Search results for: Recombinant Human HGF [from CHO cells] Proteins
#31013780 // Save this To Up
Anti-Apoptotic Effects of Recombinant Human Hepatocyte Growth Factor on Hepatocytes Were Associated with Intrahepatic Hemorrhage Suppression Indicated by the Preservation of Prothrombin Time.Hepatocyte growth factor (HGF) is an endogenously expressed bioactive substance that has a strong anti-apoptotic effect. In this study, we biochemically and histologically characterized the effects of rh-HGF on in vitro human hepatocyte injury and mouse acute liver failure (ALF) models, both of which were induced by antibody-mediated Fas signaling. rh-HGF inhibited intracellular caspase-3/7 activation and cytokeratin 18 (CK-18) fragment release in both models. Histologically, rh-HGF dramatically suppressed parenchymal damage and intrahepatic hemorrhage. Among the laboratory parameters, prothrombin time (PT) was strongly preserved by rh-HGF, and PT was well correlated with the degree of intrahepatic hemorrhage. These results showed that the anti-apoptotic effect of rh-HGF on hepatocytes coincided strikingly with the suppression of intrahepatic hemorrhage. PT was considered to be the best parameter that correlated with the intrahepatic hemorrhages associated with hepatocellular damage. The action of rh-HGF might derive not only from its anti-apoptosis effects on liver parenchymal cells but also from its stabilization of structural and vasculature integrity.
1576 related Products with: Anti-Apoptotic Effects of Recombinant Human Hepatocyte Growth Factor on Hepatocytes Were Associated with Intrahepatic Hemorrhage Suppression Indicated by the Preservation of Prothrombin Time.RABBIT ANTI HUMAN SDF-1 A Rabbit Polyclonal Antibod Growth Differentiation Fa Recombinant Human Vascula Fibroblast Growth Factor Sheep Polyclonal Antibody Rabbit Polyclonal Antibod Recombinant Human Platele Fibroblast Growth Factor Sheep Polyclonal Antibody Rabbit Polyclonal Antibod Growth Differentiation Fa
#30107380 // Save this To Up
Isolation and Characterization of a Chinese Hamster Ovary Heparan Sulfate Cell Mutant Defective in Both Met Receptor Binding and Hepatocyte Growth Factor NK1/Met Signaling.The up-regulation of hepatocyte growth factor/receptor, HGF/Met, signal transduction is observed in most of human cancers. Specific heparan sulfate structures enhance the HGF/Met signaling at both cell and animal-based model systems. Biochemical studies indicate that heparan sulfate interacts with HGF and a natural occurring splicing variant NK1 of HGF with similar affinity. However, it is currently unknown if cell surface heparan sulfate binds to Met at physiological conditions and if specific cell surface heparan sulfate structures are required for effective HGF/Met or NK1/Met signaling.
1494 related Products with: Isolation and Characterization of a Chinese Hamster Ovary Heparan Sulfate Cell Mutant Defective in Both Met Receptor Binding and Hepatocyte Growth Factor NK1/Met Signaling.IGF-1R Signaling Phospho- Cell Meter™ Annexin V B Cell Meter™ Live Cell C Rat monoclonal anti mouse Cell Meter™ Intracellul Ovary serous papillary ad Cell Meter™ Annexin V B Cell Meter™ Fluorimetri Cell Meter™ Live Cell C Rat monoclonal anti mouse Cell Meter™ Annexin V B Cell Meter™ Live Cell C
#29115510 // Save this To Up
HGF induces the serine‑phosphorylation and cell surface translocation of ROMK (Kir 1.1) channels in rat kidney cells.Extracellular potassium homeostasis is dependent on the activity of potassium channels, which are expressed on the apical membrane of epithelial tubular cells. The renal outer medullary potassium channel (ROMK) is considered to be the major route for potassium transport into the tubule lumen. Hepatocyte growth factor (HGF) exerts multiple biological activities and is important for maintaining renal homeostasis. It is also anti‑apoptotic and mitogenic for protection and recovery from ARF. Whether HGF regulates the ion channel activities remains to be elucidated, therefore, the present study aimed to investigate the modulation of HGF on the expression of ROMK in cultured renal tubular cells. NRK‑52E cells were treated with recombinant HGF, however, no alterations in the total expression of ROMK were observed by western blot analysis. In examining the serine 44 phosphorylation of ROMK in NRK‑52E cells, the present study observed that HGF enhanced the serine 44 phosphorylation of ROMK. In addition, to investigate whether HGF‑Met signaling induces the movement of ROMK to the cell surface in NRK‑52E cells, the protein constituents of cells were separated into plasma membrane and cytoplasm. Using immunofluorescence assay, the expression of ROMK on the plasma membrane was increased in the HGF‑treated NRK‑52E cells, which suggested that ROMK was translocated to the plasma membrane following the HGF‑induced phosphorylation of serine 44. Therefore, HGF may be important in potassium excretion and perform antihyperkalemic effects through the translocation of potassium channels.
2659 related Products with: HGF induces the serine‑phosphorylation and cell surface translocation of ROMK (Kir 1.1) channels in rat kidney cells.superSf9-3 insect cells Cell Cycle Phospho-Specif Macrophage Colony Stimula Human Large Intestine Mic MarkerGeneTM in vivo lacZ GLP 2 ELISA Kit, Rat Prog Sf21 insect cells Kidney clear cell carcino Octyl â D 1 thioglucopyr Nile Red, A lipophilic dy T-Cell Receptor Signaling GFP Expressing Human Inte
#28045643 // Save this To Up
Production of human mutant biologically active hepatocyte growth factor in Chinese hamster ovary cells.Hepatocyte growth factor (HGF) is a potent multifunctional cytokine that affects proliferation, migration, and morphogenesis of various cells. HGF is secreted as an inactive single-chain precursor protein and activated by the cleavage of serine proteases to form heterodimers. In our current study, the cleavage site of HGF was blocked by replaced Arg 494 of Glu (R494E) that resulted in the single-chain HGF (R494E) unable to be cleaved by serine proteases. We established Chinese hamster ovary (CHO) cells overexpressing HGF (R494E), the expression of HGF (R494E) achieved 12 mg/L and was similar to a previously reported study. The recombinant protein was then purified from culture medium using a two-step chromatographic procedure that resulted in about a 40% recovery rate. The purified HGF (R494E) was obtained as a single-chain active protein. It concluded that HGF (R494E) exhibited a biologically active protein and the overexpressing CHO cell line supplied sufficient material for future studies. The R494E replacement of the cleavage site would be beneficial to the utility of other similar therapeutic proteins.
2294 related Products with: Production of human mutant biologically active hepatocyte growth factor in Chinese hamster ovary cells.Epidermal Growth Factor ( Epidermal Growth Factor ( Fibroblast Growth Factor Macrophage Colony Stimula Goat Anti-Human Fibroblas Epidermal Growth Factor ( Keratinocyte Growth Facto Fibroblast Growth Factor Growth Factor (Human) Ant Human Insulin-like Growth Hamster anti mouse Insuli Fibroblast Growth Factor
#26011014 // Save this To Up
Moss-made pharmaceuticals: from bench to bedside.Over the past two decades, the moss Physcomitrella patens has been developed from scratch to a model species in basic research and in biotechnology. A fully sequenced genome, outstanding possibilities for precise genome-engineering via homologous recombination (knockout moss), a certified GMP production in moss bioreactors, successful upscaling to 500 L wave reactors, excellent homogeneity of protein glycosylation, remarkable batch-to-batch stability and a safe cryopreservation for master cell banking are some of the key features of the moss system. Several human proteins are being produced in this system as potential biopharmaceuticals. Among the products are tumour-directed monoclonal antibodies with enhanced antibody-dependent cytotoxicity (ADCC), vascular endothelial growth factor (VEGF), complement factor H (FH), keratinocyte growth factor (FGF7/KGF), epidermal growth factor (EGF), hepatocyte growth factor (HGF), asialo-erythropoietin (asialo-EPO, AEPO), alpha-galactosidase (aGal) and beta-glucocerebrosidase (GBA). Further, an Env-derived multi-epitope HIV protein as a candidate vaccine was produced, and first steps for a metabolic engineering of P. patens have been made. Some of the recombinant biopharmaceuticals from moss bioreactors are not only similar to those produced in mammalian systems such as CHO cells, but are of superior quality (biobetters). The first moss-made pharmaceutical, aGal to treat Morbus Fabry, is in clinical trials.
Toludine Blue Solution Analysis Tool for Custom TOOS (3 (N Ethyl 3 methyl Total Antioxidant Capacit Mouse Anti-Cholera Toxin 4-Amino-N-methyl-α-tolue Analysis Tool for AAH-ANG Fluorescein 5 thiosemicar EpiQuik Total Histone E Sheep Anti-C. perfringens N,N,N Trimethyl 4 (6 phen Analysis Tool for AAH-CYT
#20547143 // Save this To Up
The neuroprotective effect of erythropoietin-transduced human mesenchymal stromal cells in an animal model of ischemic stroke.Erythropoietin (EPO) exhibits diverse cellular functions, including neurotrophic, anti-oxidant, anti-apoptotic, and anti-inflammatory effects in non-hematopoietic tissues. This study evaluated whether bone marrow mesenchymal stromal cells (MSCs) transduced with the EPO gene (EPO-MSCs) promoted neural cell survival and improved neurological deficits caused by ischemic stroke. EPO-MSCs stably produced high levels of EPO (10IU/ml) without any alteration of their mesenchymal phenotype. Both EPO transduction and treatment with 10 international units (IU) of recombinant human EPO (rhEPO) provided protection from H(2)O(2)-induced oxidative injury in human bone marrow mesenchymal stromal cells and in SH-SY5Y cells. EPO-MSCs were more protected than were MSCs treated with 10IU rhEPO (10U-MSCs). We also found that the expression of the neurotrophic factors BDNF, PD-ECGF, HGF, SDF-1alpha, and TGF-1beta increased in EPO-MSCs, while only BDNF and TGF-1beta increased in 10U-MSCs. Implantation of EPO-MSCs in an animal model of ischemic stroke significantly improved neurological function and decreased infarct volumes without affecting hematocrit level. An evaluation of the brain tissue 21days after implantation showed that EPO and phosphorylated Akt (a downstream mediator of EPO) increased only in brains implanted with EPO-MSCs. Transduction of the EPO gene into MSCs induced secretion of EPO and various trophic factors that may provide excellent neuroprotective effects in both in vitro and in vivo models of ischemic stroke.
1112 related Products with: The neuroprotective effect of erythropoietin-transduced human mesenchymal stromal cells in an animal model of ischemic stroke.Proteins and Antibodies H Proteins and Antibodies H Goat Anti-Human HAX1, (in TCP-1 theta antibody Sour Mouse Anti-Human Interleu Goat Anti-Human, Mouse, R Mouse anti human Integrin Interferon-a Receptor Typ Goat Anti-Human Tryptopha Human Inflammation Array Goat Anti-Human Mammaglob Goat Anti-Human FMR1, (in
#20512979 // Save this To Up
Glycoprotein production for structure analysis with stable, glycosylation mutant CHO cell lines established by fluorescence-activated cell sorting.Stable mammalian cell lines are excellent tools for the expression of secreted and membrane glycoproteins. However, structural analysis of these molecules is generally hampered by the complexity of N-linked carbohydrate side chains. Cell lines with mutations are available that result in shorter and more homogenous carbohydrate chains. Here, we use preparative fluorescence-activated cell sorting (FACS) and site-specific gene excision to establish high-yield glycoprotein expression for structural studies with stable clones derived from the well-established Lec22.214.171.124 glycosylation mutant of the Chinese hamster ovary (CHO) cell line. We exemplify the strategy by describing novel clones expressing single-chain hepatocyte growth factor/scatter factor (HGF/SF, a secreted glycoprotein) and a domain of lysosome-associated membrane protein 3 (LAMP3d). In both cases, stable GFP-expressing cell lines were established by transfection with a genetic construct including a GFP marker and two rounds of cell sorting after 1 and 2 weeks. The GFP marker was subsequently removed by heterologous expression of Flp recombinase. Production of HGF/SF and LAMP3d was stable over several months. 1.2 mg HGF/SF and 0.9 mg LAMP3d were purified per litre of culture, respectively. Homogenous glycoprotein preparations were amenable to enzymatic deglycosylation under native conditions. Purified and deglycosylated LAMP3d protein was readily crystallized. The combination of FACS and gene excision described here constitutes a robust and fast procedure for maximizing the yield of glycoproteins for structural analysis from glycosylation mutant cell lines.
2063 related Products with: Glycoprotein production for structure analysis with stable, glycosylation mutant CHO cell lines established by fluorescence-activated cell sorting.Cell Explorer™ Fixed Ce Cell Meter™ Caspase 3 7 Cell Explorer™ Live Cel Human PAI-1 (stable mutan Cell Meter™ Annexin V B Human tumor cell array, 1 Cell Navigator™ Lysosom Cell Meter™ Fluorimetri Cell Navigator™ Mitocho Cell Meter™ Live Cell C Cell Meter™ Cell Viabil Cell Meter™ Live Cell C
#19846215 // Save this To Up
An artificial extracellular matrix created by hepatocyte growth factor fused to IgG-Fc.The design of artificial extracellular matrices (ECM) has attracted much attention in tissue engineering and regenerative medicine as well as in molecular biology research. A recombinant hepatocyte growth factor (HGF), fused to an immunoglobulin G (IgG) Fc region (abbreviated as AeHGF-Fc) was constructed and confirmed by Western blot assay. Almost similar amounts of HepG2 cells adhered to AeHGF-Fc-coated surface compared to collagen-coated one with large morphological changes. Immobilized AeHGF-Fc continuously activated Akt in HepG2 cells whereas Akt activation induced by soluble HGF rapidly decreased with time, indicating that immobilized AeHGF-Fc follows different signal transduction pathways compared to soluble HGF.
1341 related Products with: An artificial extracellular matrix created by hepatocyte growth factor fused to IgG-Fc.Hamster anti mouse Insuli Growth Factor (Human) Ant Rabbit Polyclonal Antibod Sheep Polyclonal Antibody Rat monoclonal anti mouse Human Growth Factor Array Human Angiopoietin Growth RABBIT ANTI HUMAN SDF-1 A Rat monoclonal anti mouse Human Growth Factor Array Rabbit Polyclonal Antibod Rat monoclonal anti mouse
#19818855 // Save this To Up
Overproduction of recombinant human hepatocyte growth factor in Chinese hamster ovary cells.Hepatocyte growth factor (HGF) is a potent multi-functional protein that affects morphogenesis, cell migration, organ regeneration, and tumor invasion in various tissues, and has thus been considered to have potential as a therapeutic target in various diseases. In our current study, we established Chinese hamster ovary (CHO) cells overexpressing recombinant human HGF (rhHGF) protein and in a 5 day batch culture process using a 7.5l bioreactor (5l working volume) and serum-free medium these cells could produce over 13 mg/l of rhHGF protein. The recombinant protein was then purified to homogeneity from the culture supernatant using a two-step chromatographic procedure that resulted in about a 35% recovery rate. This purified rhHGF was found to be a mixture of inactive pro-HGF and an active heterodimeric form of this protein with a higher molecular weight than its counterpart expressed from insect cells. This finding suggests that the glycosylation of rhHGF protein in CHO cells differs from that in insect cells. Inactive pro-HGF was found to rapidly convert to the active heterodimeric form of HGF in the presence of FBS (Fetal Bovine Serum), suggesting that this process would occur also when injected into human body. We further demonstrate in cell proliferation and scattering activity assays that our purified rhHGF protein preparation is functionally active with a half-maximal effective concentration of 36.3 ng/ml.
1973 related Products with: Overproduction of recombinant human hepatocyte growth factor in Chinese hamster ovary cells.Macrophage Colony Stimula Macrophage Colony Stimula Fibroblast Growth Factor Growth Differentiation Fa Goat Anti-Human Fibroblas Recombinant Human WNT Inh Recombinant Human Intrins Fibroblast Growth Factor Human Insulin-like Growth Human Insulin-like Growth Hamster anti mouse Insuli Recombinant Human Platele
#17516916 // Save this To Up
Production of plasmid DNA encoding human hepatocyte growth factor for gene therapy.pUDK-HGF, recombinant plasmid DNA encoding human HGF (hepatocyte growth factor), is a potential agent for gene therapy of ischaemic disease. Production of pUDK-HGF is essential for its clinical application. In the present paper, a large-scale manufacturing process was developed, including fermentation, cell harvest, alkaline lysis, capturing plasmid DNA with Q-Sepharose XL chromatography, size-exclusion chromatography on a Sephacryl S1000 column and refining with Source 15Q anion-exchange chromatography. The quality criteria of pUDK-HGF such as purity, concentration, homogeneity, residual RNA, chromosomal DNA, contaminated protein, endotoxin and HGF expression efficacy all were analysed and met the requirements for pharmaceutical-grade plasmid DNA.
2155 related Products with: Production of plasmid DNA encoding human hepatocyte growth factor for gene therapy.Growth Differentiation Fa Goat Anti-Human Fibroblas Epidermal Growth Factor ( Human Fibroblast Growth F Keratinocyte Growth Facto Human Endocrine Gland Vas Human, Connective Tissue Human Growth Factor Array RABBIT ANTI HUMAN SDF-1 A Human Growth and Differen Human Fibroblast Growth F Fibroblast Growth Factor
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
Schweiz Züri +41435006251
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
GENTAUR Nederland BV
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
53 Iskar Str. 1191 Kokalyane, Sofia