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Colony Stimulating Factor 3 (CSF3), formerly called granulocyte colony stimulating factor (G­CSF), is a pleiotropic cytokine. It is mainly produced by monocytes and macrophages upon activation by endotoxin, TNF­α and IFN­γ. Many cell types secreted this protein after LPS, IL1 or TNF­α activation, including fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. CSF3 is cytokine that acts in hematopoiesis by controlling the production, differentiation and function of two related white cell populations of the blood, the granulocytes and the monocytes­macrophages. In addition, it may function in some adhesion or recognition events at the cell surface.

Colony Stimulating Factor 3 (CSF3), previously known as granulocyte colony stimulating factor (G-CSF) is a pleiotropic cytokine and mainly produced by monocytes and macrophages upon activation by endotoxin, TNF-α and IFN-γ. Many cell types secreted this protein after LPS, IL-1 or TNFα activation, including fibroblasts, endothelial cells, astrocytes and bone marrow stromal cells. Various carcinoma cell lines and myeloblastic leukemia cells can express CSF3 constitutively. CSF3 is cytokine that acts in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytesmacrophages. In addition it may function in some adhesion or recognition events at the cell surface.

Rat CX3CL1 is a chemokine that is unlike most chemokines because it contains the C-X-X-X-C motif. It is expressed by neurons, endothelial cells, follicular dendritic cells, and some lymphocytes. Expression of CX3CL1 is induced by activation of the transcription factor NFKB1 through IFNG, IL1B, TNF, or LPS. CX3CL1 is chemotactic for T-cells and monocytes and plays a role in angiogenesis, as well as regulation of leukocyte traffic at the endothelium. CX3CL1 expressed by neurons suppress microglia in order to protect neurons from damage caused by reactive molecules expressed by microglia. CX3CL1 is a ligand for CX3CR1 as well as virus-encoded receptors M3 and US28.

Rat CXCL1 is an ELR type of CXC chemokine. First discovered in mouse fibroblasts, it is secreted by melanoma cells and expressed by neutrophils, monocytes, keratinocytes, macrophages, epithelial cells, and fibroblasts. CXCL1 participates in chemotaxis and cell activation of neutrophils during inflammation. CXCL1 inhibits embryonic oligodendrocyte precursor migration, suggesting a role in spinal cord development. It also plays a role in would healing, angiogenesis, and tumorigenesis. CXCL1 is believed to be the major inflammatory factor in recurrent herpetic stromal keratitis. CXCR2 is the receptor that CXCL1 binds.

Rat CXCL10 is a CXC chemokine lacking the ELR motif. It is expressed in and secreted by monocytes, endothelial cells, fibroblasts, and other cell types transiently after induction by IFNG or constitutively after induction by oncogenic Ras. It is chemotactic for monocytes and T-cell lymphocytes. CXCL10 plays a role in angiostasis, inhibits bone marrow colony formation, and promotes T-cell adhesion to endothelial cells. Knock-out mice have immune system abnormalities, including defective proliferation of T–cells, resulting in increased susceptibility to autoimmune disease and viral infections. It is closely related to CXCL9 and CXCL11, all three of which are ligands for CXCLR3. Increased expression of CXCL10 and CXCR3 is associated with autoimmune myasthenia gravis.

CXCL10 is a CXC chemokine lacking the ELR motif. It is expressed in and secreted by monocytes, endothelial cells, fibroblasts, and other cell types after induction by interferon gamma and may be an important mediator of inflammatory response to interferons. It is chemotactic for monocytes and T-cell lymphocytes. CXCL10 plays a role in angiostasis, inhibits bone marrow colony formation, and promotes T-cell adhesion to endothelial cells. CXCL10 also exhibits antimicrobial properties against Gram-positive and Gram-negative bacteria. It is closely related to CXCL9 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!

Rat CXCL12 is a CXC chemokine lacking the ELR motif. It was first found in bone marrow stromal cells and is expressed in bone marrow stromal cells constitutively as well as a wide variety of cells with the exception of blood cells. Expression of CXCL12 is downregulated in fibroblasts by the phorbol ester TPA and in serum-deprived fibroblasts that have been stimulated by serum. CXCL12 acts as a ligand for CXCR4 and CXCR7. It is chemotactic for hematopoietic progenitor cells expressing CD34, mononuclear cells, and cerebellar granule cells. CXCL12 plays a role in lymphopoiesis, myelopoiesis, vascularization of the gastrointestinal tract, and cerebellar development. CXCL12-alpha is one of six alternatively spliced isoforms of the CXCL12 gene. It is four amino acids shorter at the C-terminus than the canonical sequence, CXCL12-beta.

Rat CXCL12 is a CXC chemokine lacking the ELR motif. It was first found in bone marrow stromal cells and is expressed in bone marrow stromal cells constitutively as well as a wide variety of cells with the exception of blood cells. Expression of CXCL12 is downregulated in fibroblasts by the phorbol ester TPA and in serum-deprived fibroblasts that have been stimulated by serum. CXCL12 acts as a ligand for CXCR4. It is chemotactic for hematopoietic progenitor cells expressing CD34, mononuclear cells, and cerebellar granule cells. CXCL12 plays a role in lymphopoiesis, myelopoiesis, vascularization of the gastrointestinal tract, and cerebellar development. CXCL12-beta is one of six alternatively spliced isoforms of the CXCL12 gene and is used as the canonical sequence.

Rat CXCL14 is a CXC chemokine lacking the ELR motif. It is expressed constitutively in many normal tissues, including brain, lung, ovaries, kidneys, and muscle. CXCL14 is chemotactic for monocytes, macrophages, dendritic cells, activated NK cells, and B cells. It possesses tumor suppressing function in certain cancers possibly due to migrations of NK cells, inhibition of angiogenesis, and reduction of settlement rate of tumor cells. However in contradiction, it can induce tumor growth in other types of cancers. CXCL14 is a natural antagonist for CXCR4 and inhibits CXCL12.

Rat 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 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.

Rat CXCL2 is an ELR type of CXC chemokine. It is secreted by monocytes and macrophages and expressed in a variety of other cells. Expression of CXCL2 is induced by IL1, TNF, and LPS. CXCL2 participates in chemotaxis of neutrophils, basophils, 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. CXCL2 is a ligand for CXCR2. CXCL2 shares significant amino acid sequence homology with CXCL1.

Rat CXCL3 is an ELR type of CXC chemokine. It is secreted by monocytes and macrophages and expressed in a variety of other cells. As a result of alternative splicing, there are two isoforms of rat CXCL3 that differ from each other by three amino acid residues. This recombinant rat CXCL3 is the canonical sequence often referred to as CXCL3A or CINC2A. CXCR2 is the receptor that CXCL3 binds. CXCL3 participates in chemotaxis and cell activation of neutrophils. 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 monocyte-derived dendritic cells, pushing them towards a myeloid-derived suppressor cell (MDSC)-like phenotype.

Rat CXCL3 is an ELR type of CXC chemokine. It is secreted by monocytes and macrophages and expressed in a variety of other cells. As a result of alternative splicing, there are two isoforms of rat CXCL3 that differ from each other by three amino acid residues. This recombinant rat CXCL3 isoform is often referred to as CXCL3B or CINC2B. CXCR2 is the receptor that CXCL3 binds. CXCL3 participates in chemotaxis and cell activation of neutrophils. 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 monocyte-derived dendritic cells, pushing them towards a myeloid-derived suppressor cell (MDSC)-like phenotype.

Rat CXCL6 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 IFNG. Rat CXCL6 is a ligand for Rat CXCR1. 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. Rat CXCL6 has also been referred to as rat CXCL5 and is an ortholog of human CXCL5 and CXCL6, as well as murine CXCL5.

Raffinose is a natural trisaccharide composed of galactose, glucose and fructose. It primarily serves as a carbon source for yeast as well as being an important component in some cryopreservation solutions.

Additionally, it is known to improve digestion and increase the absorption of calcium.

Raffinose is naturally found in a variety of vegetables and grains, and is hydrolyzed by α-gal.

D-Ribose is an aldopentose monosaccharide. It is phosphorylated into D-ribose 5-phosphate by ribokinase and then supports the synthesis of tryptophan and histidine. Additionally, D-ribose 5-phosphate is part of the pentose phosphate pathway. D-Ribose may be used as a cell culture media supplement.

Rat beta-defensin 1 (DEFB1) is an antimicrobial peptide that contributes to the innate and adaptive immune systems 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 tissue, mainly of the respiratory and genitourinary tract, as well as in monocytes, macrophages, and dendritic cells. DEFB1 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). 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 is abnormally expressed in Goto-Kakizaki (GK) rats suggesting a role of DEFB1 in diabetic nephropathy.

Rat beta-defensin 3 (DEFB3) 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, DEFB3 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, including the skin and lungs, and in leukocytes. Expression of DEFB3 is induced by proinflammatory cytokines such as IL1B and IFNG. Expression of rat DEFB3 was also found to be induced in bronchoalveolar lavage fluid by inflammatory diesel exhaust particles. DEFB3 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). Inhibition of DEFB3 by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

Rat beta-defensin 4 (DEFB4) 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, DEFB4 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 lung and skin, as well as in monocytes and macrophages. Expression is induced by proinflammatory cytokines, such as IL1B and IFNG. DEFB4 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). DEFB4 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. DEFB4 also stimulates cholinergic Ca2+-dependent epithelial Cl- secretion. Inhibition of DEFB4 by high salt concentration may play a role in the pathogenesis of cystic fibrosis.

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. Additionally, EGF has been shown to inhibit gastric secretion, is involved in wound healing and signals through a receptor known as c-erbB (a class I tyrosine kinase receptor).