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Sino Biological
smagp ![a Schematics of type I, type II, type III and tail-anchored (TA) proteins showing their topologies in the ER membrane. b Outline of the in vitro assay where either canine pancreatic microsomes or semi-permeabilised HeLa cells were used as sources of ER membrane; following translation, membrane inserted radiolabelled precursor proteins are recovered by centrifugation and analysed by SDS-PAGE and phosphorimaging. The N-glycosylation of lumenal domains, confirmed by treatment with endoglycosidase H (Endo H), indicates successful membrane translocation/insertion. c The chemical structure of ipomoeassin F (Ipom-F), a potent and selective inhibitor of Sec61-mediated protein translocation . d Model type III TMPs used in this study were synthesised as outlined in ( b ) using canine pancreatic microsomes: ( di ) an N-terminally OPG2-tagged form of the HIV protein Vpu (OPG2Vpu), ( dii ) small cell adhesion glycoprotein containing an artificial N-glycosylation site <t>(SMAGP),</t> ( diii ) glycophorin C (GypC), ( div ) tumour necrosis factor receptor superfamily member 17 containing an artificial N-glycosylation <t>site</t> <t>(BCMA)</t> and ( dv ) synaptotagmin 1 (Syt1). Variably N-glycosylated (XGly) and non-glycosylated (0Gly) species are indicated, having been confirmed using Endo H (lane 2). Other symbols are: AAs, amino acid residues; Cyt, cytosol; Lum, ER lumen; RRL, rabbit reticulocyte lysate; s.s., N-terminal signal sequence. Estimated hydrophobicity values ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\triangle$$\end{document} △ Gapp) of predicted transmembrane domains (TMDs) in kcal /mol were calculated using: http://dgpred.cbr.su.se/ (full protein scan option). Charged amino acid residues, D, E, H, K, R; polar amino acid residues, N, Q, S, T, Y.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_9459/pmc08249459/pmc08249459__42003_2021_2363_Fig1_HTML.jpg) Smagp, supplied by Sino Biological, 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/product/bcma+expression/Human+BCMA%2FTNFRSF17%2FCD269+Gene+ORF+cDNA+clone+expression+plasmid/pmc08249459-208-7-13 Average 90 stars, based on 1 article reviews
smagp - by Bioz Stars,
2026-09
90/100 stars
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Boster Bio
human tnfrsf17 bcma enzyme Human Tnfrsf17 Bcma Enzyme, supplied by Boster Bio, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/bcma+expression/BCMA+(TNFRSF17)+(NM_001192)+Human+Over-expression+Lysate/pmc09511648__jitc___2022___005403supp002-22-13-19 Average 91 stars, based on 1 article reviews
human tnfrsf17 bcma enzyme - by Bioz Stars,
2026-09
91/100 stars
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Full length Clone DNA of Rattus norvegicus tumor necrosis factor receptor superfamily, member 17.
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Full length Clone DNA of Rat tumor necrosis factor receptor superfamily, member 17 with C terminal HA tag.
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Full length Clone DNA of Rat tumor necrosis factor receptor superfamily, member 17 with N terminal Myc tag.
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Full length Clone DNA of Human tumor necrosis factor receptor superfamily, member 17 with C terminal OFPSpark / RFP tag.
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Full length Clone DNA of Human tumor necrosis factor receptor superfamily, member 17 with C terminal His tag.
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Full length Clone DNA of Rat tumor necrosis factor receptor superfamily, member 17 with C terminal Myc tag.
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Full length Clone DNA of Rhesus tumor necrosis factor receptor superfamily, member 17 with C terminal His tag.
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Full length Clone DNA of Rhesus tumor necrosis factor receptor superfamily, member 17 with C terminal Myc tag.
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Full length Clone DNA of Rhesus tumor necrosis factor receptor superfamily, member 17 with C terminal HA tag.
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Full length Clone DNA of Human tumor necrosis factor receptor superfamily, member 17 with C terminal Myc tag.
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Image Search Results
Journal: Communications Biology
Article Title: An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum
doi: 10.1038/s42003-021-02363-z
Figure Lengend Snippet: a Schematics of type I, type II, type III and tail-anchored (TA) proteins showing their topologies in the ER membrane. b Outline of the in vitro assay where either canine pancreatic microsomes or semi-permeabilised HeLa cells were used as sources of ER membrane; following translation, membrane inserted radiolabelled precursor proteins are recovered by centrifugation and analysed by SDS-PAGE and phosphorimaging. The N-glycosylation of lumenal domains, confirmed by treatment with endoglycosidase H (Endo H), indicates successful membrane translocation/insertion. c The chemical structure of ipomoeassin F (Ipom-F), a potent and selective inhibitor of Sec61-mediated protein translocation . d Model type III TMPs used in this study were synthesised as outlined in ( b ) using canine pancreatic microsomes: ( di ) an N-terminally OPG2-tagged form of the HIV protein Vpu (OPG2Vpu), ( dii ) small cell adhesion glycoprotein containing an artificial N-glycosylation site (SMAGP), ( diii ) glycophorin C (GypC), ( div ) tumour necrosis factor receptor superfamily member 17 containing an artificial N-glycosylation site (BCMA) and ( dv ) synaptotagmin 1 (Syt1). Variably N-glycosylated (XGly) and non-glycosylated (0Gly) species are indicated, having been confirmed using Endo H (lane 2). Other symbols are: AAs, amino acid residues; Cyt, cytosol; Lum, ER lumen; RRL, rabbit reticulocyte lysate; s.s., N-terminal signal sequence. Estimated hydrophobicity values ( \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\triangle$$\end{document} △ Gapp) of predicted transmembrane domains (TMDs) in kcal /mol were calculated using: http://dgpred.cbr.su.se/ (full protein scan option). Charged amino acid residues, D, E, H, K, R; polar amino acid residues, N, Q, S, T, Y.
Article Snippet: The cDNAs for BCMA (Uniprot: Q02223) and
Techniques: In Vitro, Centrifugation, SDS Page, Translocation Assay, Sequencing
Journal: Communications Biology
Article Title: An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum
doi: 10.1038/s42003-021-02363-z
Figure Lengend Snippet: Primer list 1.
Article Snippet: The cDNAs for BCMA (Uniprot: Q02223) and
Techniques: Clone Assay, Plasmid Preparation
Journal: Communications Biology
Article Title: An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum
doi: 10.1038/s42003-021-02363-z
Figure Lengend Snippet: Primer list 2.
Article Snippet: The cDNAs for BCMA (Uniprot: Q02223) and
Techniques: Plasmid Preparation