Search results for: Recombinant Human IGF1 long R3 Proteins
#37301443 2023/06/08 To Up
Insulin-Like Growth Factor1 Preserves Gastric Pacemaker Cells and Motor Function in Aging via ERK1/2 Activation.
Impaired gastric motor function in the elderly causes reduced food intake leading to frailty and sarcopenia. We previously found that aging-related impaired gastric compliance was mainly owing to depletion of interstitial cells of Cajal (ICC), pacemaker cells, and neuromodulator cells. These changes were associated with reduced food intake. Transformation-related protein 53-induced suppression of extracellular signal-regulated protein kinase (ERK)1/2 in ICC stem cell (ICC-SC) cell-cycle arrest is a key process for ICC depletion and gastric dysfunction during aging. Here, we investigated whether insulin-like growth factor 1 (IGF1), which can activate ERK in gastric smooth muscles and invariably is reduced with age, could mitigate ICC-SC/ICC loss and gastric dysfunction in klotho mice, a model of accelerated aging.Vy Truong Thuy Nguyen, Negar Taheri, Egan L Choi, Todd A Kellogg, David R Linden, Yujiro Hayashi
2392 related Products with: Insulin-Like Growth Factor1 Preserves Gastric Pacemaker Cells and Motor Function in Aging via ERK1/2 Activation.
20ug5 10ug100.00 ug100.00 ug250ul100.00 ug1 kit(96 Wells)2 Pieces/Box250ul10ug100.00 ugRelated Pathways
#37261455 2023/06/01 To Up
Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris.
Insulin-like growth factor-1 (IGF-1) is a pleiotropic protein hormone and has become an attractive therapeutic target because of its multiple roles in various physiological processes, including growth, development, and metabolism. However, its production is hindered by low heterogenous protein expression levels in various expression systems and hard to meet the needs of clinical and scientific research. Here, we report that human IGF-1 and its analog Long R3 IGF-1 (LR3 IGF-1) are recombinant expressed and produced in the Pichia pastoris (P. pastoris) expression system through being fused with highly expressed xylanase XynCDBFV. Furthermore, purified IGF-1 and LR3 IGF-1 display excellent bioactivity of cell proliferation compared to the standard IGF-1. Moreover, higher heterologous expression levels of the fusion proteins XynCDBFV-IGF-1 and XynCDBFV-LR3 IGF-1 are achieved by fermentation in a 15-L bioreactor, reaching up to about 0.5 g/L XynCDBFV-IGF-1 and 1 g/L XynCDBFV-TEV-LR3 IGF-1. Taken together, high recombinant expression of bioactive IGF-1 and LR3 IGF-1 is acquired with the assistance of xylanase as a fusion partner in P. pastoris, which could be used for both clinical and scientific applications. KEY POINTS: • Human IGF-1 and LR3 IGF-1 are produced in the P. pastoris expression system. • Purified IGF-1 and LR3 IGF-1 show bioactivity comparable to the standard IGF-1. • High heterologous expression of IGF-1 and LR3 IGF-1 is achieved by fermentation in a bioreactor.Zequn Lu, Ning Liu, Huoqing Huang, Yuan Wang, Tao Tu, Xing Qin, Xiaolu Wang, Jie Zhang, Xiaoyun Su, Jian Tian, Yingguo Bai, Huiying Luo, Bin Yao, Honglian Zhang
1250 related Products with: Recombinant expression of IGF-1 and LR3 IGF-1 fused with xylanase in Pichia pastoris.
10µg10010µg100ul10001010021010002x 100ug2Related Pathways
#21752560 2011/07/12 To Up
Doping control analysis of selected peptide hormones using LC-MS(/MS).
With the constantly increasing sensitivity and robustness of liquid chromatography-mass spectrometry-based instruments combined with enhanced reproducibility as well as mass accuracy and resolution, LC-MS(/MS) has become an integral part of sports drug testing programs particularly concerning the detection of peptide hormones. Although several of the relevant peptidic drugs such as insulins (Humalog LisPro, Novolog Aspart, etc.), growth hormone releasing peptides (GHRPs, e.g., GHRP-2, GHRP-6, Hexarelin, etc.), and insulin-like growth factors (e.g., IGF-1, IGF-2, long-R(3)-IGF-1) are currently analyzed using dedicated top-down analytical procedures, i.e. employing specifically tailored sample preparation procedures followed by targeted LC-MS(/MS) measurements focusing on intact analytes, first approaches towards multi-analyte methods have been established. These allow the determination of the prohibited substances in blood and urine doping control specimens following therapeutic applications. In addition, the use of new complementary devices such as ion mobility analyzers, e.g., in hybrid mass spectrometers yielded promising data for the differentiation of isobaric insulins, which outlines the potential to further accelerate and multiplex doping control analytical assays to meet the continuously increasing demands of rapid and unambiguous test methods. Moreover, the potential of LC-MS/MS to target recombinant peptide hormones such as human growth hormone using bottom-up approaches has been demonstrated by targeting proteotypic peptides that unambiguously differentiate the recombinant molecule from the naturally occurring and endogenously produced analog.Mario Thevis, Andreas Thomas, Wilhelm Schänzer
1092 related Products with: Doping control analysis of selected peptide hormones using LC-MS(/MS).
0.1 mg 100 ug50 µl 0.1 mg 100 μg 0.1 mg 0.1 mg 50 ug50 ug50 ug50 ug50Related Pathways
#9867252 // To Up
Involvement of insulin-like growth factor-1 and its binding proteins in proliferation and differentiation of murine bone marrow-derived macrophage precursors.
Insulin-like growth factor 1 (IGF-1) and its binding proteins (IGFBPs) are involved in proliferation and differentiation of many cell types. In the present study, the involvement of IGF-1 and IGFBPs in proliferation and differentiation of murine bone marrow-derived macrophages (BMDM) was investigated. L929-conditioned media (LCM) containing abundant macrophage colony-stimulating factor CSF-1 were used to stimulate BMDM development from their bone marrow precursors. The alteration of IGF-1 and IGFBPs during LCM-induced BMDM proliferation and differentiation was first studied. The cells were cultured in RPMI complete media containing 20% LCM for different time periods and then incubated in serum-free media for 24 h. The supernatants were collected for Western ligand blotting and immunoblotting analyses, and the cell pellets for Northern blotting analyses. The mRNA level of IGF-1 increased in a time-dependent manner. An increase of IGFBP-4 accumulation in the conditioned media was also observed during this process. However the mRNA expression of IGFBP-4 remained constant, indicating a posttranscriptional regulation of IGFBP-4 secretion and/or stability. The effects of exogenous recombinant human IGF-1 (rhIGF-1) on BMDM proliferation and differentiation were further studied. Two IGF-1 analogs (long R3 IGF-1 and des [1-3] IGF-1) were also used in parallel with regular IGF-1 to indicate the involvement of IGFBPs in BMDM development. Cells were cultured in complete media containing 20% LCM for different time periods, and then incubated in serum-free media in the presence of rhIGF-1 or its analogs for 24 h. These three forms of IGF-1 all potentiated the proliferation of freshly isolated BMDM precursors (d 0). rhIGF-1 and long R3 IGF-1, but not des (1-3) IGF-1, continued to stimulate the cell proliferation on d 1. The effects of these three forms of IGF-1 on BMDM differentiation were investigated using mannose receptor expression as a marker. Long R3 IGF-1 and des (1-3) IGF-1, but not rhIGF-1, enhanced BMDM differentiation on d 4. The different effects of rhIGF-1 and its analogs on BMDM differentiation suggest that the accumulation of IGFBP-4 in BMDM development might have an inhibitory effect on IGF-1 actions by sequestering free IGF-1.E Long, H T Huynh, X Zhao
1399 related Products with: Involvement of insulin-like growth factor-1 and its binding proteins in proliferation and differentiation of murine bone marrow-derived macrophage precursors.
100.00 ug100.00 ug10ug100.00 ug10ug10ug100.00 ug100.00 ug2 Pieces/Box1 kit(96 Wells)100.00 ugProteinRelated Pathways
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