Search results for: Recombinant Bovine Placental Lactogen
#27743526 // Save this To Up
Activities for leptin in bovine trophoblast cells.Leptin is involved in various reproductive processes in humans and rodents, including placental development and function. The specific ways that leptin influences placental development and function in cattle are poorly understood. This work was completed to explore how leptin regulates hormone, cytokine and metalloprotease transcript abundance, and cell proliferation in cultured bovine trophoblast cells. In the first set of studies, cells were cultured in the presence of graded recombinant bovine leptin concentrations (0, 10, 50, 250 ng/mL) for 6 or 24 h. Transcript profiles were examined from extracted RNA. Leptin supplementation did not affect abundance of the maternal recognition of pregnancy factor, interferon-tau (IFNT), but leptin increased (P < 0.05) abundance of chorionic somatomammotropin hormone 2 (CSH2; ie, placental lactogen) at both 6 and 24 h at each concentration tested. At 24 h, the greatest CSH2 abundance (P < 0.05) was detected in cells supplemented with 50 ng/mL leptin. Transcript abundance of the remodeling factor, metalloprotease 2 (MMP2), was greater (P < 0.05) in leptin-treated cells at 24 h but not at 6 h. The 24 h MMP2 response was greatest (P < 0.05) at 250 ng/mL. Transcript abundance for MMP9 was not altered by leptin treatment. In a separate set of studies, cell proliferation assays were completed. Leptin supplementation did not affect bovine trophoblast cell line proliferation at any dose tested. In conclusion, leptin supplementation did not affect bovine trophoblast cell proliferation or IFNT expression, but leptin increases CSH2 and MMP2 transcript abundance. Both of these factors are involved with peri-implantation and postimplantation placental development and function, and this implicates leptin as a potential mediator of early placental development and function in cattle.
Leptin ELISA Kit, Rat Lep MOUSE ANTI BOVINE ROTAVIR anti HSV (II) gB IgG1 (mo anti HCMV IE pp65 IgG1 (m anti HCMV gB IgG1 (monocl Macrophage Colony Stimula Macrophage Colony Stimula Insulin from Bovine Pancr Recombinant Bovine Leptin Recombinant Bovine Leptin Recombinant Bovine Leptin GLP 1 ELISA Kit, Rat Gluc
#24112823 // Save this To Up
The isolation and characterization of a telomerase immortalized goat trophoblast cell line.Trophoblast cells play vital roles in the processes of embryonic implantation and placentation. Many toxicological compounds can induce the malfunction of trophoblast cells, resulting in implantation failure or early embryonic loss. The finite lifespan of primary trophoblast cells limits investigation of the long-term effects of some toxicological compounds on trophoblast cells in vitro. In this study, primary goat trophoblast cells were purified by density gradient centrifugation and specific immuno-affinity purification. Then, the purified cells were immortalized through transfection of a plasmid containing the human telomerase reverse transcriptase (hTERT) gene. hTERT-transfected goat trophoblast cells (hTERT-GTCs) could steadily express hTERT gene and exhibit higher telomerase activity, and persistently proliferate without any signs of senescence up to 50 passages. The immortalized goat trophoblast cells still possessed the basic and key properties of normal primary goat trophoblast cells to express the specific intracellular marker cytokeratin 7 (CK-7) and secrete chorionic gonadotrophin β-subunit (CG-β) and placental lactogen (PL). Further studies showed that the immortalized goat trophoblast cells expressed vimentin and non-classical MHC class I antigen and exhibited invasive phenotype, suggesting that the immortalized goat trophoblasts resembled human extravillous trophoblasts. In addition, this cell line did not show neoplastic transformation either in vivo or in vitro. We concluded the immortalized goat trophoblast cells by hTERT transfection retained the basic and key characteristics of primary trophoblast cells and may provide a useful model to study the effects of some toxicological compounds on trophoblast cells.
1189 related Products with: The isolation and characterization of a telomerase immortalized goat trophoblast cell line.anti SLAM anti CDw150 IgG anti CD37 IgG2b (monoclon AP-1 Reporter – HEK293 Nrf antioxidant pathway A Goat Anti-Human Androgen Goat Anti-Human Synaptogy Goat Anti- T-cell differe Apoptotic Cell Isolation Rabbit Anti-SF9 Insect Ce Rabbit Anti-Insect Cell L Tissue array of ovarian g EXOC7 antibody Host Goat
#21862694 // Save this To Up
Bone morphogenetic protein 4 accelerates the establishment of bovine trophoblastic cell lines.Trophoblastic cells play a crucial role in implantation and placentogenesis. A large proportion of the failures of conception in cows occur in the peri-implantation period, which are known as early embryo losses. In exploring this critical phenomenon, trophoblastic cell lines can provide substantial information. Unfortunately, there are few cell lines for this purpose in cattle because of the difficulty of raising successive cell stock in the long term. In this study, 12 new cell lines were established using bone morphogenetic protein 4 (BMP4). BMP4 stimulated embryonic cells to enter the trophoblastic cell lineage but there were no significant differences between intact and BMP4-treated groups. Only one out of 49 embryos developed trophoblastic cells in the intact group. Finally, 12 cell lines were maintained for around 30 passages, and they retained trophoblastic characteristics and expressed bovine trophoblastic genes: placental lactogen, interferon-τ, pregnancy-associated glycoprotein 1, and prolactin-related protein 1. Although the gene expression patterns were different among cell lines and depended on the cells, there was no significant relationship between the expression intensities of genes and the treatment dose of BMP4. All of them expressed bovine POU domain class 5 transcription factor 1 and caudal-type homeobox 2. The expression of these genes was confirmed by quantitative RT-PCR and immunohistochemical detection. These results suggest that BMP4 is involved in the raising of trophoblast cell lines from early embryonic cells and the newly developed cell lines can provide different types of bovine trophoblastic cells with different cell lineages. This may constitute a significant new tool for the examination of trophoblastic differentiation.
1506 related Products with: Bone morphogenetic protein 4 accelerates the establishment of bovine trophoblastic cell lines.Anti C Reactive Protein A Bone Morphogenetic Protei Bone Morphogenetic Protei Bone Morphogenetic Protei Bone Morphogenetic Protei Bone Morphogenetic Protei Bone Morphogenetic Protei Human Bone Morphogenetic Polyclonal Antibody Bone Rabbit Anti-Cell death in Rabbit Anti-P2RX4 ATP gat Rabbit Anti-P2RX4 ATP gat
#18677398 // Save this To Up
Native and recombinant bovine placental lactogens.The bovine placenta produces a wide variety of proteins that are structurally and functionally similar to the pituitary proteins from the GH/PRL gene family. Bovine placental lactogen (bPL) is a 200-amino acid long glycoprotein hormone that exhibits both lactogenic and somatogenic properties. The apparent molecular masses of purified native (n) bPL molecules (31-33 kDa) exceed 23 041 Da, which is the theoretical molecular mass of the protein core. At least six isoelectric variants (pI: 4.85-6.3) of bPL were described in cotyledonary extracts and three different bPL isoforms (pI: 4.85-5.25) were found in fetal sera. The bPL molecules that are detected in higher concentrations in peripheral circulation exhibit a more acidic pI than those present in placental homogenates. This may reflect an important glycosylation process occurring just prior to the bPL secretion. The bPL mRNA is transcribed in trophectoderm binucleate cells starting from Day 30 of pregnancy until the end of gestation. In mothers, bPL is involved in the regulation of ovarian function, mammogenesis, lactogenesis, and pregnancy stage-dependent adaptation of nutrient supplies to the fetus. Due to the higher fetal, compared to maternal concentrations of circulating hormone, it has been suggested that bPL primarily targets fetal tissues.
Recombinant Bovine Placen Recombinant Bovine Placen Recombinant Bovine Placen Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Native Bovine Apo Transfe Native Bovine Apo Transfe Native Bovine Apo Transfe Native Bovine Aprotinin Native Bovine Aprotinin Native Bovine Aprotinin
#18252946 // Save this To Up
Bovine prolactin-related protein-I is anchored to the extracellular matrix through interactions with type IV collagen.The bovine placenta produces an array of proteins structurally similar to pituitary prolactin (PRL). At least ten genes of the bovine placental PRL family, including bovine placental lactogen (bPL) and ten bovine PRL-related protein-I to -X (bPRP-I to -X), encode hormones/cytokines predicted to be involved in the establishment and maintenance of pregnancy. Targets and biological roles for most members of the bovine PRL family have yet to be specified. This study focused on three members of bovine PRL family, bPL, bPRP-I, and bPRP-VI. An alkaline phosphatase (AP) tagging strategy was used to monitor interactions of the ligands with their targets. AP-bPRP-I and AP-bPRP-VI specifically bound to tissue sections of the bovine placentome. AP-bPRP-I and AP-bPRP-VI binding within the placentome mimicked the distribution of the extracellular matrix (ECM). Consequently, AP fusion protein binding to individual ECM components (heparin, laminin, fibronectin, type I collagen, and type IV collagen) was evaluated. AP-bPRP-I specifically bound to type IV collagen, but not to the other ECM components. AP-bPRP-VI exhibited weak interactions with ECM components, while AP-bPL and AP did not show significant binding to any of the ECM components. Binding of AP-bPRP-I to type IV collagen was concentration-dependent, influenced by salt concentrations, and specific to the N-terminal cross-linking domain (7S) of type IV collagen but not its triple-helical domain. The interaction of bPRP-I with type IV collagen suggests that bPRP-I accumulates in the ECM where it likely acts on cells traversing the bovine placentome.
1766 related Products with: Bovine prolactin-related protein-I is anchored to the extracellular matrix through interactions with type IV collagen.NC1 fragment of bovine GB NATIVE HUMAN PROLACTIN, P Human dopachrome tautomer Bovine prolactin-induced Bovine Collagen Type IV P Rabbit Anti-Bovine Collag NATIVE HUMAN PROLACTIN, P MOUSE ANTI BOVINE ROTAVIR ELMGBI Mouse IgG anti bov Mouse anti-bovine type I Mouse anti-bovine type I ELRGBI Rat IgG anti bovin
#17961217 // Save this To Up
Expression and characterization of novel ovine orthologs of bovine placental prolactin-related proteins.The prolactin-related proteins (PRPs) are non-classical placental-specific members of the prolactin/growth hormone family. Among ruminants, they are expressed in the cotyledonary villi of cattle and goat. We investigated placental PRP in sheep in order to gain a comprehensive understanding of the function and evolution of these molecules. We also examined the sequence properties, expression and lactogenic activation of the cloned genes.
2692 related Products with: Expression and characterization of novel ovine orthologs of bovine placental prolactin-related proteins.Endorphin, Beta (Bovine, Lipotropin (61 64) Beta ( Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Recombinant Bovine Aproti Recombinant Bovine Aproti Recombinant Bovine Aproti Native Bovine BSA Protein Native Bovine BSA Protein Native Bovine BSA Protein Recombinant Bovine BTC Pr
#17897591 // Save this To Up
Radioimmunoassay of bovine placental lactogen using recombinant and native preparations: determination of fetal concentrations across gestation.Concentrations of bovine placental lactogen (bPL) were determined in fetal plasma samples by twelve double-antibody competitive radioimmunoassay systems (RIA I-XII) based on either recombinant bPL (non-glycosylated) or native bPL (glycosylated). Both preparations were used as standard and tracer, and for primary antisera production. The minimum detection limit measured by these RIA varied from 0.02 to 0.6 ng bPL mL(-1). The coefficients of correlation of different bPL RIA systems were up to 90% (P < 0.0001) when each RIA was tested against the average values of all twelve RIA systems. All developed RIA were used to investigate the incidence of different bPL isoforms in bovine fetal serum samples (n = 71). Fetal concentrations ranged from 11.8 to 35.7 ng mL(-1) at the third month and from 1.1 to 13.5 ng mL(-1) at the ninth month of gestation. They tended to decrease with advancing gestation. In general, those RIA systems that used recombinant bPL as the standard measured higher values than those using the native bPL preparation. These differences decreased toward the end of gestation (P < 0.05), suggesting a lower rate of glycosylation. Our results provide evidence of different glycosylated isoforms of bPL in fetal serum at different gestation periods.
2406 related Products with: Radioimmunoassay of bovine placental lactogen using recombinant and native preparations: determination of fetal concentrations across gestation.Recombinant Bovine Placen Recombinant Bovine Placen Recombinant Bovine Placen Recombinant Rabbit Placen Recombinant Rabbit Placen Recombinant Rabbit Placen Recombinant Sheep Placent Recombinant Sheep Placent Recombinant Sheep Placent Recombinant Human Placent Recombinant Human Placent Recombinant Human Placent
#16221993 // Save this To Up
Cloning of the bovine antiapoptotic regulator, BCL2-related protein A1, and its expression in trophoblastic binucleate cells of bovine placenta.This report studied the identification and sequence of a full-length cDNA for the bovine BCL2 antiapoptotic family member, BCL2-related protein A1 (BCL2A1), and its localized and quantitative expression in the placenta to clarify the regulatory mechanism of trophoblast cell proliferation and differentiation during implantation and placental development. We cloned a full-length bovine BCL2A1 cDNA with 725 nucleotides and an open-reading frame corresponding to a protein of 175 amino acids. The predicted amino acid sequence shared 78% homology with human BCL2A1. All BCL2 homology domains (BH1, BH2, BH3, and BH4) in bovine BCL2A1 were conserved as well as in other mammalian BCL2A1. In the placentomes, in situ hybridization demonstrated that the BCL2A1 was limited in binucleate cells expressing various pregnancy-specific molecules like placental lactogen. BCL2-associated X protein (BAX) was also expressed in binucleate cells. Quantitative real-time RT-PCR detection exhibited a high-level expression of BCL2A1 in the conceptus at Day 21 of gestation, and it was expressed and increased in the extraembryonic membrane, cotyledon, and intercotyledon from implantation to term. BAX expression intensity increased with progression of gestation and remained elevated in postpartum. Caspase-3 protein (CASP3) and mRNA (CASP3) were detected from late gestation to postpartum in placenta as well as in the results of TUNEL detection. We believe that the apoptosis of binucleate cells may be regulated by the balance of the BCL2A1 and BAX. BCL2A1 genes produced a BCL2A1 protein in the mammalian cell-expression system. This molecule is a new candidate for antiapoptotic maintenance of the binucleate cells that support placental functions throughout gestation in bovine.
2933 related Products with: Cloning of the bovine antiapoptotic regulator, BCL2-related protein A1, and its expression in trophoblastic binucleate cells of bovine placenta.Bovine prolactin-induced Insulin from Bovine Pancr Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Native Bovine ALPI CIAP P Recombinant Bovine Aproti Recombinant Bovine Aproti Recombinant Bovine Aproti Native Bovine BSA Protein Native Bovine BSA Protein Native Bovine BSA Protein Recombinant Bovine BTC Pr
#11504534 // Save this To Up
Isolation and characterization of a bovine blastocyst-derived trophoblastic cell line, BT-1: development of a culture system in the absence of feeder cell.We established a trophoblastic cell line, bovine trophoblast-1 (BT-1), derived from in vitro matured and fertilized blastocyst. While several trophoblastic cell lines have been previously reported using feeder cell, BT-1 could be cultured in the absence of feeder cell. BT-1 was cultured for more than 18 months (over 75 passage) in the absence of feeder cells, using bovine endometrial fibroblast-conditioned medium (fibroblast-conditioned medium). We found that the cell growth was accelerated in fibroblast-conditioned medium. In bromodeoxyuridine incorporation analysis, BT-1 cells growth rate in fibroblast-conditioned medium was about two-fold higher than that in conventional medium. Furthermore, fibroblast-conditioned medium accelerated attachment of BT-1 cells to culture dishes following plating. BT-1 showed epithelial morphology and expressed cytokeratin. During continuous culture, cells accumulated fluid under the cell sheet and form dome-like structure that eventually transformed into free floating vesicles. Reverse transcription polymerase chain reaction analysis and immunoblot analysis demonstrated that BT-1 cells expressed interferon-tau as well as placental lactogen (PL). Immunofluorescence analysis demonstrated that a small number of cells were PL-positive, and these cells were binucleate. The BT-1 trophoblastic cell line could serve as a powerful model system for the study of trophoblast cell lineage and proliferation.
2304 related Products with: Isolation and characterization of a bovine blastocyst-derived trophoblastic cell line, BT-1: development of a culture system in the absence of feeder cell.Rabbit Anti-SF9 Insect Ce Rabbit Anti-Insect Cell L Biocidal ZF, spray disinf Biocidal ZF, spray disinf Biocidal ZF, spray disinf anti SLAM anti CDw150 IgG anti CD37 IgG2b (monoclon Human Stromal Cell-Derive Mouse Stromal Cell-Derive Cell Meter™ Intracellul Cell Meter™ Fluorimetri Cell Meter™ Fluorimetri
#11483014 // Save this To Up
Large-scale preparation of recombinant ovine prolactin and determination of its in vitro and in vivo activity.Recombinant bovine Ala-prolactin (PRL) (GenBank Accession No. V00112) in prokaryotic expression plasmid pMON3401 was mutated using a mutagenesis kit, to prepare plasmid encoding ovine PRL (oPRL) (GenBank Accession No. M27057) Escherichia coli cells transformed with this latter plasmid overexpressed large amounts of oPRL upon induction with nalidixic acid. The expressed protein, found in inclusion bodies, was refolded and purified to homogeneity on a Q-Sepharose column, yielding an electrophoretically pure fraction composed of over 98% monomeric protein of the expected molecular mass of approximately 23 kDa. The biological activity of the recombinant oPRL after proper renaturation was evidenced in vitro by its ability to stimulate proliferation of rat lymphoma Nb(2) cells possessing PRL receptors, to stimulate luciferase activity in HEK 293 cells transiently transfected with oPRL receptors, and to induce progesterone secretion in primary cultures of luteal cells obtained from midpregnant ewes. In contrast to ovine growth hormone or ovine placental lactogen, recombinant oPRL had no galactopoietic effect in lactating ewes.
3000 related Products with: Large-scale preparation of recombinant ovine prolactin and determination of its in vitro and in vivo activity.Recombinant Ovine Interfe Recombinant Ovine Interfe EnzyChrom™ Kinase Assay MarkerGeneTM in vivo lacZ MarkerGeneTM Fluorescent Resorufin Oleate, Fluorog MarkerGeneTM Long Wavelen MarkerGeneTMFluorescent A Macrophage Colony Stimula Macrophage Colony Stimula Recombinant Influenza HA Recombinant Influenza HA
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