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myelin associated glycoprotein  (Bioss)


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    Structured Review

    Bioss myelin associated glycoprotein
    Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated <t>glycoprotein;</t> MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.
    Myelin Associated Glycoprotein, supplied by Bioss, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/myelin associated glycoprotein/product/Bioss
    Average 90 stars, based on 3 article reviews
    myelin associated glycoprotein - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "MicroRNA-210 contributes to peripheral nerve regeneration through promoting the proliferation and migration of Schwann cells."

    Article Title: MicroRNA-210 contributes to peripheral nerve regeneration through promoting the proliferation and migration of Schwann cells.

    Journal: Experimental and therapeutic medicine

    doi: 10.3892/etm.2017.4869

    Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated glycoprotein; MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.
    Figure Legend Snippet: Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated glycoprotein; MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.

    Techniques Used: Transfection, Western Blot, Standard Deviation, Negative Control



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    Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated <t>glycoprotein;</t> MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.
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    Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated <t>glycoprotein;</t> MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.
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    Image Search Results


    Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated glycoprotein; MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.

    Journal: Experimental and therapeutic medicine

    Article Title: MicroRNA-210 contributes to peripheral nerve regeneration through promoting the proliferation and migration of Schwann cells.

    doi: 10.3892/etm.2017.4869

    Figure Lengend Snippet: Figure 4. miR‑210 has an effect on the protein levels of GAP‑43, MAG and MBP. (A and B) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of GAP‑43 were detected by western blot analysis. Relative protein levels were calculated using β‑actin as an internal reference. (C and D) The protein levels of MBP were detected by western blot after transfection with miR‑210 mimics or miR‑210 inhibitor. β‑actin was used as an internal reference. (E and F) After transfection with miR‑210 mimics or miR‑210 inhibitor, the protein levels of MAG were detected by western blot using β‑actin as an internal reference. All experiments were repeated three times and values are expressed as the mean ± standard deviation. **P<0.01, ***P<0.001. miR, microRNA; MAG, myelin‑associated glycoprotein; MBP, myelin basic protein; GAP‑43, growth‑associated protein 43; NC, negative control.

    Article Snippet: The membranes were blocked with 5% skimmed milk, followed by incubation with primary antibodies against growth-associated protein-43 (GAP-43; 1:200 dilution; Santa Cruz Biotechnologies, Inc., Dallas, TX, USA; cat. no. sc-33705), myelin-associated glycoprotein (MAG; 1:500 dilution; Bioss, Beijing, China; cat no. bs-0257R), myelin basic protein (MBP; 1:500 dilution; Bioss; cat. no. bs-0380R) and β‐actin (1:1,000, Santa Cruz Biotechnologies, Inc.) at 4 ̊C overnight.

    Techniques: Transfection, Western Blot, Standard Deviation, Negative Control

    Journal: Cell reports

    Article Title: PARP1-mediated PARylation activity is essential for oligodendroglial differentiation and CNS myelination

    doi: 10.1016/j.celrep.2021.109695

    Figure Lengend Snippet:

    Article Snippet: Rabbit polyclonal MAG , Millipore , Cat#AB1567; RRID: AB_2110397.

    Techniques: Binding Assay, Purification, Control, Recombinant, Electron Microscopy, Protein Extraction, Lysis, Protease Inhibitor, Transfection, Staining, Bicinchoninic Acid Protein Assay, Magnetic Beads, SYBR Green Assay, Western Blot, Knock-Out, Software

    Top 10 upregulated and downregulated proteins in Sham group and Caffeine group compared with the HI group

    Journal: CNS Neuroscience & Therapeutics

    Article Title: Proteomic analysis of the effects of caffeine in a neonatal rat model of hypoxic‐ischemic white matter damage

    doi: 10.1111/cns.13834

    Figure Lengend Snippet: Top 10 upregulated and downregulated proteins in Sham group and Caffeine group compared with the HI group

    Article Snippet: The membranes were blocked with 5% fat‐free milk and then incubated with the following primary antibodies: rabbit anti‐MBP monoclonal antibodies (1:1000), mouse anti‐SITR2 monoclonal antibodies (1:2500), rabbit anti‐myelin‐associated glycoprotein (MAG) polyclonal antibodies (1:1000; cat. no. 14386‐1‐AP; Proteintech), rabbit anti‐myelin proteolipid protein (PLP) polyclonal antibodies (1:1000; cat. no. DF13282; Affinity Biosciences), rabbit anti‐PSD‐95 polyclonal antibodies (1:1000), and rabbit anti‐synaptophysin polyclonal antibodies (1:5000); rabbit anti‐β‐tubulin polyclonal antibodies (1:5000; cat. no. 10068‐1‐AP; Proteintech) was used as the loading control.

    Techniques: Sequencing, Histone Deacetylase Assay, RNA Binding Assay