rabbit polyclonal anti-lin28a Search Results


90
Absolute Biotech Inc rabbit polyclonal anti-lin28a
(A) Quantification (top) and representative immunoblot (bottom) of <t>Lin28a</t> protein levels in lysates from hippocampal neurons exposed to BDNF with or without transcription blockade (Actinomycin-D) for the indicated times, normalized to GAPDH and plotted relative to 0-min BDNF without Actino-mycin-D (set as 1.0). #p < 0.05, ANOVA; *p < 0.05, t test.
Rabbit Polyclonal Anti Lin28a, supplied by Absolute Biotech Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal anti-lin28a/product/Absolute Biotech Inc
Average 90 stars, based on 1 article reviews
rabbit polyclonal anti-lin28a - by Bioz Stars, 2026-02
90/100 stars
  Buy from Supplier

92
Cusabio lin28a
(A) Quantification (top) and representative immunoblot (bottom) of <t>Lin28a</t> protein levels in lysates from hippocampal neurons exposed to BDNF with or without transcription blockade (Actinomycin-D) for the indicated times, normalized to GAPDH and plotted relative to 0-min BDNF without Actino-mycin-D (set as 1.0). #p < 0.05, ANOVA; *p < 0.05, t test.
Lin28a, supplied by Cusabio, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/lin28a/product/Cusabio
Average 92 stars, based on 1 article reviews
lin28a - by Bioz Stars, 2026-02
92/100 stars
  Buy from Supplier

Image Search Results


(A) Quantification (top) and representative immunoblot (bottom) of Lin28a protein levels in lysates from hippocampal neurons exposed to BDNF with or without transcription blockade (Actinomycin-D) for the indicated times, normalized to GAPDH and plotted relative to 0-min BDNF without Actino-mycin-D (set as 1.0). #p < 0.05, ANOVA; *p < 0.05, t test.

Journal: Molecular cell

Article Title: A Rapid Induction Mechanism for Lin28a in Trophic Responses

doi: 10.1016/j.molcel.2016.12.025

Figure Lengend Snippet: (A) Quantification (top) and representative immunoblot (bottom) of Lin28a protein levels in lysates from hippocampal neurons exposed to BDNF with or without transcription blockade (Actinomycin-D) for the indicated times, normalized to GAPDH and plotted relative to 0-min BDNF without Actino-mycin-D (set as 1.0). #p < 0.05, ANOVA; *p < 0.05, t test.

Article Snippet: Rabbit polyclonal anti-Lin28a , LifeSpan Biosciences , Cat#LS-C165782 now LS- {"type":"entrez-nucleotide","attrs":{"text":"B11566","term_id":"2092687","term_text":"B11566"}} B11566.

Techniques: Western Blot

(A) Representative immunoblot (left) and quantified Lin28a protein levels (right) normalized to HSC70 from immunoblot of lysates from hippocampal neurons pre-treated with vehicle (DMSO) or the MEK/Erk inhibitor U0126 (30 min) prior to BDNF. Erk1/2 inhibition prevents Lin28a induction by BDNF (#p < 0.01, ANOVA) and decreases basal Lin28a protein levels (*p < 0.05, t test).

Journal: Molecular cell

Article Title: A Rapid Induction Mechanism for Lin28a in Trophic Responses

doi: 10.1016/j.molcel.2016.12.025

Figure Lengend Snippet: (A) Representative immunoblot (left) and quantified Lin28a protein levels (right) normalized to HSC70 from immunoblot of lysates from hippocampal neurons pre-treated with vehicle (DMSO) or the MEK/Erk inhibitor U0126 (30 min) prior to BDNF. Erk1/2 inhibition prevents Lin28a induction by BDNF (#p < 0.01, ANOVA) and decreases basal Lin28a protein levels (*p < 0.05, t test).

Article Snippet: Rabbit polyclonal anti-Lin28a , LifeSpan Biosciences , Cat#LS-C165782 now LS- {"type":"entrez-nucleotide","attrs":{"text":"B11566","term_id":"2092687","term_text":"B11566"}} B11566.

Techniques: Western Blot, Inhibition

(A) Representative immunoblot (left) and densitometric quantification (right) of purified Lin28a protein co-associated with purified GST-TRBP, normalized to TRBP pull-down and plotted relative to GST-TRBPWT (set as 1.0). A lower band in the GST-TRBP conditions that migrates similarly to GST alone reflects partial cleavage of the GST tag through a protease site between GST and TRBP. Uncropped blots are shown in Figure S4A.

Journal: Molecular cell

Article Title: A Rapid Induction Mechanism for Lin28a in Trophic Responses

doi: 10.1016/j.molcel.2016.12.025

Figure Lengend Snippet: (A) Representative immunoblot (left) and densitometric quantification (right) of purified Lin28a protein co-associated with purified GST-TRBP, normalized to TRBP pull-down and plotted relative to GST-TRBPWT (set as 1.0). A lower band in the GST-TRBP conditions that migrates similarly to GST alone reflects partial cleavage of the GST tag through a protease site between GST and TRBP. Uncropped blots are shown in Figure S4A.

Article Snippet: Rabbit polyclonal anti-Lin28a , LifeSpan Biosciences , Cat#LS-C165782 now LS- {"type":"entrez-nucleotide","attrs":{"text":"B11566","term_id":"2092687","term_text":"B11566"}} B11566.

Techniques: Western Blot, Purification

Shown is a graphical model. Left: at baseline, TRBP undergoes polyubiquitination and degradation facilitated by Merlin protein. Lin28a protein levels are negligible as it undergoes rapid turnover. Right: growth factor binding to cognate receptors activates Erk1/2 signaling and subsequent TRBP phosphorylation, which stabilizes TRBP and enhances the TRBP/Lin28a protein complex, elevating Lin28a protein levels. Downstream inhibition of Let-7 miRNAs facilitates protein synthesis from pro-growth mRNAs. Bottom: The rapid Erk1/2-dependent induction pathway exerts Lin28a-dependent trophic effects on neuronal spines and peritoneal macrophage survival.

Journal: Molecular cell

Article Title: A Rapid Induction Mechanism for Lin28a in Trophic Responses

doi: 10.1016/j.molcel.2016.12.025

Figure Lengend Snippet: Shown is a graphical model. Left: at baseline, TRBP undergoes polyubiquitination and degradation facilitated by Merlin protein. Lin28a protein levels are negligible as it undergoes rapid turnover. Right: growth factor binding to cognate receptors activates Erk1/2 signaling and subsequent TRBP phosphorylation, which stabilizes TRBP and enhances the TRBP/Lin28a protein complex, elevating Lin28a protein levels. Downstream inhibition of Let-7 miRNAs facilitates protein synthesis from pro-growth mRNAs. Bottom: The rapid Erk1/2-dependent induction pathway exerts Lin28a-dependent trophic effects on neuronal spines and peritoneal macrophage survival.

Article Snippet: Rabbit polyclonal anti-Lin28a , LifeSpan Biosciences , Cat#LS-C165782 now LS- {"type":"entrez-nucleotide","attrs":{"text":"B11566","term_id":"2092687","term_text":"B11566"}} B11566.

Techniques: Binding Assay, Inhibition

KEY RESOURCES TABLE

Journal: Molecular cell

Article Title: A Rapid Induction Mechanism for Lin28a in Trophic Responses

doi: 10.1016/j.molcel.2016.12.025

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: Rabbit polyclonal anti-Lin28a , LifeSpan Biosciences , Cat#LS-C165782 now LS- {"type":"entrez-nucleotide","attrs":{"text":"B11566","term_id":"2092687","term_text":"B11566"}} B11566.

Techniques: Recombinant, Protease Inhibitor, TaqMan microRNA Assay, Plasmid Preparation, shRNA, Software