-21 is important for the maturation of T and B cells in Germinal Centers (GCs) and supports the formation of antigen-specific memory B cells and long-lived plasma cells. The formation of Th17 cells is promoted by IL-21. IL-21 is an important key factor in chronic inflammatory and in autoantibody-mediated skin diseases, where Th17, Th1, Tfh or B cells are critically involved. IL-21 is a promising immunotherapeutic agent for cancer. CD8 T cells expressing IL-21R fight cancer and drive autoimmune disease. IL-21 promotes maturation, enhances cytotoxicity, and induces the production of IFN- gamma and perforin by NK cells. IL-21 is known to directly induce apoptosis in certain types of lymphoma. Finally, IL-21 is used in adoptive transfer of in vitro expanded tumor antigen-specific CD8 + T cells (TILs cells) and IL-21 induced a long-lived memory phenotype compared to the cells not treated with IL-21. The protein IL-21 (mouse) (monomeric):Fc (LALA-PG)-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-21 (mouse):Fc (LALA-PG) Knobs sequence (synthesizing a protein of 60kDa) and one encoding for the Fc (LALA-PG) Holes sequence (synthesizing a protein of 28kDa). Both vectors transfected into CHO cells produce both Fc (LALA-PG) molecules (Knobs-into-Holes technology; J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)) required for dimerization of the Fc moieties and for secretion of the final protein IL-21 (mouse) (monomeric):Fc (LALA-PG)-KIH (human). The LALA-PG mutations inhibit binding to FcgammaRs and C1q while FcRn binding and Fc stability remain unaffected. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
IGFL4 (human) (rec.) (His) Reference: AG-40B-0251 The Insulin-growth factor-like gene family is a new family of proteins consisting of four proteins in humans (IGFL1 to 4) and one in mice (mIGFL). mIGFL is expressed in normal skin in mice and further upregulated during inflammation responses in the skin or after skin wounding. In humans only IGFL1 expression is increased in psoriatic skin samples. mIGFL and human IGFL1, 3 and 4 interact with specificity and high affinity to a novel receptor named IGF-like family receptor 1 (formerly TMEM-149). Analysis of the amino acid sequence of IGFLR1 indicated that this receptor is likely a novel member of the TNF-R family. IGFLR1 is expressed most abundantly on mouse T cells, suggesting that mIGFL and IGFL1 produced in the skin may potentially exert regulatory functions on T cell responses. In addition to the ovary, spinal cord and fetal skin, IGFL1 is also expressed in head and neck tumors, uterine tumors, squamous cell carcinomas and lung adenocarcinoma. In many cancers, IGFL1 (as well as the other IGFLs) plays multiple roles in regulating the proliferation, differentiation and apoptosis of cancer cells. Biological functions of IGFL4 are not characterized yet.
IL-4 (mouse):Fc (mouse) (rec.) (non-lytic) Reference: CHI-MF-12004V Interleukin-4 (IL-4) is a cytokine produced by type 2 helper T cells, the Th2 cells. These cells tends to make a specific set of lymphokines including IL-4, IL-5, IL-6, IL-10, IL-13, IL-3 and GM-CSF and fail to produce IL-2, IFN-gamma, and lymphotoxin (TNF-beta). In addition, mast cells can produce IL-4. IL-4 exerts numerous effects on various hematopoietic cell types. On B cells, IL-4 promotes immunoglobulin class switching to IgE and IgG1 isotypes and upregulates MHC class II and CD23 expression. IL-4 promotes survival, growth, and differentiation of both T and B lymphocytes, mast cells and endothelial cells. In addition, IL-4 inhibits the production of TNF, IL-1, and IL-6 by macrophages.
20S Immunoproteasome (human) (untagged) Reference: SBB-PP0144 The 20S immunoproteasome is structurally similar to constitutive 26S proteasome. The 20S core of immunoproteasome contains two outer rings composed of alpha-subunits, and two internal 7-subunit containing rings each possessing 3 specific subunits responsible for proteasome catalytic activity. In immunoproteasomes these subunits (ß1, ß2, ß5) are replaced by three inducible subunits: PSMB9, PSMB10 and PSMB8, (ß1i, ß2i, ß5i). These stress-induced subunits allow for the production of MHC-1 associating peptides, which are displayed as antigens on the cell surface. These displayed peptides can then be recognized by immune surveillance CD8 T cells. 20S immunoproteasome is recognized as a strong drug target for autoimmune disease and cancer.
Fc (LAEA-PG)-KIH (mouse) IgG2b Control (rec.) Reference: AG-35B-0019 Negative control in experiments with recombinant proteins fused to mouse IgG2b Fc (LAEA-PG)-KIH. This protein is not an appropriate negative control for other standard Fc protein constructs. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
IL-35 (human):Fc (LALA-PG)-KIH (human) (rec.) Reference: AG-40B-0252 Interleukin-12 (IL-12) family members are heterodimer glycoproteins, composed of two covalently linked subunits, alpha and beta chains. The alpha-subunit consists of IL-23p19, IL-27p28, and IL-12p35 and the beta-subunit includes IL-12p40 and Epstein-Barr virus-induced gene (Ebi3). IL-12 members bind to cognate heterodimeric receptor chains expressed on T cells. This family includes IL-12, IL-23, IL-27 and IL-35 and IL-39. IL-12 and IL-23 are predominantly proinflammatory cytokines that contribute key roles in the development of Th1 and Th17 cells, respectively. IL-27 has both pro- and anti-inflammatory properties and is a potent T cell immunomodulator. IL-35, a new member of this family, is a potent inhibitory cytokine produced by natural, thymus-derived regulatory T cell (nTreg) populations. Recently, a subset of B cells that produce IL-35 was identified and shown to provide protection against autoimmune diseases. These IL-12 family members link innate immunity with the development of adaptive immunity and are also important for regulating T cell responses. IL-35 is composed of two subunits, IL-12A and Epstein-Barr virus-induced gene 3 (EBI3) signals via a heterodimeric receptor consisting of IL-12Rbeta2 and glycoprotein (gp130), leading to activation of STAT 1 and 4. IL-35 is a potent suppressive cytokine directly limiting the inflammatory response that has important roles in infection, cancer and autoimmune diseases. The protein IL-35 (human):Fc (LALA-PG)-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-12A:Fc Knobs sequence (synthesizing a protein of 68kDa) and one encoding for the IL27B/EBI3:Fc Holes sequence (synthesizing a protein of 60kDa). Both vectors transfected into HEK293 cells produce both Fc molecules (Knobs-into-Holes technology; J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)) required for dimerization and for secretion of the final protein IL-35 (human):Fc (LALA-PG)-KIH (human) (rec.). The LALA-PG mutations inhibit binding to FcgammaRs and C1q while FcRn binding and Fc stability remain unaffected. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
Fc (LALA-PG)-KIH (human):GDF15 (human) (rec.) Reference: AG-40B-0253 Growth and differentiation factor 15 (GDF15, also known as macrophage inhibitory cytokine-1 (MIC-1)), is a member of the transforming growth factor (TGF)-beta superfamily and was initially identified in activated macrophages. GDF15 acts through a recently identified receptor called Glial-derived Neurotrophic Factor (GDNF) Receptor Alpha-Like (GFRAL) which signals through the Rearranged during Transfection (RET) tyrosine kinase receptor. GDF15 is highly expressed in placenta and brain, and it is expressed at lower levels in kidney, pancreas, prostate and colon. Similar to other TGF-beta family proteins, GDF15 is synthesized as a large precursor protein that is cleaved to release the mature protein that shares 66% and 97% amino acid sequence identity with the human and rat proteins, respectively. Biologically active GDF15 is a disulfide-linked homodimer of the mature protein. The effects of GDF-15 are pleiotropic and include appetite regulation, actions on metabolism, pregnancy, cell survival, immune response and inflammation. GDF-15 also plays different roles in the pathophysiology of cardiovascular disease, autoimmunity, cancer-associated anorexia/cachexia and diabetes. High levels of GDF15 cause anorectic effects and cachexia, largely if not exclusively through the suppression of food intake via modulation of neuropeptide Y and pro-opiomelanocortin levels. Various functions have been reported for GDF15, including inhibition of TNF-alpha production from lipopolysaccharide-stimulated macrophages and the induction of cartilage formation. GDF15 promotes also neuronal survival. GFRAL and GDF15 signaling is implicated in diet-based obesity and insulin resistance. GDF15 is cardioprotective via inhibition of platelet activation, limiting atherosclerosis, promoting recovery following myocardial infarction and regulating angiogenesis. The protein Fc (LALA-PG)-KIH (human):GDF15 (human) (rec.) is produced by using two different vectors, one encoding for the Fc Knobs (LALA-PG) (human):GDF15 (human) sequence (synthesizing a protein of 47kDa) and one encoding for the Fc Holes (LALA-PG) sequence (synthesizing a protein of 30kDa). Both vectors transfected into HEK293 cells produce both Fc molecules (Knobs-into-Holes technology; J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)) required for dimerization and for secretion of the final protein Fc (LALA-PG)-KIH (human):GDF15 (human) (rec.). This Fc-KIH format allows our human GDF15 protein to form a dimer that is the most active structure to bind and activate the GFRAL and RET receptor complex. The LALA-PG mutations inhibit binding to FcgammaRs and C1q while FcRn binding and Fc stability remain unaffected. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
Fc (LALA-PG)-KIH (human):IL-1Ra (mouse) (monomeric) (rec.) Reference: AG-40B-0254 IL-1 is a group of inflammatory cytokines, represented by interleukin-1alpha and interleukin-1beta. IL-1Ra is a cytokine initially isolated from macrophages. It shares 19% of homologous amino acids with IL1A and 30% of homologous amino acids with IL1B. IL-1Ra is abundant in the proximal digestive tract reproductive system, skin, bone marrow, and liver. IL-1Ra is the principal endogenous IL-1 antagonist. IL-1Ra is upregulated during host acute or chronic inflammatory responses. IL-1Ra plays diverse roles in anti-inflammatory and anti-tumor processes, either inhibiting tumor angiogenesis and proliferation or suppressing tumor migration and metastasis. The protein Fc (LALA-PG)-KIH (human):IL-1Ra (mouse) (monomeric) (rec.) is produced by using two different vectors, one encoding for the Fc Knobs (LALA-PG) (human):IL-1Ra (mouse) sequence (synthesizing a protein of 50kDa) and one encoding for the Fc Holes (LALA-PG) sequence (synthesizing a protein of 30kDa). Both vectors transfected into HEK293 cells produce both Fc molecules (Knobs-into-Holes technology; J.B. Ridgway, et al.; Protein Eng. 9, 617 (1996)) required for dimerization and for secretion of the final protein Fc (LALA-PG)-KIH (human):IL-1Ra (mouse) (monomeric) (rec.). This Fc-KIH format allows our mouse IL-1Ra protein to form a monomer that is the most active structure to bind and inhibit the IL-1 receptor. The LALA-PG mutations inhibit binding to FcgammaRs and C1q while FcRn binding and Fc stability remain unaffected. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.