IL-12 (mouse):Fc-KIH (human) (rec.) Reference: AG-40B-0240 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, 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. IL-39, the newest member of IL-12 family, mediates the inflammatory response through the activation of STAT1/STAT3 signaling pathway. These IL-12 family members link innate immunity with the development of adaptive immunity and are also important for regulating T cell responses. IL-12 is composed of two subunits IL-12A/p35 and IL-12B/p40 and signals via a high-affinity IL-12R, leading to activation of STAT 4. IL-12 is produced by macrophages, dendritic cells and B cells. The key role of the pro-inflammatory IL-12 is to induce the IFN-gamma which regulates the Th responses, to promote the naïve T cells to directly differentiate into effector cells (Th1) and then release IFN-gamma. The protein IL-12 (mouse):Fc-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-12A/p35:Fc Knobs sequence (synthesizing a protein of 60kDa) and one encoding for the IL12B/p40:Fc Holes sequence (synthesizing a protein of 75kDa). Both vectors transfected into CHO 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-12 (mouse):Fc-KIH (human) (rec.). 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-38 (aa 1-152) (human) (monomeric):Fc-KIH (human) (rec.) Reference: AG-40B-0241 IL-38 (IL-1F10) belongs to the IL-1 family of proteins. IL-38 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-38 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-38 is unregulated during some autoimmune diseases such as Systemic Lupus Erythematosus. The protein IL-38 (aa 1-152) (human) (monomeric):Fc-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-38 (aa 1-152) (human):Fc Knobs sequence (synthesizing a protein of 45kDa) and one encoding for the Fc 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-38 (aa 1-152) (human)(monomeric):Fc-KIH (human) (rec.). 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 (human):Grancalcin (human) (rec.) Reference: AG-40B-0242 Grancalcin is a member of a new family of proteins named penta-EF-hand (PEF), which contains five repetitive EF hand motifs. PEF proteins form a unique group including calpain, sorcin, grancalcin, ALG-2 (apoptosis-linked gene-2 protein) and peflin. The penta-EF hand members are Ca2+-binding proteins implicated in regulating cell migration, apoptosis and the mobilization of immune cells. Senescent cells accumulate in the bone marrow and secrete factors, termed senescence-associated secretory phenotype (SASP), that can promote skeletal aging. Recently, senescent neutrophils and macrophages in the bone marrow were shown to be critical cell types during skeletal aging releasing Grancalcin (GCA) to promote such aging. Grancalcin seems to act by competitively binding to and inactivating PlexinB2 functions in bone marrow stromal cells (BMSCs) leading to repression of osteogenesis and increase of adipogenesis. Increased Grancalcin expression in immune cells (bone marrow macrophages and in neutrophils) is due to higher endotoxin levels observed during aging.
Flagellin (rec.) (untagged) (highly active) Reference: AG-40B-0243 Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. It activates the innate immune system through the receptor Toll-like Receptor 5 (TLR5) and the intracellular protein NLRC4 (NLR family CARD domain-containing protein 4).
Irisin (rec.) (HEK293) Reference: AG-40B-0102 Irisin is a recently described exercise-induced hormone secreted by skeletal muscle in mice and humans. Irisin activates beige fat cells (beige cells have a gene expression pattern distinct from either white or brown fat and are preferentially sensitive to the polypeptide hormone Irisin). Irisin is cleaved from the type I membrane protein FNDC5 and improves systemic metabolism by increasing energy expenditure.
IGFL1 (human) (rec .) Reference: AG-40B-0244 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 and 3 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.
Fc (LALA-PG)-KIH (human) IgG1 Control (rec.) Reference: AG-35B-0018 Negative control in experiments with recombinant proteins fused to human IgG1 Fc (LALA-PG)-KIH (Knobs-into-Holes) (e.g. Prod. No. AG-40B-0248). This protein is not an appropriate negative control for other standard Fc protein constructs. The protein Fc (LALA-PG)-KIH (human) IgG1 Control (rec.) is produced by using two different vectors, one encoding for the Fc (LALA-PG) Knobs sequence with a small linker (synthesizing a protein of 29kDa) 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 and for secretion of the final protein Fc (LALA-PG)-KIH (human) IgG1 Control (rec.). The Fc contains the mutations LALA-PG that abolish the interaction between the Fc and FcgammaRs and therefore Fc undesirable effects. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.
B-Xpander™ CD40L (human) (rec.) (Animal Free) Reference: AG-40B-0010AF B-Xpander™ is a potent enhanced Multimeric human CD40L cytokine, for B cell activation, B cell expansion (proliferation) and cell therapy applications. In-house production using a proprietary protocol and a characterized and certified CHO cell line allows the supply of the most active Multimeric human CD40L proteins in GMP-like format. Interest in B cells has recently increased in immunotherapies using Engineered B cells or Tumor-Infiltrating Lymphocytes (TILs). However, current methods for B cell expansion are inefficient, time consuming and can lead to insufficient B cell numbers and persistent T cell exhaustion. Our B-Xpander™ protein improves current protocols for B cell stimulation by mimicking the natural interaction between CD40L and CD40 molecules on B cells. B-Xpander™ Quality Features: • Production in characterized and certified CHO cell line (for GMP-grade manufacturing)* • High Bioactivity tested by ELISA/Cell-based Assays • Verified Purity & Homogeneity by SEC • Low Endotoxin Level • Batch-to-Batch Consistency • Animal-component free Production • No cross-linking Reagents necessary
Fc (LALA-PG)-KIH (human):GDF15 (mouse) (rec.) Reference: AG-40B-0245 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 (mouse) (rec.) is produced by using two different vectors, one encoding for the Fc Knobs (LALA-PG) (human):GDF15 (mouse) sequence (synthesizing a protein of 45kDa) 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 (mouse) (rec.). This Fc-KIH format allows our mouse GDF15 protein to form a dimer that is the most active structure to bind and activate the GFRAL and RET receptor complex. The Fc contains the mutations LALA-PG that abolish the interaction between the Fc and FcgammaRs and therefore Fc undesirable effects. 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):Irisin (monomeric) (rec.) Reference: AG-40B-0246 Irisin is a recently described exercise-induced hormone secreted by skeletal muscle in mice and humans. Irisin activates beige fat cells (beige cells have a gene expression pattern distinct from either white or brown fat and are preferentially sensitive to the polypeptide hormone Irisin). Irisin is cleaved from the type I membrane protein FNDC5 and improves systemic metabolism by increasing energy expenditure. Upon exercise, FNDC5 expressed by skeletal muscles is proteolytically processed and secreted as the myokine Irisin, which has several functions: i) it contributes to the conversion of white fat to higher oxygen consumable brown fat (also called beige fat) in response to exercise; ii) it regulates bone mineral density and bones remodeling; and iii) it increases synaptic plasticity and rescues memory and cognitive function of the brain in mouse models of Alzheimer’s disease. Irisin not only plays a vital role in energy metabolism but also has crucial roles in a variety of processes such as inflammation, proliferation, metastasis, aging and neural differentiation. The protein Fc (LALA-PG)-KIH (human):Irisin (monomeric) (rec.) is produced by using two different vectors, one encoding for the Fc Knobs (LALA-PG) (human):Irisin sequence (synthesizing a protein of 55kDa) 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):Irisin (monomeric) (rec.). The Fc contains the mutations LALA-PG that abolish the interaction between the Fc and FcgammaRs and therefore Fc undesirable effects. 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-23 (mouse):Fc (LALA-PG)-KIH (human) (rec.) Reference: AG-40B-0248 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, 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. IL-39, the newest member of the IL-12 family, mediates the inflammatory response through the activation of STAT1/STAT3 signaling pathway. These IL-12 family members link innate immunity with the development of adaptive immunity and are also important for regulating T cell responses. Interleukin-23 (IL-23) is composed of the IL-12 p40 chain covalently linked to p19, a chain related to the IL-12 p35 subunit. IL-23 signals through the IL-23 receptor complex, which is composed of the IL-12Rbeta1 chain and a gp130-like chain, IL-23R. Triggering of the IL-23 receptor complex leads to the activation of Tyk2, Jak2 and STAT1, 3 and 4. IL-23 induces IFN-gamma production, Th1 cell differentiation and activation of the antigen-presenting functions of dendritic cells. IL-23 induces autoimmune inflammation and thus may be responsible for autoimmune inflammatory diseases and important for tumorigenesis. The protein IL-23 (mouse):Fc (LALA-PG)-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-23A/p19:Fc Knobs sequence (synthesizing a protein of 55kDa) and one encoding for the IL-12B/p40:Fc Holes sequence (synthesizing a protein of 75kDa). Both vectors transfected into CHO 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-23 (mouse):Fc (LALA-PG)-KIH (human) (rec.). The Fc contains the mutations LALA-PG that abolish the interaction between the Fc and FcgammaRs and therefore Fc undesirable effects. 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-27 (mouse):Fc (LALA-PG)-KIH (human) (rec.) Reference: AG-40B-0249 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. IL-39, the newest member of IL-12 family, mediates the inflammatory response through the activation of STAT1/STAT3 signaling pathway. These IL-12 family members link innate immunity with the development of adaptive immunity and are also important for regulating T cell responses. IL-27 is composed of two subunits, IL-27p28 and Epstein-Barr virus-induced gene 3 (EBI3) signals via a heterodimeric receptor consisting of WSX-1 and glycoprotein (gp130), leading to activation of STAT 1 and 3. IL-27 is pro-inflammatory and promotes NK and T cell proliferation as well as the production of IFN-gamma. It is anti-inflammatory, inhibiting Th2 and Th17 cell activities and stimulating the production of IL-10 by T regulatory cells. IL-27 has potent antiviral activities against numerous viruses, by increasing the production of interferons (IFNs). Finally, IL-27 has antitumor activity as well as anti-angiogenic activity with activation of the production of anti-angiogenic chemokines. The protein IL-27 (mouse):Fc-KIH (human) (rec.) is produced by using two different vectors, one encoding for the IL-27A/p28:Fc Knobs sequence (synthesizing a protein of 62kDa) and one encoding for the IL27B/EBI3:Fc Holes sequence (synthesizing a protein of 60kDa). Both vectors transfected into CHO 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-27 (mouse): Fc (LALA-PG)-KIH (human) (rec.). The Fc contains the mutations LALA-PG that abolish the interaction between the Fc and FcgammaRs and therefore Fc undesirable effects. InVivoKines™ are a new generation of recombinant fusion proteins for immunotherapeutic, preclinical and translational in vivo research, developed and manufactured by AdipoGen Life Sciences.