H_Products

CXCL17 is a CXC chemokine appearing to lack the ELR motif, yet functioning as a chemokine that does contain the ELR motif as it plays a role in angiogenesis and is chemotactic for neutrophils. It also plays a role in regulation of mucosal inflammatory responses and is chemotactic for macrophages, monocytes, dendritic cells, and immature myeloid-derived cells. CXCL17 is coregulated with VEGF and may play a role in regulating tumorigenesis through angiogenesis. CXCL17 expression has been observed in several tissues, but appears to be restricted to mucosal sites such as the digestive system, lung airways, the urethra, and different sites of the female reproductive system. CXCL17 is a ligand for the receptor GPR35.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

CXCL2 is an ELR type of CXC chemokine. It is secreted by monocytes and macrophages and expressed in a variety of other cells. CXCL2 participates in chemotaxis of polymorphonuclear leukocytes and hematopoietic stem cells. It plays a role in would healing, angiogenesis, tumorigenesis, and pathogenesis of airway remodeling in asthma. CXCL2 exhibits antimicrobial activity against E. coli and S. aureus. CXCR2 is the receptor that CXCL2 binds. The amino acid sequence of CXCL2 is significantly homologous to that of CXCL1.

CXCL3 is an ELR type of CXC chemokine. It is secreted by monocytes and macrophages and expressed in a variety of other cells. CXCL3 participates in chemotaxis and cell activation of neutrophils. CXCL3 is a ligand for CXCR2. It plays a role in would healing, inflammation, angiogenesis, tumorigenesis, metastasis, and pathogenesis of airway remodeling in asthma. CXCL3 has an effect on the differentiation and function of human monocyte-derived dendritic cells, pushing them towards a myeloid-derived suppressor cell (MDSC)-like phenotype. CXCL3 exhibits antimicrobial activity against E. coli and S. aureus.

CXCL5 is an ELR type of CXC chemokine. It is expressed in various epithelial cell lines alongside CXCL8 (IL8) and CXCL1 in response to stimulation by IL1 or TNF-alpha. It is down regulated by IFN-gamma. Like many CXC chemokines, CXCL5 is a ligand for CXCR2. It is a chemoattractant and activator of neutrophils, and plays a role in angiogenesis and inflammation, as well as the metastasis of various cancers. It also blocks insulin signaling by activating the JAK2/STAT5/SOCS2 pathway.

CXCL5 is an ELR type of CXC chemokine. It is expressed in various epithelial cell lines alongside CXCL8 (IL8) and CXCL1 in response to stimulation by IL1 or TNF-alpha. It is down regulated by IFN-gamma. Like many CXC chemokines, CXCL5 is a ligand for CXCR2. It is a chemoattractant and activator of neutrophils, and plays a role in angiogenesis and inflammation, as well as the metastasis of various cancers. It also blocks insulin signaling by activating the JAK2/STAT5/SOCS2 pathway. The truncated form of CXCL5 (8-78 a.a.) has been reported as being 3-fold more potent than the full length protein (1-78 a.a.).

CXCL9 is a CXC chemokine lacking the ELR motif. It is expressed in and secreted by macrophages, epithelial cells, and other cell types after induction by IFN-gamma. It is chemotactic for stimulated T-cell lymphocytes and plays a role in T-cell activation, angiostasis, inhibition of neovascularization, and inhibition of hematopoietic progenitor cells. CXCL9 is most closely related to CXCL10 and CXCL11, all three of which are ligands for CXCLR3.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

Cysteine-rich angiogenic inducer 61 (Cyr61) is a dynamically expressed, multifunctional matricellular protein of the CCN family encoded by the Cyr61 gene. Cyr61 is critical for cardiovascular development during embryogenesis and regulates inflammation, wound healing and fibrogenesis in the adult. It is involved in cell adhesion, cell migration, cell proliferation, and cell differentiation. Cyr61 consists of four domains: an IGFBP domain, a VWF type C domain, a TSP type I domain, and a cysteine knot domain.

Human beta-defensin 1 (DEFB1) is an antimicrobial peptide that contributes to the innate and adaptive immune system and is active against bacteria, fungi, and viruses. Like the other β-defensins, DEFB1 is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is constitutively expressed in epithelial cells, mainly of the kidney and the female reproductive tract, as well as in monocytes, macrophages, and dendritic cells. DEFB1 is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB1 than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. The primary role of DEFB1 is believed to be prevention of microbial colonization on epithelia. Inhibition of DEFB1 by high salt concentration may play a role in the pathogenesis of cystic fibrosis. DEFB1 may also play a role in the pathogenesis of severe sepsis.

Human beta-defensin 103A (DEFB103A) is an antimicrobial peptide that contributes to the innate and adaptive immune systems and is active against gram-negative and gram-positive bacteria, fungi, and viruses. Like the other β-defensins, DEFB103A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed in epithelial tissue of many organs, heart and skeletal muscle tissue, and leukocytes. Expression of DEFB103A is induced by proinflammatory cytokines such as IL1B and IFNG. DEFB103A is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB103A than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. DEFB103A has been shown to have a greater positive surface charge than DEFB1 or DEFB4A, giving it greater antimicrobial activity. Inhibition of DEFB103A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Human beta-defensin 104A (DEFB104A) is an antimicrobial peptide that contributes to both the innate and the adaptive immune systems and is active against gram-negative and gram-positive bacteria, fungi, and viruses. Like the other β-defensins, DEFB104A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed at highest levels in the testis and stomach, and at lower levels in the uterus, neutrophils, thyroid, lung, and kidney. Expression of DEFB104A is upregulated by phorbol 12-myristate 13-acetate (PMA), as well as in response to infection with gram-positive and gram-negative bacteria. DEFB104A is a cationic peptide and interacts with the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). LTA and LPS have higher affinity for DEFB103A than for Ca+2 and Mg+2 ions. The larger defensin molecule displaces the smaller ion, changing the membrane structure and affecting the stability of the membrane; this can lead to the formation of pores and subsequent depolarization or lysis. DEFB104A has been shown to be more active against Pseudomonas aeruginosa than DEFB1, DEFB4A, or DEFB103A. Inhibition of DEFB104A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Human beta-defensin 4A (DEFB4A) is an antimicrobial peptide that contributes to the innate immune system and is active against gram-negative bacteria, fungi, and viruses. It also contributes to the adaptive immune system through recruitment of leukocytes to sites of infection through chemotaxis. Like the other β-defensins, DEFB4A is a small protein that contains a motif consisting of six cysteine residues which form three intramolecular disulfide bridges. It is expressed in epithelia of many organs, including the lungs and skin, as well as in monocytes and macrophages. Expression is induced by 1,25-dihydroxyvitamin D3 and proinflammatory cytokines, such as IL1B and IFNG, and downregulated by the anti-inflammatory steroid dexamethasone. DEFB4A is a cationic peptide that disrupts the membranes of invading microbes, which are negatively charged due to the presence of lipopolysaccharides (LPS) or lipoteichoic acid (LTA). DEFB4A stimulates mast cells to induce Ca2+ mobilization, histamine release, and COX-1 mediated prostaglandin D2 release in a G-protein-dependent and phospholipase C-dependent manner. Inhibition of DEFB4A by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

DL-Homocysteic acid is a glutamic acid analog and a receptor agonist of NMDA. It disrupts calcium homeostasis and induces degeneration of spinal motor neurons, and has a cytotoxic effect on the central nervous system. DL-Homocysteic acid also induces oxidative stress in brain tissues and inhibits arterial pressure, heart rate and diaphragm electromyogram activity. Complexes with DL-Homocysteic acid and cations like sodium and zinc have been synthesized.

EGF (Epidermal Growth Factor) is a family of growth factors that are derived from membrane-anchored precursors. The family is characterized by the presence of at least one “EGF-like domain” (characterized by the presence of three disulfide bonds, formed from 6 conserved cysteine residues) in their extracellular domain. EGF was originally discovered as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition and stunting of growth when injected into newborn mice. Mature human EGF shares 70% amino acid sequence identity with mature mouse and rat EGF. Human EGF was isolated from urine based on its inhibitory effect on gastric secretion and is sometimes called urogastrone.

EPGN is a member of the epidermal growth factor family and expression has been seen in several tissues, including the testis, liver, heart and certain tumor cells. It is a strong mitogen for fibroblasts and epithelial cells but has low affinity for its main receptor, ErbB1. The enhanced mitogenic potential is attributed to inefficient receptor ubiquitylation and endocytosis. EPGN stimulates phosphorylation of c- erbB-1 and MAP kinases in epithelial cells. The protein contains a conserved sequence of six cysteine residues and two N-linked glycosylation sites, with two hydrophobic regions comprised of a signal sequence and a transmembrane domain. Alternative splicing of the EPGN gene results in multiple isoforms.

EREG is a member of the epidermal growth factor (EGF) family and is expressed mainly in the placenta and peripheral blood leukocytes, as well as in certain carcinomas of the bladder, lung, kidney, and colon. EREG stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Additionally, it inhibits the growth of several tumor-derived epithelial cell lines. EREG is synthesized as a transmembrane protein and the ectodomain is cleaved by a protease to release the mature protein. The mature protein can bind to EGFR, as well as most members of the ERBB family of RTKs.

FAM19A2 (TAFA-2) is chemokine-like protein containing ten cysteine residues that are conserved amongst the FAM19A (TAFA) family. This family of proteins was first identified by using a clustering algorithm on uncharacterized cDNA sequences and found to be distantly related to C-C motif chemokines, such as CCL3. FAM19A2 is expressed predominantly in the CNS, with very low expression levels detected in colon and spleen. Expression levels of FAM19A2 are highest in the occipital and frontal cortex and it is believed to be expressed constitutively. FAM19A2 is hypothesized to function as a brain-specific chemokine that regulates immune response in the CNS, as a neurokine that modulates immune response, or as a control of axonal sprouting following brain injury.

GoldBio growth factors are manufactured for RESEARCH USE ONLY and cannot be sold for human consumption!

FGF10/KGF2 is a member of the Fibroblast Growth Factor family of proteins. KGF2 cDNA encodes a 208 amino acid residue protein with a hydrophobic amino-terminal signal peptide. Human KGF2 shares 92% and 95% amino acid sequence identity with mouse and rat KGF2, respectively. In the FGF family, KGF2 is most closely related to FGF7 (KGF1), FGF3 and FGF22 (see additional information). The expression of KGF2 transcript has been shown to be most abundant in the embryo and adult lung. Recombinant KGF2 has been shown to be mitogenic for epithelial and epidermal cells but not fibroblasts. KGF2 may play unique roles in brain and lung development, wound healing and limb bud formation.

FGF13 is a member of the Fibroblast Growth Factor family of proteins. It is one of four FGFs that act as intracellular signaling molecules, independent of FGF receptors. They have instead been shown to interact with voltage-gated ion channels and the MAPK scaffold protein, islet-brain 2. FGF13 is expressed in the developing and adult central nervous system and acts to stabilize microtubules. It is required for axon and leading process development, as well as neuronal migration. It is believed to be a candidate gene for syndromal and nonspecific forms of X-chromosome-linked intellectual disability (XLID).

FGF19 is a member of the Fibroblast Growth Factor family of proteins. It is in the same endocrine signaling subfamily as FGF21 and FGF23 and is the human ortholog of mouse FGF15. FGF19 is a heparin-dependent ligand and binds exclusively to FGFR4. It is essential for brain and heart development, as well as the metabolism of bile acid, hepatic protein, and glycogen. FGF19 mRNA is expressed in several tissues including fetal cartilage, skin, and retina, as well as adult gall bladder and is overexpressed in a colon adenocarcinoma cell line.