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biotinylated ephrin b1 fc (R&D Systems)

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R&D Systems biotinylated ephrin b1 fc
Biotinylated Ephrin B1 Fc, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+ephrin+a5+fc/Recombinant+Human+Ephrin-A5+Fc+Chimera+Biotinylated+Protein/pm41692350-89-26-28
Average 90 stars, based on 5 article reviews

biotinylated ephrin b1 fc - by Bioz Stars, 2026-09

90/100 stars

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Incubation:

Article Title: Boundary cells regulate a switch in the expression of FGF3 in hindbrain rhombomeres
Article Snippet: .. Briefly, embryos were incubated in PBS with 0.1% Tween20, 5% goat serum for 2 hours (hrs) prior to incubation for 16 hrs with the following antibodies: rabbit anti-GFP (1:400, Molecular Probes, CA USA), rabbit anti-EphA4 (1:250) [33], mouse anti-chondroitin sulphate proteoglycan (CSPG, 1:50, Sigma, MO USA), as Page 2 of 12 (page number not for citation purposes) well as recombinant human ephrin A5-Fc (5 μg/ml, R&D systems, MN USA). .. Following PBS washes, the following secondary antibodies were added: anti-rabbit or antimouse Alexa 488 and anti-rabbit Alexa 594 (all 1:400, Molecular Probes, CA USA) to be visualized under epi-fluorescent microscope, or anti-rabbit and anti-mouse-HRP (1:250, Sigma, MO USA) visualized with AEC substrate system (Lab Vision Corporation, CA USA).

Article Title: Ephrin-A5/EphA4 signalling controls specific afferent targeting to cochlear hair cells.
Article Snippet: .. SGNs from newborn mice were isolated, cultured as previously described51 and incubated with a 5 mg ml 1 human ephrin-A5-Fc (R&D systems, Minneapolis, MN, USA) solution pre-clustered for 1 h at 37 C with 50mg ml 1 anti-human IgG-Fc (R&D systems, Minneapolis, MN, USA). .. Before beginning growth cone collapse assay, cells were pre-treated with either Y-27632 dihydrochloride (7 h, 10 mM; Tocris, Bristol, UK) or ML-7 (5 h, 10mM; Sigma-Aldrich, St Louis, MO, USA).

Article Title: Boundary cells regulate a switch in the expression of FGF3 in hindbrain rhombomeres
Article Snippet: .. Briefly, embryos were incubated in PBS with 0.1% Tween20, 5% goat serum for 2 hours (hrs) prior to incubation for 16 hrs with the following antibodies: rabbit anti-GFP (1:400, Molecular Probes, CA USA), rabbit anti-EphA4 (1:250) [ ], mouse anti-chondroitin sulphate proteoglycan (CSPG, 1:50, Sigma, MO USA), as well as recombinant human ephrin A5-Fc (5 μg/ml, R&D systems, MN USA). .. Following PBS washes, the following secondary antibodies were added: anti-rabbit or anti-mouse Alexa 488 and anti-rabbit Alexa 594 (all 1:400, Molecular Probes, CA USA) to be visualized under epi-fluorescent microscope, or anti-rabbit and anti-mouse-HRP (1:250, Sigma, MO USA) visualized with AEC substrate system (Lab Vision Corporation, CA USA).

Recombinant:

Article Title: Ephrin-A/EphA specific co-adaptation as a novel mechanism in topographic axon guidance
Article Snippet: .. The medium on explant cultures was replaced with warm F12-MC containing recombinant human ephrin-A5-Fc, mouse EphA3-Fc (both RnD Systems, Minneapolis, MN, USA) or human Fc fragment (Calbiochem, San Diego, CA, USA). .. For inhibitor experiments, 30 mM Pitstop2 (Abcam, Cambridge, UK) or 400 mU/ml sphingomyelinase (Sigma-Aldrich, St. Louis, MO, USA) in F12-MC was applied during a 15 or 30 min pre-incubation, respectively, and thereafter together with ephrin-A5-Fc, EphA3-Fc or Fc.

Article Title: Boundary cells regulate a switch in the expression of FGF3 in hindbrain rhombomeres
Article Snippet: .. Briefly, embryos were incubated in PBS with 0.1% Tween20, 5% goat serum for 2 hours (hrs) prior to incubation for 16 hrs with the following antibodies: rabbit anti-GFP (1:400, Molecular Probes, CA USA), rabbit anti-EphA4 (1:250) [ ], mouse anti-chondroitin sulphate proteoglycan (CSPG, 1:50, Sigma, MO USA), as well as recombinant human ephrin A5-Fc (5 μg/ml, R&D systems, MN USA). .. Following PBS washes, the following secondary antibodies were added: anti-rabbit or anti-mouse Alexa 488 and anti-rabbit Alexa 594 (all 1:400, Molecular Probes, CA USA) to be visualized under epi-fluorescent microscope, or anti-rabbit and anti-mouse-HRP (1:250, Sigma, MO USA) visualized with AEC substrate system (Lab Vision Corporation, CA USA).

Article Title: Ephrin-A/EphA specific co-adaptation as a novel mechanism in topographic axon guidance
Article Snippet: .. The medium on explant cultures was replaced with warm F12-MC containing recombinant human ephrin-A5-Fc, mouse EphA3-Fc (both RnD Systems, Minneapolis, MN, USA) or human Fc fragment (Calbiochem, San Diego, CA, USA). .. For inhibitor experiments, 30 μM Pitstop2 (Abcam, Cambridge, UK) or 400 mU/ml sphingomyelinase (Sigma-Aldrich, St. Louis, MO, USA) in F12-MC was applied during a 15 or 30 min pre-incubation, respectively, and thereafter together with ephrin-A5-Fc, EphA3-Fc or Fc.

Isolation:

Cell Culture:

Control:

Article Title: Ephrin-A5 acts as a repulsive cue for migrating cortical interneurons.
Article Snippet: Cortical interneurons are born in the germinative zones of the ganglionic eminences in the subpallium, and migrate tangentially in spatially and temporally well-defined corridors into the neocortex.. Because ephrin-A5 is expressed in the ventricular zone (VZ) of the ganglionic eminences at these developmental stages, we examined the possible effects of this molecule on interneuron migration.. Double-immunocytochemistry of dissociated neurons from the medial ganglionic eminences (MGE) revealed that calbindin-positive cells express the EphA4-receptor.

Saline:

Injection:

Staining:

Article Title: Ephrin-A5 inhibits growth of embryonic sensory neurons.
Article Snippet: To visualize expression of EphA receptors on growth cones, E7 DRGs were dissected from 1 to 3 embryos, cut into 2–6 pieces (‘‘DRG explants’’), pooled, and 3–4 explants were plated in glass-bottomed wells coated with poly-dl-ornithine and laminin, and cultured overnight in F14/N2 (Gibco), supplemented with either NGF or NT3, as described previously for trigeminal neurons (Adams and Scott, 1998). .. Live cultures were incubated with human ephrin-A5-Fc (10 Ag/ml; R & D Systems, Minneapolis, MN) for 1 h at 37-C, fixed in 4% paraformaldehyde with 10% sucrose in PBS, and stained with biotinylated antihuman-IgG-Fc antibody (Jackson, West Grove, PA) amplified with Tyramide Signal Amplification (TSA, New England Nuclear, Boston, MA) and Texas Red avidin (Vector, Burlingame, CA). ..

Amplification:

Avidin-Biotin Assay:

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$RNase1‐induced T‐cell dysregulation may require the internalization of RNase1 into T cells. A) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in EphA4‐knockdown (sh‐EphA4#1), ALK‐knockdown (sh‐ALK#1), or control (sh‐Ctrl) activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). B) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with different concentrations of recombinant EphrinA5 as indicated for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). C) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), Cpd1 (10 µ m ), or RNase1 combined to Cpd1 for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). D) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), crizotinib (0.5 µ m ), or RNase1 combined to crizotinib for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). E) Left: Western blot analysis of RNase1 in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) for different time‐points as indicated. Right: Western blot analysis of RNase1 in unactivated PBMC‐derived T cells and activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) for different time‐points as indicated. β‐actin served as a loading control. Representative data from three independent experiments. F) Left: Western blot analysis of RNase1 in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) or RNase1 combined with dynasore (10 µ m for 1 h treatment) for 48 h. Right: Quantitative results of Western blot of RNase1 in the left panel of (F). Quantitative data were analyzed from three independent experiments. G) Left: Western blot analysis of RNase1 in unactivated PBMC‐derived T cells and activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) or RNase1 combined with dynasore (10 µ m for 1 h treatment) for 48 h. β‐actin served as a loading control. Right: Quantitative results of Western blot of RNase1 in the left panel of (G). Quantitative data were analyzed from three independent experiments. H) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), dynasore (10 µ m for 1 h treatment), or RNase1 combined with dynasore (20 µ m for 1 h treatment) for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). I) Western blot analysis of the whole cell lysate (WCL), cytoplasmic, and nuclear fractions in activated Jurkat T cells (JA) and 1 µg mL −1 RNase1‐treated activated Jurkat T cells (JAR). Representative data from three independent experiments. J) Immunocytochemistry staining of RNase1 in activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) for 48 h. Nuclei were counterstained with DAPI. Representative images of n = 2 independent replicates. Scale bar: 10 µm. Data represent mean ± S.D. ** p , 0.001–0.01, and *** p < 0.001 by two‐sided unpaired Student's t ‐test.$

Journal: Advanced Science

Article Title: Ribonuclease 1 Induces T‐Cell Dysfunction and Impairs CD8 + T‐Cell Cytotoxicity to Benefit Tumor Growth through Hijacking STAT1

doi: 10.1002/advs.202404961

Figure Lengend Snippet: RNase1‐induced T‐cell dysregulation may require the internalization of RNase1 into T cells. A) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in EphA4‐knockdown (sh‐EphA4#1), ALK‐knockdown (sh‐ALK#1), or control (sh‐Ctrl) activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). B) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with different concentrations of recombinant EphrinA5 as indicated for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). C) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), Cpd1 (10 µ m ), or RNase1 combined to Cpd1 for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). D) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), crizotinib (0.5 µ m ), or RNase1 combined to crizotinib for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). E) Left: Western blot analysis of RNase1 in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) for different time‐points as indicated. Right: Western blot analysis of RNase1 in unactivated PBMC‐derived T cells and activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) for different time‐points as indicated. β‐actin served as a loading control. Representative data from three independent experiments. F) Left: Western blot analysis of RNase1 in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ) or RNase1 combined with dynasore (10 µ m for 1 h treatment) for 48 h. Right: Quantitative results of Western blot of RNase1 in the left panel of (F). Quantitative data were analyzed from three independent experiments. G) Left: Western blot analysis of RNase1 in unactivated PBMC‐derived T cells and activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) or RNase1 combined with dynasore (10 µ m for 1 h treatment) for 48 h. β‐actin served as a loading control. Right: Quantitative results of Western blot of RNase1 in the left panel of (G). Quantitative data were analyzed from three independent experiments. H) Quantitative RT‐PCR analysis of IL‐2 mRNA expression in unactivated Jurkat T cells and activated Jurkat T cells treated without or with RNase1 (1 µg mL −1 ), dynasore (10 µ m for 1 h treatment), or RNase1 combined with dynasore (20 µ m for 1 h treatment) for 48 h. Representative data from three independent experiments (each experiment contains three technical replicates). I) Western blot analysis of the whole cell lysate (WCL), cytoplasmic, and nuclear fractions in activated Jurkat T cells (JA) and 1 µg mL −1 RNase1‐treated activated Jurkat T cells (JAR). Representative data from three independent experiments. J) Immunocytochemistry staining of RNase1 in activated PBMC‐derived T cells treated without or with RNase1 (1 µg mL −1 ) for 48 h. Nuclei were counterstained with DAPI. Representative images of n = 2 independent replicates. Scale bar: 10 µm. Data represent mean ± S.D. ** p , 0.001–0.01, and *** p < 0.001 by two‐sided unpaired Student's t ‐test.

Article Snippet: Recombinant EphrinA5 (#374‐EA‐200, R&D Systems) was added to medium at the indicated concentrations for 48 h. The used concentrations of inhibitors were 10 μ m Cpd1 (#sc‐314230; Santa Cruz Biotechnology), 0.5 μ m crizotinib (#TM‐T1661‐1; TargetMol), and 10 μ m dynasore (#SI‐D7693; Sigma‐Aldrich).

Techniques: Quantitative RT-PCR, Expressing, Knockdown, Control, Recombinant, Western Blot, Derivative Assay, Immunocytochemistry, Staining