mouse anti rat glut4 monoclonal antibodies  (Cell Signaling Technology Inc)

Journal: PLoS ONE

Article Title: The Effect of Gonadotropin on Glucose Transport and Apoptosis in Rat Ovary

doi: 10.1371/journal.pone.0042406

Figure Lengend Snippet: Ovaries from immature rats were fixed and adjacent paraffin sections were cut. Glut1, Glut2, Glut3 and Glut4 proteins were localized with corresponding specific antibodies by ABC (avidin -biotin complex) method. Column Glut show positivities and immunoreactivities for Glut1, Glut2, Glut3 and Glut4 respectively by IHC. Note that Glut1–4 were not only detected in granulosa cells, theca cells but also in oocyte. Each independent data came form six ovaries. Magnification, 400×, Bar = 20 µm.

Article Snippet: Mouse monoclonal anti-rat Glut4 was from Cell Signaling (Cell Signaling, USA).

Techniques: Avidin-Biotin Assay

Journal: PLoS ONE

Article Title: The Effect of Gonadotropin on Glucose Transport and Apoptosis in Rat Ovary

doi: 10.1371/journal.pone.0042406

Figure Lengend Snippet: The ovaries were also collected for Glut mRNA analysis by real-time PCR and RT-PCR. The Glut mRNA abundance were normalized by 18S rRNA and β-actin. Although eCG significantly increased Glut1, Glut3 and Glut4 mRNA level, these responses were abrogated by eCG antiserum. Neither eCG alone nor the combination of eCG and eCG antiserum elicited a significant response in the Glut2 mRNA regulation. **, P<0.01.

Article Snippet: Mouse monoclonal anti-rat Glut4 was from Cell Signaling (Cell Signaling, USA).

Techniques: Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction

Journal:

Article Title: VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts

doi:

Figure Lengend Snippet: VAMP2 and VAMP3 GFP chimeras are found on intracellular GLUT4myc membrane compartments. L6-GLUT4myc myoblasts were transfected with 2 μg of V2-GFP (left) or V3-GFP (right) cDNA, and cells were fractionated to yield internal membranes plus cytosol. Intracellular GLUT4 vesicles were immunoadsorbed from the internal membrane-containing fractions with the use of monoclonal GLUT4 antibody (1F8) or nonimmune mouse IgG (NI). The resulting immune pellets (P) and supernatants (S) were separated by 12% SDS-PAGE and immunoblotted with polyclonal anti-GLUT4 (top panels) or anti-GFP (bottom panels) IgGs. Shown are results from one of four representative experiments. The open and closed arrowheads point to GLUT4 and the GFP-v-SNAREs, respectively.

Article Snippet: Monoclonal mouse anti-rat glucose transporter GLUT4 (1F8) antibody was purchased from Genzyme Diagnostics (Cambridge, MA).

Techniques: Transfection, SDS Page

Journal:

Article Title: VAMP2, but Not VAMP3/Cellubrevin, Mediates Insulin-dependent Incorporation of GLUT4 into the Plasma Membrane of L6 Myoblasts

doi:

Figure Lengend Snippet: A model of the intracellular GLUT4 compartment and insulin-stimulated GLUT4 traffic in L6 muscle cells. Under basal conditions, GLUT4 is continuously recycled to and from the plasma membrane (PM) but is largely sequestered intracellularly within the endosomal sorting system (SE) and a specialized GLUT4 vesicular (SV) pool. Other proteins, such as the transferrin receptor (TfR), recycle constitutively through the recycling endosome (RE). The mobilization of specific proteins out of both the RE and SV compartments can be modulated by insulin, possibly by differential protein sorting out of the SE. Insulin potentiates the exocytosis of GLUT4 from the SV pool by inducing the Rac-mediated formation of cortical actin mesh structures beneath the cell surface. This remodeled actin mesh recruits GLUT4-containing vesicles from the SV, allowing them to fuse with the PM. These insulin-responsive GLUT4 vesicles found in the actin mesh also comprise VAMP2, a vesicle SNARE that is essential for the incorporation of GLUT4 into the plasma membrane.

Article Snippet: Monoclonal mouse anti-rat glucose transporter GLUT4 (1F8) antibody was purchased from Genzyme Diagnostics (Cambridge, MA).

Techniques: