Only in Titles

           Search results for: Recombinant Human BMF Proteins    

paperclip

#27130558   2016/04/30 Save this To Up

Persistent bone marrow depression following short-term treatment with temozolomide.

Temozolomide (TMZ) is, in combination with radiotherapy (RT), the treatment of choice for glioblastoma multiforme. Although generally well tolerated, haematological side effects are observed in approximately 1-10% of patients receiving TMZ. We report a case of a patient who developed severe bone marrow failure (BMF) after only 3 weeks of concomitant TMZ. The BMF was grave with no signs of improvement for 12 months, resulting in more than 100 transfusions of blood cells.

1045 related Products with: Persistent bone marrow depression following short-term treatment with temozolomide.

Bone marrow tissue array, Normal bone marrow tissue Bone marrow tumor and adj Normal bone marrow tissue Multiple myeloma test tis Bone marrow tumor and nor Anti-Bone Morphogenetic P Anti Bone Morphogenetic P Anti-Bone Morphogenetic P Anti Bone Morphogenetic P Interleukin-34 IL34 (N-t HMGB1 (N-term) antibody

Related Pathways

paperclip

#25906158   2015/04/24 Save this To Up

Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.

The mitochondrial pathway of apoptosis is initiated by Bcl-2 homology region 3 (BH3)-only members of the Bcl-2 protein family. On upregulation or activation, certain BH3-only proteins can directly bind and activate Bak and Bax to induce conformation change, oligomerization and pore formation in mitochondria. BH3-only proteins, with the exception of Bid, are intrinsically disordered and therefore, functional studies often utilize peptides based on just their BH3 domains. However, these reagents do not possess the hydrophobic membrane targeting domains found on the native BH3-only molecule. To generate each BH3-only protein as a recombinant protein that could efficiently target mitochondria, we developed recombinant Bid chimeras in which the BH3 domain was replaced with that of other BH3-only proteins (Bim, Puma, Noxa, Bad, Bmf, Bik and Hrk). The chimeras were stable following purification, and each immunoprecipitated with full-length Bcl-xL according to the specificity reported for the related BH3 peptide. When tested for activation of Bak and Bax in mitochondrial permeabilization assays, Bid chimeras were ~1000-fold more effective than the related BH3 peptides. BH3 sequences from Bid and Bim were the strongest activators, followed by Puma, Hrk, Bmf and Bik, while Bad and Noxa were not activators. Notably, chimeras and peptides showed no apparent preference for activating Bak or Bax. In addition, within the BH3 domain, the h0 position recently found to be important for Bax activation, was important also for Bak activation. Together, our data with full-length proteins indicate that most BH3-only proteins can directly activate both Bak and Bax.

2778 related Products with: Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax.

Recombinant Mouse BAX Pro Recombinant Mouse BAX Pro Recombinant Mouse BAX Pro Recombinant Mouse BAX Pro CAR,Car,Constitutive andr Recombinant Human Androge Androgen Receptor (Phosph Androgen Receptor (Phosph Rabbit Anti-Human Androge Rabbit Anti-Human Androge Androgen Receptor (Ab 650 Recombinant Human Bcl-2 -

Related Pathways

paperclip

#23076521   2012/11/02 Save this To Up

Problems encountered in bicistronic IRES-GFP expression vectors employed in functional analyses of GC-induced genes.

Our laboratory has developed a series of Gateway(®) compatible lentiviral expression systems for constitutive and conditional gene knock-down and over-expression. For tetracycline-regulated transgenic expression, we constructed a lentiviral "DEST" plasmid (pHR-TetCMV-Dest-IRES-GFP5) containing a tetracycline-responsive minimal CMV promoter, followed by an attP site-flanked DEST cassette (for efficient cloning of cDNAs by "Gateway(®)" recombination cloning) and green fluorescent protein (GFP) driven by an internal ribosomal entry site (IRES).This lentiviral bicistronic plasmid allows immediate FACS identification and characterization of successfully transfected cell lines. Although this system worked well with several cDNAs, we experienced serious problems with SLA, Bam and BMF. Particularly, we cloned the cDNA for human SLA (Src-like adapter), a candidate gene in GC-induced apoptosis, into this plasmid. The resulting construct (pHR-TetCMV-SLA-IRES-GFP5) was transfected into HEK 293-T packaging cells to produce viral particles for transduction of CEM-C7H2-2C8 cells. Although the construct produced many green fluorescent colonies at the HEK 293-T and the CEM-C7H2-2C8 level, we could not detect any SLA protein with α-SLA antibody from corresponding cell lysates. In contrast, the antibody readily detected SLA in whole cell lysate of HEK 293-T cells transfected with a GST-flagged SLA construct lacking IRES-GFP. To directly address the potential role of the IRES-GFP sequence, we cloned the SLA coding region into pHR-TetCMV-Dest, a vector that differs from pHR-TetCMV-Dest-IRES-GFP5 just by the absence of the IRES-GFP cassette. The resulting pHR-TetCMV-SLA construct was used for transfection of HEK 293-T cells. Corresponding lysates were assayed with α-SLA antibody and found positive. These data, in concert with previous findings, suggest that the IRES-GFP cassette may interfere with translation of certain smaller size cDNAs (like SLA) or generate fusion proteins and entail defective virus production in an unpredictable manner.

1123 related Products with: Problems encountered in bicistronic IRES-GFP expression vectors employed in functional analyses of GC-induced genes.

Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon Anti AGO2 Human, Monoclon Anti AGO2 Mouse, Monoclon DNA (cytosine 5) methyltr Human Epstein-Barr Virus Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Jurkat Cell Extract (Indu Mouse Epstein-Barr Virus TGF beta induced factor 2

Related Pathways

paperclip

#21311795   2011/03/15 Save this To Up

Fluorescent labeling of membrane proteins on the surface of living cells by a self-catalytic glutathione S-transferase omega 1 tag.

Imaging a specific protein of interest in live cell has versatile applications in biological research. Recently, diverse chemical tags have been developed to overcome the limits of autofluorescence protein (FP) tags. However, current chemical methods still need to be progressed to compete with FPs in the scope of specificity and convenience in staining procedure. We report a novel protein tagging method that provides a convenient and specific fluorescent labeling of membrane proteins. Ω tag is developed by employing a mammalian enzyme glutathione sulfur-transferase omega 1 (GSTO1) and its partner dye, 5-bromomethyl fluorescein (BMF). Ω-tagged membrane proteins were labeled by BMF efficiently for live cell imaging and in-gel analysis. Endocytosis of epidermal growth factor receptor (EGFR) was successfully visualized by using this Ω tagging system. Ω tag will provide a convenient tool for the physiological study of membrane proteins in live cells.

2803 related Products with: Fluorescent labeling of membrane proteins on the surface of living cells by a self-catalytic glutathione S-transferase omega 1 tag.

5 (2 Aminoethylamino) 1 n 1,1'-Dioctadecyl-3,3,3',3 glutathione S-transferase Recombinant HBsAg adr [fr Recombinant HBsAg adr [fr Recombinant Canine ApoJ C Recombinant Canine ApoJ C Recombinant Human RAGE AG Recombinant Human RAGE AG glutathione transferase a Atto 550 Protein Labeling Atto 655 Protein Labeling

Related Pathways

paperclip

#20945437   2011/02/22 Save this To Up

The transforming growth factor-beta (TGF-β) mediates acquisition of a mesenchymal stem cell-like phenotype in human liver cells.

Transforming growth factor-beta (TGF-β) mediates several and sometime opposite effects in epithelial cells, inducing growth inhibition, and apoptosis but also promoting an epithelial to mesenchymal transition (EMT) process, which enhances cell migration and invasion. TGF-β plays relevant roles in different liver pathologies; however, very few is known about its specific signaling and cellular effects in human primary hepatocytes. Here we show that TGF-β inhibits proliferation and induces pro-apoptotic genes (such as BMF or BIM) in primary cultures of human fetal hepatocytes (HFH), but also up-regulates anti-apoptotic genes, such as BCL-XL and XIAP. Inhibition of the epidermal growth factor receptor (EGFR), using gefitinib, abrogates the increase in the expression of the anti-apoptotic genes and significantly enhances cell death. Simultaneously, TGF-β is able to induce an EMT process in HFH, coincident with Snail up-regulation and a decrease in E-cadherin levels, cells showing mesenchymal proteins and reorganization of the actin cytoskeleton in stress fibers. Interestingly, these cells show loss of expression of specific hepatic genes and increased expression of stem cell markers. Chronic treatment with TGF-β allows selection of a population of mesenchymal cells with a de-differentiated phenotype, reminiscent of progenitor-like cells. Process is reversible and the mesenchymal stem-like cells re-differentiate to hepatocytes under controlled experimental conditions. In summary, we show for the first time that human hepatocytes may respond to TGF-β inducing different signals, some of them might contribute to tumor suppression (growth inhibition and apoptosis), but others should mediate liver tumor progression and invasion (EMT and acquisition of a stem-like phenotype).

1468 related Products with: The transforming growth factor-beta (TGF-β) mediates acquisition of a mesenchymal stem cell-like phenotype in human liver cells.

Human Transforming Growth Human Transforming Growth TGF beta induced factor 2 Epidermal Growth Factor ( Epidermal Growth Factor ( Macrophage Colony Stimula Macrophage Colony Stimula RABBIT ANTI HUMAN SDF-1 A Growth Factor (Human) Ant Goat Anti-Human Fibroblas Epidermal Growth Factor ( Epidermal Growth Factor (

Related Pathways

paperclip

#18462686   2008/05/08 Save this To Up

Structural plasticity underpins promiscuous binding of the prosurvival protein A1.

Apoptotic pathways are regulated by protein-protein interactions. Interaction of the BH3 domains of proapoptotic Bcl-2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner, others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study, crystal structures of complexes between the prosurvival protein A1 and the BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such as an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis. Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity. This study, in combination with published data, suggests that interactions between conserved residues demarcate optimal binding.

2397 related Products with: Structural plasticity underpins promiscuous binding of the prosurvival protein A1.

S100 alpha - Rabbit polyc Acyl CoA binding Protein E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran E. coli SSB (Single Stran Taq SSB (Single Stranded Taq SSB (Single Stranded Mouse Anti-Human Retinol Human S100 Calcium Bindin ribosome binding protein ribosome binding protein

Related Pathways

paperclip

#16645638   2006/12/14 Save this To Up

Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets.

All BH3-only proteins, key initiators of programmed cell death, interact tightly with multiple binding partners and have sequences of low complexity, properties that are the hallmark of intrinsically unstructured proteins (IUPs). We show, using spectroscopic methods, that the BH3-only proteins Bim, Bad and Bmf are unstructured in the absence of binding partners. Detailed sequence analyses are consistent with this observation and suggest that most BH3-only proteins are unstructured. When Bim binds and inactivates prosurvival proteins, most residues remain disordered, only the BH3 element becomes structured, and the short alpha-helical molecular recognition element can be considered to behave as a 'bead on a string'. Coupled folding and binding is typical of many IUPs that have important signaling roles, such as BH3-only proteins, as the inherent structural plasticity favors interaction with multiple targets. This understanding offers promise for the development of BH3 mimetics, as multiple modes of binding are tolerated.

1497 related Products with: Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets.

Recombinant Human IFN-alp Recombinant Human IFN-alp Carboxyfluorescein diacet Acyl CoA binding Protein Actin binding EGFP Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi Clostridum difficile toxi

Related Pathways

  •  
  • No related Items
paperclip

#15598951   2004/12/15 Save this To Up

Low-dose interleukin-11 in patients with bone marrow failure: update of the M. D. Anderson Cancer Center experience.

Recombinant interleukin (IL)-11 is a thrombopoietic growth factor. The purpose of this study was to assess the toxicity, safety and efficacy of low-dose recombinant IL-11 in patients with bone marrow failure (BMF).

2090 related Products with: Low-dose interleukin-11 in patients with bone marrow failure: update of the M. D. Anderson Cancer Center experience.

Human Interleukin-11 IL-1 Mouse Interleukin-11 IL-1 Recombinant Human Interle Recombinant Human Interle Recombinant Mouse Interle Recombinant Mouse Interle Breast cancer tissue arra Breast cancer (IDC) tissu Breast cancer and adjacen Bone marrow tumor and adj Rat monoclonal anti mouse Bone and cartilage cancer

Related Pathways

paperclip

#14561217   2004/01/23 Save this To Up

Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.

The dynein and myosin V motor complexes are multi-protein structures that function to transport molecules and organelles within the cell. DLC (dynein light-chain) proteins, found as components of both dynein and myosin V motor complexes, connect the complexes to their cargoes. One of the roles of these motor complexes is to selectively sequester the pro-apoptotic 'BH3-only' (Bcl-2 homology 3-only) proteins, Bim (Bcl-2-interacting mediator of cell death) and Bmf (Bcl-2-modifying factor), and so regulate their cell death-inducing function. In vivo DLC2 is found exclusively as a component of the myosin V motor complex and Bmf binds DLC2 selectively. On the other hand, Bim interacts with DLC1 (LC8), an integral component of the dynein motor complex. The two DLCs share 93% sequence identity yet show unambiguous in vivo specificity for their respective BH3-only ligands. To investigate this specificity the three-dimensional solution structure of DLC2 was elucidated using NMR spectroscopy. In vitro structural and mutagenesis studies show that Bmf and Bim have identical binding characteristics to recombinant DLC2 or DLC1. Thus the selectivity shown by Bmf and Bim for binding DLC1 or DLC2, respectively, does not reside in their DLC-binding domains. Remarkably, mutational analysis of DLC1 and DLC2 indicates that a single surface residue (residue 41) determines the specific localization of DLCs with their respective motor complexes. These results suggest a molecular mechanism for the specific compartmentalization of DLCs and their pro-apoptotic cargoes and implicate other protein(s) in defining the specificity between the cargoes and the DLC proteins.

1929 related Products with: Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands.

17β-Acetoxy-2α-bromo-5 5α-N-Acetyl-2'H-androst- 5α-N-Acetyl-2'H-androst- 3-O-Acetyl 5,14-Androstad 3-O-Acetyl-17-O-tert-buty Androsta-1,4,6-triene-3,1 (3β)-Androsta-5,16-diene Androst-4-ene-3,6,17-trio (5α)-Androstane-3,11,17- 19 Hydroxy 4 androstene 3 Epiandrosterone (3 beta H Rabbit Anti-Human Androge

Related Pathways

  •  
  • No related Items