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Biosynth Carbosynth dithiol proteasecleavable peptide cross linker gpq w gcrdgpqgiwgqdrcg new england peptides inc
Dithiol Proteasecleavable Peptide Cross Linker Gpq W Gcrdgpqgiwgqdrcg New England Peptides Inc, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/england+peptide+inc/Toluene-3%2C4-dithiol/pm39643619-275-56-62
Average 93 stars, based on 1 article reviews

dithiol proteasecleavable peptide cross linker gpq w gcrdgpqgiwgqdrcg new england peptides inc - by Bioz Stars, 2026-09

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Article Title: Functional T cells are capable of supernumerary cell division and longevity.
Article Snippet: .. Cells were added to the wells of a 96-well plate and medium containing brefeldin A from Tonbo Biosciences and various concentrations of RGYVYQGL VSV-N peptide synthesized by New England Peptide Inc (now named Vivitide) to yield a final concentration of 3 μM brefeldin A and labelled concentrations of peptide. .. After 4–5 h, cells were stained extracellularly with anti-mouse CD8a (53-6.7; 1:100) from BD Biosciences, anti-mouse CD45.1 (A20; 1:400), anti-mouse CD45.2 (104; 1:400) and Ghost Dye Red 780 (1:1,000) from Tonbo Biosciences and N-tetramer (1:200), fixed and permeabilized using Tonbo Foxp3/ Transcription Factor Staining Kit, and then stained intracellularly in Tonbo Permeabilization buffer with TNF (MP6-XT22; 1:100) from BD Biosciences and IFNγ (XMG1.2; 1:100) from BioLegend.

Article Title: The TAG Family of Cancer/Testis Antigens is Widely Expressed in a Variety of Malignancies and Gives Rise to HLA-A2–Restricted Epitopes
Article Snippet: The TAG-1, TAG-2a, TAG-2b, and TAG-2c cancer/ testis genes, known to be expressed in an unusually high percentage of melanoma cell lines, are shown here to be expressed in a variety of tumor lines of diverse histologic type, including cancers of the brain, breast, colon, lung, ovary, pharynx, and tongue.. The genes are also expressed in fresh, uncultured melanoma, and ovarian cancer cells.. Epitope prediction algorithms were used to identify potential HLA-A1, HLA-A2, HLA-A3, HLA-B7, and HLA-B8 epitopes, and these potential epitopes were tested for their ability to stimulate a peptide-specific cytotoxic T lymphocyte response using lymphocytes from healthy donors.

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NAP effect on tyrosine phosphorylation (pY) of the 16-amino acid FIQGY-peptide fragment derived from the L1-CD, containing a single tyrosine. (A) 2A2-L1s cells were incubated in the absence and presence of 10−9 M NAP, and extracted cell lysates were incubated with FIGQY-peptide conjugated to agarose beads at room temperature for the indicated time (Methods). FIGQpY-peptide was measured using mouse anti-pY mAb (PY20). The magnitude of pY in FIGQY-peptide was quantified by densitometric analysis of anti-pY antibody-agarose bead bands separated by SDS-PAGE. Densities of FIGQpY-peptide bands were normalized to values obtained at time 0. Shown are mean ± SEM % FIGQpY-peptide compared to values at time 0 from 5 independent experiments (F =9.84, p< 0.0001). Peak phosphorylation occurred at 10 minutes following NAP treatment of intact cells. (B) Dose response curve for NAP phosphorylation of FIQGY-peptide by cell lysate from NAP-treated 2A2-L1s cells. Reactions were carried out for 10 min at room temperature in the presence of the indicated concentrations of NAP. pY levels were normalized to values in cells that were not treated with NAP (lane 0). Shown is a representative gel from 12 experiments. Densitometry was obtained from 7 – 12 independent experiments (F = 2.48, p < 0.05). (C) Lysate of cerebral cortex from post-natal day 10 rat pups was incubated in the absence and presence of 10−12 M NAP for 10 minutes. NAP treatment of rat brain lysates significantly increased phosphorylation of FIGQY-peptide (n=7; **t=2.888, ** p < 0.01). (D) 2A2-L1s cells were incubated for 15 minutes at room temperature in the absence and presence of 10−9 M NAP and 20 uM PP2, and cell lysates were then incubated with FIGQY-peptide to determine the effect of drug treatments on pY; *t=3.45, *p=0.010, n=8; **t=3.55, **p=0.0085, n=8.

Journal: Biological psychiatry

Article Title: Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G

doi: 10.1016/j.biopsych.2019.08.020

Figure Lengend Snippet: NAP effect on tyrosine phosphorylation (pY) of the 16-amino acid FIQGY-peptide fragment derived from the L1-CD, containing a single tyrosine. (A) 2A2-L1s cells were incubated in the absence and presence of 10−9 M NAP, and extracted cell lysates were incubated with FIGQY-peptide conjugated to agarose beads at room temperature for the indicated time (Methods). FIGQpY-peptide was measured using mouse anti-pY mAb (PY20). The magnitude of pY in FIGQY-peptide was quantified by densitometric analysis of anti-pY antibody-agarose bead bands separated by SDS-PAGE. Densities of FIGQpY-peptide bands were normalized to values obtained at time 0. Shown are mean ± SEM % FIGQpY-peptide compared to values at time 0 from 5 independent experiments (F =9.84, p< 0.0001). Peak phosphorylation occurred at 10 minutes following NAP treatment of intact cells. (B) Dose response curve for NAP phosphorylation of FIQGY-peptide by cell lysate from NAP-treated 2A2-L1s cells. Reactions were carried out for 10 min at room temperature in the presence of the indicated concentrations of NAP. pY levels were normalized to values in cells that were not treated with NAP (lane 0). Shown is a representative gel from 12 experiments. Densitometry was obtained from 7 – 12 independent experiments (F = 2.48, p < 0.05). (C) Lysate of cerebral cortex from post-natal day 10 rat pups was incubated in the absence and presence of 10−12 M NAP for 10 minutes. NAP treatment of rat brain lysates significantly increased phosphorylation of FIGQY-peptide (n=7; **t=2.888, ** p < 0.01). (D) 2A2-L1s cells were incubated for 15 minutes at room temperature in the absence and presence of 10−9 M NAP and 20 uM PP2, and cell lysates were then incubated with FIGQY-peptide to determine the effect of drug treatments on pY; *t=3.45, *p=0.010, n=8; **t=3.55, **p=0.0085, n=8.

Article Snippet: Antibody goat polyclonal antibody (pAb) against the L1-CD Santa Cruz Biotech SC-1508, RRID: AB_631086 mAb against the L1-ECD Santa Cruz Biotech SC-53386 RRID: AB_628937 total L1; rabbit pAb against C-terminus of ankyrin-G Santa Cruz Biotech SC-28561, RRID: AB_633909 mAb against spectrin Santa Cruz Biotech SC-46696, RRID: AB_671135 goat pAb against actin Santa Cruz Biotech SC-1616 , RRID: AB630836 mAB against EphB2 Santa Cruz Biotech SC-130752, RRID: AB_2099957 goat pAb to actin Santa Cruz Biotech SC-1616, RRID AB630836 rabbit pAb against Src Santa Cruz Biotech SC-18, RRID:AB_631324 Antibody mAB anti-Phosphotyrosine Abcam ab10321, RRID: AB_297058 HRP-conjugated secondary antibodies against mouse Jackson ImmunoResearch Laboratories 115-035-062, RRID: AB_2338504 rHRP-conjugated secondary antibodies against rabbit Jackson ImmunoResearch Laboratories 711-035-152, RRID: AB_10015282 rHRP-conjugated secondary antibodies against Goat Jackson ImmunoResearch Laboratories 705-035-003, RRID: AB_2340390 mAb 5G3 Maine Biotech Services ascites production service Bacterial or Viral Strain goat anti-mouse IgG conjugated with Alexa Fluor-546 Thermo Fisher Scientific A-11003, RRID: AB_2534071 goat anti-rabbit IgG conjugated with Alexa Fluor 488 Thermo Fisher Scientific R37120 , RRID: AB_2556548 mAB to b-tubulin Cell Signaling Technology #86298, RRID:AB_2715541 Biological Sample Recombinant Human EphB2 Protein Thermo Fisher Scientific PV3625 Kinase assay buffer Thermo Fisher Scientific PV3189 Biological Sample Sprague Dawley rat pups Charles River Breeding, Worcester, MA Cell Line NIH/3T3 American Type Culture Collection (ATCC) CRL-1658 Chemical Compound or Drug Commercial Assay Or Kit Halt Protease and Phosphatase Inhibitor Cocktail Thermo Scientific Cat #: 1862495 Lipofectamine 2000 Invitrogen Cat#: 11668027 NHS-activated dry agarose beasds Thermofisher Cat #: 26196, Deposited Data; Public Database Genetic Reagent Organism/Strain Peptide, Recombinant Protein NAP New England Peptide Inc FIGQY peptides Genscript USA Inc. Recombinant DNA plasmid, pcDNA3+ wild-type human L1 (hL1) cDNA gene Dr. Patricia Maness, The University of Nother Carolina at Chapell Hill LK, Thelen K, Maness PF.

Techniques: Derivative Assay, Incubation, SDS Page

NAP activation of EphB2 phosphorylation of L1. (A) Effect of NAP on association of L1 with EphB2. L1 was immunoprecipitated with mAb 5G3 from 2A2-L1s cells in the absence and presence of 10−9 M NAP, and coimmunoprecipitated proteins were separated and blotted with antibodies to L1 and EphB2. Densities of EphB2 bands were normalized to those for L1, and values for NAP treatment were expressed as a percentage of control values. Shown is the mean ± SEM % increase in L1 association with EphB2 following NAP treatment derived from 8-9 independent experiments; *t=3.17,*p <0.05, n = 8. (B) Dose-dependent stimulation by NAP of tyrosine phosphorylation of FIGQY-peptide by recombinant EphB2 (F = 2.45, p<0.05). pY levels following NAP treatment were normalized to control values (0 NAP). Shown is the mean ± SEM % increase in pY levels following treatment with the indicated concentrations of NAP derived from 6-9 independent experiments (C) Stimulation of EphB2 phosphorylation of L1 by 10−9 M NAP and P7A-NAP (P7A), but not by 10−9 M I6A-NAP (I6A), SAL, or octanol (Oct). Shown is a representative gel and densitometric analysis from 7 independent experiments. pY levels for each drug treatment were normalized to values obtained in the absence of drugs (Control) (F = 2.84, p<0.05); **t = 4.01, **p = 0.0070; *t= 3.01, *p=0.0235, n=7.

Journal: Biological psychiatry

Article Title: Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G

doi: 10.1016/j.biopsych.2019.08.020

Figure Lengend Snippet: NAP activation of EphB2 phosphorylation of L1. (A) Effect of NAP on association of L1 with EphB2. L1 was immunoprecipitated with mAb 5G3 from 2A2-L1s cells in the absence and presence of 10−9 M NAP, and coimmunoprecipitated proteins were separated and blotted with antibodies to L1 and EphB2. Densities of EphB2 bands were normalized to those for L1, and values for NAP treatment were expressed as a percentage of control values. Shown is the mean ± SEM % increase in L1 association with EphB2 following NAP treatment derived from 8-9 independent experiments; *t=3.17,*p <0.05, n = 8. (B) Dose-dependent stimulation by NAP of tyrosine phosphorylation of FIGQY-peptide by recombinant EphB2 (F = 2.45, p<0.05). pY levels following NAP treatment were normalized to control values (0 NAP). Shown is the mean ± SEM % increase in pY levels following treatment with the indicated concentrations of NAP derived from 6-9 independent experiments (C) Stimulation of EphB2 phosphorylation of L1 by 10−9 M NAP and P7A-NAP (P7A), but not by 10−9 M I6A-NAP (I6A), SAL, or octanol (Oct). Shown is a representative gel and densitometric analysis from 7 independent experiments. pY levels for each drug treatment were normalized to values obtained in the absence of drugs (Control) (F = 2.84, p<0.05); **t = 4.01, **p = 0.0070; *t= 3.01, *p=0.0235, n=7.

Techniques: Activation Assay, Immunoprecipitation, Derivative Assay, Recombinant

Effect of EphB2 knockdown on NAP antagonism of ethanol inhibition of L1 adhesion. (A) 2A2-L1s cells were treated with an EphB2 siRNA or a scrambled siRNA. L1 and actin were used as loading controls, and densities of protein bands were normalized to those obtained in untreated cells (Control). Shown is a representative gel and mean ± SEM % changes in EphB2 expression derived from 9 independent experiments (F=9.33, p< 0.001); * t =1.07, p <0.0.0044, n=10. (B) EphB2 siRNA specifically reduced while scrambled siRNA had no effect on the phosphorylation of FIGQY-peptide from lysates of 2A2-L1s cells treated with 10−12 M NAP. Values for pY in NAP-treated siRNA-treated cells were normalized to values in control cells that were not treated with NAP (F = 2.77, p < 0.05); *t = 2.47, p =0.04, n=8; t = 2.54, p=0.039, n =8. (C) EphB2-siRNA specifically reduced while scrambled siRNA had no effect on NAP antagonism of ethanol inhibition of L1 adhesion. Values for ethanol inhibition of L1 adhesion in the presence of NAP were normalized to values obtained in the absence of NAP (38.6 ± 6.9%) (F = 7.17, p < 0.0001); t= 9.30, ***p =0.0000, n = 9; t = 7.41, ***p = 0.0001, n =9).

Journal: Biological psychiatry

Article Title: Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G

doi: 10.1016/j.biopsych.2019.08.020

Figure Lengend Snippet: Effect of EphB2 knockdown on NAP antagonism of ethanol inhibition of L1 adhesion. (A) 2A2-L1s cells were treated with an EphB2 siRNA or a scrambled siRNA. L1 and actin were used as loading controls, and densities of protein bands were normalized to those obtained in untreated cells (Control). Shown is a representative gel and mean ± SEM % changes in EphB2 expression derived from 9 independent experiments (F=9.33, p< 0.001); * t =1.07, p <0.0.0044, n=10. (B) EphB2 siRNA specifically reduced while scrambled siRNA had no effect on the phosphorylation of FIGQY-peptide from lysates of 2A2-L1s cells treated with 10−12 M NAP. Values for pY in NAP-treated siRNA-treated cells were normalized to values in control cells that were not treated with NAP (F = 2.77, p < 0.05); *t = 2.47, p =0.04, n=8; t = 2.54, p=0.039, n =8. (C) EphB2-siRNA specifically reduced while scrambled siRNA had no effect on NAP antagonism of ethanol inhibition of L1 adhesion. Values for ethanol inhibition of L1 adhesion in the presence of NAP were normalized to values obtained in the absence of NAP (38.6 ± 6.9%) (F = 7.17, p < 0.0001); t= 9.30, ***p =0.0000, n = 9; t = 7.41, ***p = 0.0001, n =9).

Techniques: Inhibition, Expressing, Derivative Assay

Journal: Biological psychiatry

Article Title: Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G

doi: 10.1016/j.biopsych.2019.08.020

Figure Lengend Snippet: KEY RESOURCES TABLE

Techniques: Recombinant, Protein Kinase Assay, Kinase Assay, Plasmid Preparation, Sequencing, Software, Transfection, Construct, Expressing

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