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Vascular endothelial growth factor (VEGF-121) is a naturally-occurring VEGF-A splice variant involved in embryonic vasculogenesis and angiogenesis. VEGF binds to VEGFR-1 and VEGFR-2, and activates Raf/MEK/ERK and PI3K/AKT pathways. VEGF-121 is released as a freely diffusible protein by a variety of normal and transformed cells. It plays an important role in neurogenesis both in vitro and in vivo (Storkebaum et al.). It has neurotrophic effects on neurons of the central nervous system and promotes growth and survival of dopaminergic neurons and astrocytes. VEGF also promotes growth and survival of vascular endothelial cells, monocyte chemotaxis, and colony formation by granulocyte-macrophage progenitor cells (Ferrara et al.).

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Neurotrophin-4 (NT-4) is a member of the nerve growth factor family which includes neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and nerve growth factor (NGF), all of which promote the differentiation, growth, and survival of peripheral and central nervous system neurons (Eide et al.). NT-4 binds and activates tropomyosin receptor kinase B (TrkB) at the cell surface; in doing so, it acts as a survival factor for certain populations of sensory neurons (Berkemeier et al.; Skaper). It has been shown that NT-4, together with BDNF, promotes neurite extension and maturation, as well as maintenance of differentiated cerebellar granule cells (Gao et al.).

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Modulate prostaglandin metabolism with 15-hydroxyprostaglandin dehydrogenase (15-PGDH). 15-PGDH catalyses the reversible oxidation of the 15-hydroxyl group in prostaglandins, resulting in inactivated metabolites (Ensor and Tai), it can act on a variety of prostaglandins as substrates in a NAD+ dependent manner (Cho et al.). As prostaglandins can have a range of effects on cellular processes, 15-PGDH is of considerable importance in drug development. In vitro and in vivo studies suggest 15-PGDH has tumor suppressive activity and is downregulated in certain cancers (Na et al.).15-PGDH belongs to the short-chain dehydrogenases/reductases (SDR) family; its primary structure indicates 20% homology with other SDRs, with some conserved amino acid residues (Krook et al.). This protein contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, apo M from STEMCELL comes lyophilised with ≥89% purity.

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Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Yang et al.; Dorssers et al.; Broughton et al.). IL-3 is produced by activated T cells and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by basophils and eosinophils (Broughton et al.). The IL-3 receptor consists of a unique alpha subunit (CD123) and a beta common subunit (βc or CD131) that is shared with the receptors for IL-5 and GM-CSF, and is the principal signal transduction subunit for these cytokines. IL-3 binding to the heterodimeric receptor activates JAK/STAT, MAPK, and PI3K signaling pathways (Woodcock et al.).

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Fibroblast growth factor acidic (FGF-acidic), also known as FGF-1, is a potent activator of DNA synthesis, cell proliferation, and chemotaxis and is known to play numerous roles in development, regeneration, and angiogenesis (Jaye et al.; Galzie et al.; Presta et al.). FGF-acidic is produced by multiple cell types and is capable of activating all cells of mesodermal origin and many cells of neuroectodermal, ectodermal, and endodermal origin. It is found in large quantities in the brain, but is also expressed in hepatocytes, vascular smooth muscle cells, neurons of the CNS, skeletal muscle cells, fibroblasts, keratinocytes, endothelial cells, intestinal columnar epithelial cells, and pituitary basophils and acidophils. FGF-acidic is secreted as a disulfide-linked homodimer and is stored in complex with heparan sulfate, a requirement for its interaction with FGF receptors (Guerrini et al.; Mohammadi et al.). Internalized FGF-acidic signals through protein kinase C and promotes cell survival by inhibiting p53 and proapoptotic signaling (Bouleau et al.).

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Interleukin 22 (IL-22) is a class 2 α-helical cytokine that signals through the class 2 cytokine receptor and activates the JAK/STAT pathway. IL-22 is secreted by Th1, Th2, Tc22, and γδ T cells, dendritic, mast and NK cells. It stimulates expression of antimicrobial peptides from epithelial cells, thus hindering bacterial infections. Depending on the interactions with other cytokines, IL-22 can either promote inflammation or prevent tissue destruction by regulating host defense and tissue homeostasis at barrier surfaces (Sonnenberg et al.).

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Interleukin 33 (IL-33) is a pro-inflammatory cytokine from the IL-1 family. It binds to the ST2 receptor and activates NF-kB and MAPK pathways. IL-33 is expressed by epithelial cells, smooth muscle cells, and fibroblasts in various tissues and organs, as well as resting basophils, mast cells, eosinophils, natural helper cells, group 2 innate lymphoid cells, dendritic cells, and activated macrophages (Schmitz et al.; Yasuda et al.). It contributes to allergic inflammation by stimulating production of the cytokines IL-4, IL-5, and IL-13 in Th2 cells, and stimulates host defense against microbial and viral infections (Liew; Yasuda et al.). In the central nervous system, IL-33 is produced by endothelial cells and astrocytes. It induces proliferation of microglia and mediates production of pro-inflammatory cytokines (Yasuoka et al.).

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Interleukin 13 (IL-13) is a type I cytokine, and signals through type I cytokine receptors to activate JAK/STAT and IRS-1/IRS-2 pathways. IL-13 is produced by T cells and innate lymphoid cells (Pulendran and Artis) and it inhibits production of pro-inflammatory cytokines, prostaglandins, and reactive oxygen and nitrogen species by monocytes and macrophages (Hershey). Unlike human B cells, IL-13 has no effect on mouse B cell development and function. IL-13 promotes eosinophil survival, activation, and recruitment, and also activates mast cells (Hershey). IL-13 regulates gastrointestinal parasite expulsion, airway hyperresponsiveness, allergic inflammation, tissue eosinophilia, goblet cell hyperplasia, intracellular parasitism, tissue remodeling, tumor cell growth, and fibrosis. IL-13 induces hypercontractility of smooth muscles by directly acting on the muscle cells as well as the enteric nerves (Wynn).

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Fibroblast growth factor 7 (FGF-7) is a member of the FGF family, and acts exclusively through a subset of FGF receptor isoforms expressed predominantly by epithelial cells (Finch and Rubin). FGF-7 seems to act specifically on epithelial cells and stimulates proliferation, migration, and differentiation of these cells, and also participates in epithelial protection and repair both in vitro and in vivo (Finch and Rubin; Werner). In contrast, FGF-7 is produced solely by cells of mesenchymal origin, and functions as a paracrine mediator of mesenchymal-epithelial communication (Rubin et al.). FGF-7 has also been shown to supplement several wound-healing properties of bioengineered skin (Erdag et al.) and to induce autophagy in human keratinocytes (Belleudi et al.). Additionally, FGF-7 has a role in pluripotent stem cell differentiation to endodermal pancreatic-like insulin-producing cells and thymic epithelial cells (Inami et al.; Niu et al.).

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Interleukin 7 (IL-7) is a member of the type I cytokine family that is critical for T and B cell development and survival. It is produced by non-hematopoietic cells in the thymus, lymphoid organs, and by bone marrow stromal cells (Lundström et al.). IL-7 binds to a receptor (IL-7R) composed of common gamma chain and IL-7Ra (CD127) and signals through the JAK/STAT and PI3K pathways. IL-7 regulates the survival of naïve and memory CD4+ and CD8+ T cells, γδ T cells, NK T cells, innate lymphoid cells, and regulatory T cells (Carrette and Surh). Although a deficiency in IL-7R still permits the generation of normal numbers of peripheral B cells in humans, stimulation of human B cell precursors with IL-7 could promote STAT5-dependent proliferation and survival in vitro (Clark et al.; Corfe and Paige). This product is animal component-free.

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Interleukin 12 (IL-12p70) is a heterodimeric cytokine composed of p35 and p40 subunits. IL-12 is produced by monocytes, macrophages, dendritic cells, neutrophils, and B cells in response to bacterial products and cytokines such as IFN-γ. The IL-12 receptor is expressed on T, NK, and dendritic cells. Upon binding, IL-12 initiates signaling via the JAK/STAT signaling pathway and stimulates NK, B, and T cells to produce IFN-γ (Watford et al.). It also regulates cytokine synthesis, proliferation of T and NK cells, and stimulates differentiation of CD4+ and CD8+ T cells (Germann and Rüde). Mice that are deficient in IL-12 are susceptible to many intracellular pathogens and have impaired IFN-γ secretion, Th1 differentiation, and NK cytolytic activity; however, Th2 development and IL-4 production are enhanced (Watford et al.).

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Interleukin 10 (IL-10) is the founding member of the IL-10 family of class II cytokines. All of the IL-10 cytokine family members have a four-helix bundle consisting of α-helical folds. Upon binding to its receptor, IL-10 activates signaling through JAK1 and STAT3. It is produced by dendritic cells, macrophages, and CD4+ T cells, as well as mast cells, NK cells, neutrophils, and B cells, under specific stimulating conditions (Saraiva and O'Garra). IL-10 can inhibit the expression of pro-inflammatory cytokines and promote healing processes, and is important for the function of regulatory T cells. IL-10 also enhances B cell proliferation, immunoglobulin secretion, and class II MHC expression, while IL-10 produced by macrophages inhibits activation of neighboring macrophages, thus allowing a level of self-regulation (Ouyang et al.).

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Stimulating T cells with HIV-1 (B Gag) peptide pool releases downstream cytokines and upregulates activation markers, enabling antigen-specific T cells to be detected or isolated for analysis. HIV-1 (B Gag) Peptide Pool is a lyophilised mixture of 123 peptides from the gag polyprotein of human immunodeficiency virus 1 (HIV-1). The pool consists of 15-mer peptides with 11-amino-acid overlaps that cover amino acids 1 to 500 on gag polyprotein. The HIV-1 gag polyprotein is a key mediator of viral particle assembly (Campbell and Rein; Dong et al.), and together with the endosomal sorting complexes required for transport (ESCRT), results in budding during virion release (Carlson et al.). Viral peptide pools are useful for a broad range of applications, including vaccine development, immunological research, and diagnostic assay development.

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Heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) is a member of the EGF family (Nishi and Klagsbrun). HBEGF promotes blastocyst adhesion to the uterine wall (Iwamoto and Mekada). It also plays a role in smooth muscle cell hyperplasia and brain injury (Nishi and Klagsburn). HBEGF produced by CD4+ T cells promotes wound healing by stimulating migration and proliferation of keratinocytes, fibroblasts, and smooth muscle cells (Blotnick et al.). It binds to EGFR, ErbB4, ErbB2, and ErbB3, activating the PI3K/AKT signaling cascade (Iwamoto and Mekada). HBEGF is produced in a variety of cells, where it contributes to physiological and pathological processes. HBEGF is overexpressed in ovarian, breast, gastric, colorectal, pancreatic, and endometrial cancers, which likely contributes to pathogenesis (Miyata et al.). This product is animal component-free.

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SARS-CoV-2 Recombinant Spike Protein, aa319-541 is expressed in Pichia pastoris and is one of four structural proteins encoded by the SARS-CoV-2 genome. The Spike Protein plays a key role in attachment to host cells allowing invasion through clathrin-mediated endocytosis. The spike protein can be cleaved by host cell proteases after aa685 to yield the N-terminal S1 subunit, and C-terminal S2 region. The S1 subunit is responsible for interacting with the host cell receptor (angiotensin-converting enzyme II) through a receptor-binding domain that is highly conserved with SARS-CoV. The S1 subunit has two conformations: a ‘down’ conformation in which the receptor is inaccessible, and an ‘up’ conformation in which the receptor is accessible. These conformational changes are key for monoclonal antibody drugs and vaccine development. At the amino terminus of the polypeptide chain, SARS-CoV-2 Recombinant spike protein contains a polyhistidine tag and a SUMOstar site.

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Lipocalin-2 (LCN2) is a member of the lipocalin superfamily, which share a highly conserved fold containing an eight-stranded antiparallel beta barrel (Flower), and transport small hydrophobic molecules. Playing a role in innate immunity, Lipocalin-2 acts as a potent bacteriostatic reagent by sequestering iron-containing siderophores (Flo et al.). It is mainly expressed in activated neutrophils, but is also secreted by other immune cells in response to infection. Lipocalin-2 has been implicated in multiple cellular processes, such as differentiation (Yang et al.), migration (Du et al.), and apoptosis (Devireddy et al.). In vitro studies suggest that lipocalin-2 is a potential therapeutic target for certain cancers, including colorectal cancer (CRC; Zhang et al.) and chronic lymphocytic leukemia (Bauvois et al.). This protein product contains a His-residue tag at the carboxyl end of the polypeptide chain. For consistency and reproducibility across your applications, lipocalin-2 from STEMCELL comes lyophilised with ≥94% purity, and endotoxin levels are verified to be ≤1.0 EU/μg protein.

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Amphiregulin is a member of the epidermal growth factor (EGF) family. It binds to several receptors including EGFR/ErbB1, HER2/ErbB2, HER3/ErbB3, and HER4/ErbB4, which activates Ras/Raf/MAPK and PI3K/AKT pathways. This results in cell proliferation, apoptosis resistance, and invasive behaviour (Normanno et al.). The expression of amphiregulin is induced by tissue injury and inflammation. Amphiregulin promotes mammary development, trophoblast growth, lung and kidney branching morphogenesis, and keratinocyte proliferation. It stimulates the growth of most cell types, including normal and transformed mammary epithelial cells, and malignant cells of the colon, prostate, cervix, and pancreas (Berasain and Avila).

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Vascular endothelial growth factor D (VEGF-D) is a member of the VEGF/platelet-derived growth factor (PDGF) family of proteins. VEGF-D is a potent angiogenic factor and promotes lymphangiogenesis, endothelial cell growth and survival, and can affect blood vessel permeability. VEGF-D is expressed in the lung, heart, small intestine, fetal lung, and at lower levels in the pancreas, colon, and skeletal muscle (Otrock et al.; Roy et al.; Stacker et al.; Yamada et al.). VEGF-D is a ligand for VEGF receptors 2 (Flk1) and 3 (Flt4) (Baldwin et al.). VEFGR-3 is highly expressed in lymphatic endothelial cells and is essential for their growth and differentiation (Otrock et al.; Roy et al.). Binding of VEGF-D to neuropilins contributes to VEGFR-3 signaling during lymphangiogenesis, whereas binding to integrin α9β1 promotes endothelial cell adhesion and migration (Roy et al.; Otrock et al.). During embryogenesis, VEGF-D also plays a role in the formation of the venous and lymphatic systems.

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Insulin-like growth factor 1 (IGF-I) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-I binds to the IGF-I receptor and is a potent activator of the PI3K/AKT pathway and also activates ERK1/2 signaling. IGF-I is required for embryonic development, and it is produced mainly in the liver in response to a hepatocyte growth hormone. In the absence of insulin, IGF-I is necessary for the maintenance of human pluripotent stem cells (Wang et al.). Together with IL-3, IGF-I stimulates differentiation and proliferation of myeloid cells and has been shown to regulate lymphopoiesis by stimulating proliferation and differentiation of T and B cells in lymphoid organs (Heemskerk et al.).

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Basic fibroblast growth factor (bFGF) is a prototypic member of the fibroblast growth factor family. Cytokines in the FGF family possess broad mitogenic and cell survival activities (Folkman and Klagsbrun; Kimelman and Kirschner) and are involved in a variety of biological processes including cell proliferation, differentiation, survival, and apoptosis (Folkman and Klagsbrun; Klagsbrun; Rifkin and Moscatelli). bFGF has the β-trefoil structure (Ponting and Russell), binds to the four FGF receptor (FGFR) family members, and activates JAK/STAT, PI3K, ERK1/2, and other receptor tyrosine kinase (RTK) signaling pathways. It supports the maintenance of undifferentiated human pluripotent stem cells (Xu et al.; Kang et al.), stimulates human pluripotent stem cells to form neural rosettes (Zhang et al.), and improves proliferation of human mesenchymal stem cells and enhances chondrogenic differentiation (Solchaga et al.). This version of bFGF is the full-length bFGF protein encoded by the human FGF2 gene consisting of 154 amino acid residues. This product is animal component-free.

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Sonic hedgehog (Shh) is a member of the Hedgehog family of secreted signaling proteins that has a prominent role in patterning during early mammalian development (Ho and Scott). It is expressed during early embryogenesis in a variety of tissues (Finco et al.). During patterning of the central nervous system, Shh directly acts on cells to specify neural cell fates, regulates proliferation and survival of oligodendrocyte precursors and neural crest cells and stimulates proliferation, differentiation, and axon growth (Ho and Scott; Martí). Shh also regulates T cell differentiation and activation (Crompton et al.). Recombinant Mouse Shh is a fully biologically active molecule.

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Interleukin 3 (IL-3) is a species-specific pleiotropic cytokine that promotes the survival and proliferation of pluripotent hematopoietic stem cells and lineage-committed progenitor cells and their differentiation into mature cells of most lineages, including basophils, neutrophils, eosinophils, macrophages, dendritic cells, erythrocytes, and megakaryocytes (Yang et al.; Dorssers et al.; Broughton et al.). IL-3 is produced by activated T cells and has a physiological role in inflammation and allergies by promoting the secretion of inflammatory mediators such as histamine, IL-4, and IL-6 by basophils and eosinophils (Broughton et al.). The IL-3 receptor consists of a unique alpha subunit (CD123) and a beta common subunit (βc or CD131) that is shared with the receptors for IL-5 and GM-CSF, and is the principal signal transduction subunit for these cytokines. IL-3 binding to the heterodimeric receptor activates JAK/STAT, MAPK, and PI3K signaling pathways (Woodcock et al.). This product is animal component-free.

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Insulin-like growth factor 2 (IGF-II) is a polypeptide that belongs to the family of insulin-like growth factors that are similar in molecular structure to proinsulin. IGF-II binding to IGF-I receptor activates a signaling cascade via the MAPK and PI3K pathways. IGF-II affects growth, differentiation, and survival of cells in a variety of tissues during embryonic development. It stimulates proliferation and migration of primary lymphatic endothelial cells, and induces lymphangiogenesis (Guvakova).

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Use omentin for the maintenance of insulin sensitivity and metabolism, decreasing levels of this adipokine have been associated with obesity, insulin resistance, and diabetes (Tan et al.). Studies have suggested that omentin may have protective effects against atherosclerosis, arterial calcification, and myocardial injury through AMP-activated protein kinase (AMPK) and Akt-dependent mechanisms (Xu et al., Kataoka et al.). Through regulation of Sirt1-dependent p53 deacetylation, omentin can inhibit proliferation and induce apoptosis in hepatocellular carcinoma cells (Zhang and Zhou). Omentin is mainly produced by visceral adipose tissue, but is also expressed in the small intestine, colon, mesothelial cells, vascular cells, and plasma (Watanabe et al). Protein sequence analysis has shown that omentin comprises 313 amino acids, with a secretory signal sequence and fibrinogen-related domain (Yang et al.). For consistency and reproducibility across your applications, Omentin from STEMCELL comes lyophilised with ≥90% purity, and is verified by LAL analysis to ensure endotoxin levels are ≤5,0 EU/μg protein.

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SARS-CoV-2 Recombinant Spike Protein, aa16-685 is expressed in HEK293 cells and is one of four structural proteins encoded by the SARS-CoV-2 genome. The Spike Protein plays a key role in attachment to host cells, allowing invasion through clathrin-mediated endocytosis. The Spike Protein can be cleaved by host cell proteases after aa685 to yield the N-terminal S1 subunit and C-terminal S2 region. The S1 subunit is responsible for interacting with the host cell receptor (angiotensin-converting enzyme II) through a receptor-binding domain that is highly conserved with SARS-CoV. The S1 subunit has two conformations: a ‘down’ conformation in which the receptor is inaccessible, and an ‘up’ conformation in which the receptor is accessible. These conformational changes are key for monoclonal antibody drugs and vaccine development. SARS-CoV-2 Recombinant Spike Protein contains a polyhistidine tag at the amino terminus; it also contains a FLAG tag at the carboxy terminus.

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Interleukin 2 (IL-2) is a monomeric cytokine that was originally identified as a T cell growth factor (Gaffen and Liu). It binds to a heterotrimeric receptor consisting of CD25, CD122, and CD132. Upon binding, it activates JAK3-, STAT5-, and AKT-dependent signaling pathways, which results in cellular proliferation and survival (Ma et al.). The majority of IL-2 is secreted by activated CD4+ and CD8+ T cells, although B cells and dendritic cells were found to produce IL-2 in small amounts. IL-2 downregulates immune responses to prevent autoimmunity during thymic development, influences the development of CD4+CD25+ regulatory T cells, and affects development of follicular helper T cells. IL-2 also controls inflammation by inhibiting Th17 differentiation (Banchereau et al.). Targeted deletions of the IL-2 gene in mice resulted in development of autoimmune hemolytic anemia, followed by ulcerative colitis. Similar effects were observed in mice that were deficient in IL-2 receptor α (Gaffen and Liu).

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Human Recombinant Angiotensin-Converting Enzyme 2 (ACE2) Protein, aa18-740, is expressed in HEK293 cells. ACE2 activity results in vasodilation by degrading vasoconstrictor angiotensin II to produce vasodilator angiotensin. Decreased expression of this enzyme is associated with cardiovascular disease and possibly also glomerular injury in diabetic nephropathy. ACE2 contains a peptidase domain at the N-terminus and a single transmembrane helix. ACE2 is also the primary human receptor for the surface spike glycoprotein of SARS-CoV-2 and SARS-CoV. This receptor is expressed in human lung and small intestine epithelia as well as the heart, kidney, and testes. The peptidase domain of ACE2 binds to the protein-binding domain of the S1 protein subunit of the spike protein; this binding results in a cleavage site becoming exposed. Cleavage, or ‘protein priming’, is done by TMPRSS2, a cellular serine protease, and by cathepsins. This cleavage activates the S2 subunit of the spike protein, allowing the fusion of the viral membrane to the host cell membrane. At the carboxy terminus, Human Recombinant ACE2 Protein contains a TEV site and a human IgG1 Fc tag.

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TRAIL (TNF-related apoptosis-inducing ligand) belongs to the tumor necrosis factor (TNF) superfamily and is associated with initiating apoptosis. TRAIL has four major receptors: two death receptors DR4 and DR5, and two decoy receptors DcR1 and DcR2. TRAIL binds to the death receptors, which recruits the Fas-associated death domain (FADD) and activates caspases 8 and 10, which eventually leads to apoptosis (Pitti et al.; Wiley et al.; Zauli and Secchiero). It has been shown that mice lacking the expression of TRAIL have defects in thymocyte apoptosis and negative selection, and these mice had increased susceptibility to autoimmune diseases (Lamhamedi-Cherradi et al.).

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Epidermal growth factor (EGF) is the founding member of the EGF family of proteins and is characterized by high affinity binding to various EGF receptors (EGFRs) and the production of mitogenic responses (Carpenter and Cohen). EGF promotes EGFR dimerization, resulting in activation of downstream pathways including PI3K, ERK1/2, JAK/STAT, β-catenin, and calcium signaling. EGF is secreted by the gut-associated salivary and Brunner’s glands, is found in a variety of body fluids, and stimulates cell proliferation and differentiation in rodent and neonatal human intestine (Wright et al.). EGF can stimulate the proliferation of mouse embryonic stem cells or induce the terminal differentiation/growth inhibition of A431 cells (Heo et al.).

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Interleukin 22 (IL-22) is a class 2 α-helical cytokine that signals through the class 2 cytokine receptor and activates the JAK/STAT pathway. IL-22 is secreted by Th1, Th2, Tc22, and γδ T cells, dendritic, mast and NK cells. It stimulates expression of antimicrobial peptides from epithelial cells, thus hindering bacterial infections. Depending on the interactions with other cytokines, IL-22 can either promote inflammation or prevent tissue destruction by regulating host defense and tissue homeostasis at barrier surfaces (Sonnenberg et al.).