Review



coding region for plxnb2  (Addgene inc)


Bioz Verified Symbol Addgene inc is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 92
      Buy from Supplier

    Structured Review

    Addgene inc coding region for plxnb2
    a , Domain organization of the TMEM260 substrate <t>PLXNB2,</t> highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.
    Coding Region For Plxnb2, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/coding region for plxnb2/product/Addgene inc
    Average 92 stars, based on 3 article reviews
    coding region for plxnb2 - by Bioz Stars, 2026-04
    92/100 stars

    Images

    1) Product Images from "Structure and mechanism of the human TMEM260 O-mannosyltransferase"

    Article Title: Structure and mechanism of the human TMEM260 O-mannosyltransferase

    Journal: bioRxiv

    doi: 10.64898/2026.03.17.711096

    a , Domain organization of the TMEM260 substrate PLXNB2, highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.
    Figure Legend Snippet: a , Domain organization of the TMEM260 substrate PLXNB2, highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.

    Techniques Used: Glycoproteomics, Reporter Assay, Control, Activity Assay

    a , Cryo-EM density map of TMEM260 in complex with the native donor Dol-P-Man and a PLXNB2-IPT1-derived acceptor peptide, determined at 3.1 Å resolution. Major structural regions are indicated and colored consistently throughout the figure. The top-right panel shows a view from the ER lumen, perpendicular to the membrane, with the acceptor peptide shown as a ribbon, the T822 glycosylation site highlighted and Dol-P-Man shown as sticks. This orientation emphasizes insertion of the N terminus into the finger region and positioning of the glycosylation site within the catalytic pocket. b , Front view of the corresponding atomic model in ribbon representation. Close-up (dashed circle) highlights the Dol-P-Man density and fitted model. c , Close-up of the ER-luminal region of TMEM260 shown in surface representation and colored by electrostatic potential, with the bound peptide as a ribbon and side chains as sticks. Dol-P-Man is shown as sticks and the T822 glycosylation site is indicated. d , Same view as in c , shown in ribbon representation to highlight specific interactions between TMEM260 residues and the acceptor peptide. The T822 glycosylation site is indicated. e , Sequence alignment of the PLXNB2-IPT1 peptide with reported O-mannosylated IPT domains from plexin, cMET and RON receptors, highlighting conserved residues proposed to define a TMEM260-specific acceptor sequon. f , Close-up of the active-site environment showing superposition of Dol-P-Man in the binary complex (all in grey including Dol-P-Man) and in the ternary complex (all in color with acceptor peptide in yellow and Dol-P-Man in black) with the PLXNB2-IPT1 peptide. In the ternary complex, the β-mannose moiety undergoes an approximately 60° rotation, indicating a peptide-induced reorientation of the donor sugar.
    Figure Legend Snippet: a , Cryo-EM density map of TMEM260 in complex with the native donor Dol-P-Man and a PLXNB2-IPT1-derived acceptor peptide, determined at 3.1 Å resolution. Major structural regions are indicated and colored consistently throughout the figure. The top-right panel shows a view from the ER lumen, perpendicular to the membrane, with the acceptor peptide shown as a ribbon, the T822 glycosylation site highlighted and Dol-P-Man shown as sticks. This orientation emphasizes insertion of the N terminus into the finger region and positioning of the glycosylation site within the catalytic pocket. b , Front view of the corresponding atomic model in ribbon representation. Close-up (dashed circle) highlights the Dol-P-Man density and fitted model. c , Close-up of the ER-luminal region of TMEM260 shown in surface representation and colored by electrostatic potential, with the bound peptide as a ribbon and side chains as sticks. Dol-P-Man is shown as sticks and the T822 glycosylation site is indicated. d , Same view as in c , shown in ribbon representation to highlight specific interactions between TMEM260 residues and the acceptor peptide. The T822 glycosylation site is indicated. e , Sequence alignment of the PLXNB2-IPT1 peptide with reported O-mannosylated IPT domains from plexin, cMET and RON receptors, highlighting conserved residues proposed to define a TMEM260-specific acceptor sequon. f , Close-up of the active-site environment showing superposition of Dol-P-Man in the binary complex (all in grey including Dol-P-Man) and in the ternary complex (all in color with acceptor peptide in yellow and Dol-P-Man in black) with the PLXNB2-IPT1 peptide. In the ternary complex, the β-mannose moiety undergoes an approximately 60° rotation, indicating a peptide-induced reorientation of the donor sugar.

    Techniques Used: Cryo-EM Sample Prep, Derivative Assay, Membrane, Glycoproteomics, Sequencing



    Similar Products

    coding region for plxnb2  (Addgene inc)
    92
    Addgene inc coding region for plxnb2
    a , Domain organization of the TMEM260 substrate <t>PLXNB2,</t> highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.
    Coding Region For Plxnb2, supplied by Addgene inc, 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/coding region for plxnb2/product/Addgene inc
    Average 92 stars, based on 1 article reviews
    coding region for plxnb2 - by Bioz Stars, 2026-04
    92/100 stars
    		  Buy from Supplier

    Image Search Results


    a , Domain organization of the TMEM260 substrate PLXNB2, highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.

    Journal: bioRxiv

    Article Title: Structure and mechanism of the human TMEM260 O-mannosyltransferase

    doi: 10.64898/2026.03.17.711096

    Figure Lengend Snippet: a , Domain organization of the TMEM260 substrate PLXNB2, highlighting IPT domains containing reported O-mannosylation sites. The AlphaFold-predicted structure of the PLXNB2-IPT1 domain is shown in pink with annotated β-strands. The T822 glycosylation site and characteristic IPT-domain prolines within the A-B strand region are indicated. b , MALDI-TOF analysis of peptide pulldowns using beads decorated with TMEM260 luminal truncations (Rl-TPR or TPR-only). The TPR region is necessary and sufficient for recruitment of the PLXNB2-IPT1 peptide. c , Schematic (top left) of the sfGFP-PLXNB2-IPT1 reporter assay used to assess TMEM260-catalyzed glycosylation in cells. Glycoproteomic analysis of T822 glycosite shows robust O-mannosylation in WT cells and in COSMC/POMGNT1 KO “SimpleCells” used as glycoengineering control, whereas O-mannose transfer to the sfGFP-PLXNB2-IPT1 reporter is abolished in HEK293 TMEM260 KO and HEK293 TMEM260 KO D52A KI cells (right). Model (bottom left) summarizing the experimental findings. In WT cells, the reporter enters the ER lumen, where the extended C-terminal peptide is recruited by TMEM260 and the T822 is O-mannosylated. In the absence of TMEM260 activity, the ER-resident O-mannosyltransferases TMTC1–4 or POMT1/2 enzymes do not act on the sfGFP-PLXNB2-IPT1 reporter.

    Article Snippet: The coding region for PLXNB2 (803-837) was amplified from pENTR223-PLXNB2 (Addgene plasmid #86236; gift from Roland Friedel; RRID:Addgene_86236) and RON (684-715) from pDONR223-MST1R (Addgene plasmid #23942; gift from William Hahn & David Root; RRID:Addgene_23942).

    Techniques: Glycoproteomics, Reporter Assay, Control, Activity Assay

    a , Cryo-EM density map of TMEM260 in complex with the native donor Dol-P-Man and a PLXNB2-IPT1-derived acceptor peptide, determined at 3.1 Å resolution. Major structural regions are indicated and colored consistently throughout the figure. The top-right panel shows a view from the ER lumen, perpendicular to the membrane, with the acceptor peptide shown as a ribbon, the T822 glycosylation site highlighted and Dol-P-Man shown as sticks. This orientation emphasizes insertion of the N terminus into the finger region and positioning of the glycosylation site within the catalytic pocket. b , Front view of the corresponding atomic model in ribbon representation. Close-up (dashed circle) highlights the Dol-P-Man density and fitted model. c , Close-up of the ER-luminal region of TMEM260 shown in surface representation and colored by electrostatic potential, with the bound peptide as a ribbon and side chains as sticks. Dol-P-Man is shown as sticks and the T822 glycosylation site is indicated. d , Same view as in c , shown in ribbon representation to highlight specific interactions between TMEM260 residues and the acceptor peptide. The T822 glycosylation site is indicated. e , Sequence alignment of the PLXNB2-IPT1 peptide with reported O-mannosylated IPT domains from plexin, cMET and RON receptors, highlighting conserved residues proposed to define a TMEM260-specific acceptor sequon. f , Close-up of the active-site environment showing superposition of Dol-P-Man in the binary complex (all in grey including Dol-P-Man) and in the ternary complex (all in color with acceptor peptide in yellow and Dol-P-Man in black) with the PLXNB2-IPT1 peptide. In the ternary complex, the β-mannose moiety undergoes an approximately 60° rotation, indicating a peptide-induced reorientation of the donor sugar.

    Journal: bioRxiv

    Article Title: Structure and mechanism of the human TMEM260 O-mannosyltransferase

    doi: 10.64898/2026.03.17.711096

    Figure Lengend Snippet: a , Cryo-EM density map of TMEM260 in complex with the native donor Dol-P-Man and a PLXNB2-IPT1-derived acceptor peptide, determined at 3.1 Å resolution. Major structural regions are indicated and colored consistently throughout the figure. The top-right panel shows a view from the ER lumen, perpendicular to the membrane, with the acceptor peptide shown as a ribbon, the T822 glycosylation site highlighted and Dol-P-Man shown as sticks. This orientation emphasizes insertion of the N terminus into the finger region and positioning of the glycosylation site within the catalytic pocket. b , Front view of the corresponding atomic model in ribbon representation. Close-up (dashed circle) highlights the Dol-P-Man density and fitted model. c , Close-up of the ER-luminal region of TMEM260 shown in surface representation and colored by electrostatic potential, with the bound peptide as a ribbon and side chains as sticks. Dol-P-Man is shown as sticks and the T822 glycosylation site is indicated. d , Same view as in c , shown in ribbon representation to highlight specific interactions between TMEM260 residues and the acceptor peptide. The T822 glycosylation site is indicated. e , Sequence alignment of the PLXNB2-IPT1 peptide with reported O-mannosylated IPT domains from plexin, cMET and RON receptors, highlighting conserved residues proposed to define a TMEM260-specific acceptor sequon. f , Close-up of the active-site environment showing superposition of Dol-P-Man in the binary complex (all in grey including Dol-P-Man) and in the ternary complex (all in color with acceptor peptide in yellow and Dol-P-Man in black) with the PLXNB2-IPT1 peptide. In the ternary complex, the β-mannose moiety undergoes an approximately 60° rotation, indicating a peptide-induced reorientation of the donor sugar.

    Article Snippet: The coding region for PLXNB2 (803-837) was amplified from pENTR223-PLXNB2 (Addgene plasmid #86236; gift from Roland Friedel; RRID:Addgene_86236) and RON (684-715) from pDONR223-MST1R (Addgene plasmid #23942; gift from William Hahn & David Root; RRID:Addgene_23942).

    Techniques: Cryo-EM Sample Prep, Derivative Assay, Membrane, Glycoproteomics, Sequencing