Review



antibody against rfp  (Proteintech)


Bioz Verified Symbol Proteintech is a verified supplier  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 96
      Buy from Supplier

    Structured Review

    Proteintech antibody against rfp
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Antibody Against Rfp, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 202 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Red+fluorescent+protein+Antibody/bio_rxiv__2025__06__04__657875-311-17-20
    Average 96 stars, based on 202 article reviews
    antibody against rfp - by Bioz Stars, 2026-10
    96/100 stars

    Images

    1) Product Images from "Direct cell-to-cell transport of Hedgehog morphogen is aided by the diffusible carrier Shifted/DmWif1"

    Article Title: Direct cell-to-cell transport of Hedgehog morphogen is aided by the diffusible carrier Shifted/DmWif1

    Journal: bioRxiv

    doi: 10.1101/2025.06.04.657875

    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: UAS.Ihog:RFP ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using an anti-RFP antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Figure Legend Snippet: A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: UAS.Ihog:RFP ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using an anti-RFP antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.

    Techniques Used: Over Expression, Mutagenesis, Control, Expressing, Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation

    Related Articles

    Incubation:

    Article Title: Nerve Injury Triggers Time-dependent Activation of the Locus Coeruleus, Influencing Spontaneous Pain-like Behavior in Rats
    Article Snippet: .. All the LC sections (30 μm) were incubated for 48 h at 4oC with an antibody against red fluorescent protein (1:500 [5F8], Chromotek, Germany) and mouse antidopamine beta hydroxylase (DBH, 1:1,000, Merck Chemicals & Life Science S.A., Spain). .. Subsequently, the antibodies were detected with a biotinylated donkey antirat antibody (1:200, Jackson ImmunoResearch Europe, United Kingdom), which was visualized with Alexa Fluor 568 streptavidin or a donkey antimouse Alexa Fluor 488 (1:1,000, Invitrogen, USA).



    Similar Products

    antibody against red fluorescence protein rfp  (Rockland Immunochemicals)
    98
    Rockland Immunochemicals antibody against red fluorescence protein rfp
    Antibody Against Red Fluorescence Protein Rfp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Anti-rfp/pmc12722035-65-8-16
    Average 98 stars, based on 1 article reviews
    antibody against red fluorescence protein rfp - by Bioz Stars, 2026-10
    98/100 stars
    		  Buy from Supplier
    antibody against rfp  (Proteintech)
    96
    Proteintech antibody against rfp
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Antibody Against Rfp, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Red+fluorescent+protein+Antibody/bio_rxiv__2025__06__04__657875-311-17-20
    Average 96 stars, based on 1 article reviews
    antibody against rfp - by Bioz Stars, 2026-10
    96/100 stars
    		  Buy from Supplier
    primary antibodies against rfp  (Proteintech)
    96
    Proteintech primary antibodies against rfp
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Primary Antibodies Against Rfp, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Red+fluorescent+protein+Antibody/pm40246179-98-10-15
    Average 96 stars, based on 1 article reviews
    primary antibodies against rfp - by Bioz Stars, 2026-10
    96/100 stars
    		  Buy from Supplier
    antibody against red fluorescent protein  (Rockland Immunochemicals)
    98
    Rockland Immunochemicals antibody against red fluorescent protein
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Antibody Against Red Fluorescent Protein, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Anti-rfp/pmc11555405-70-6-16
    Average 98 stars, based on 1 article reviews
    antibody against red fluorescent protein - by Bioz Stars, 2026-10
    98/100 stars
    		  Buy from Supplier
    antibodies against red fluorescence protein  (Proteintech)
    96
    Proteintech antibodies against red fluorescence protein
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Antibodies Against Red Fluorescence Protein, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Red+fluorescent+protein+Antibody/pm38896028-49-15-23
    Average 96 stars, based on 1 article reviews
    antibodies against red fluorescence protein - by Bioz Stars, 2026-10
    96/100 stars
    		  Buy from Supplier
    rabbit polyclonal antibodies against red fluorescent protein  (Danaher Inc)
    86
    Danaher Inc rabbit polyclonal antibodies against red fluorescent protein
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Rabbit Polyclonal Antibodies Against Red Fluorescent Protein, supplied by Danaher Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/pmc11242356-136-14-22
    Average 86 stars, based on 1 article reviews
    rabbit polyclonal antibodies against red fluorescent protein - by Bioz Stars, 2026-10
    86/100 stars
    		  Buy from Supplier
    antibody against red fluorescent protein  (Proteintech)
    96
    Proteintech antibody against red fluorescent protein
    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: <t>UAS.Ihog:RFP</t> ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using <t>an</t> <t>anti-RFP</t> antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.
    Antibody Against Red Fluorescent Protein, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antibody+against+red+fluorescent+protein/Red+fluorescent+protein+Antibody/10__1097_slash_aln__0000000000005006-125-15-22
    Average 96 stars, based on 1 article reviews
    antibody against red fluorescent protein - by Bioz Stars, 2026-10
    96/100 stars
    		  Buy from Supplier

    Image Search Results


    A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: UAS.Ihog:RFP ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using an anti-RFP antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.

    Journal: bioRxiv

    Article Title: Direct cell-to-cell transport of Hedgehog morphogen is aided by the diffusible carrier Shifted/DmWif1

    doi: 10.1101/2025.06.04.657875

    Figure Lengend Snippet: A) AlphaFold 3 model of Ihog and Shf. Ihog Ig domains (indicated) adopt a folded conformation in which Ig1-Ig4 and Ig3-Ig2 interact. This folded structure forms the surface with which Ihog interacts with Shf. Only globular domains are shown in the structural model. B) AlphaFold confidence matrix indicating the predicted aligned error of the model in A. Modeling was performed using full-length proteins. C) Detail of the interaction between Ig domains of Ihog and the EGF domains of Shf. In Blue-Orange Palette, the confidence of the interaction is measured using ChimeraX. D) Shf protein accumulation (visualised with anti-Shf antibody) induced by overexpression of different Ihog mutant forms in the dorsal compartment of wing discs using the ap.Gal4; tub.Gal80 ts driver, keeping the ventral compartment as an endogenous control: UAS.Ihog:RFP ; UAS.IhogΔFn:RFP; UAS.IhogCT:RFP ; UAS.IhogΔIg:RFP . Note that the expression of Ihog form lacking the Ig domains is unable to recruit Shf. This is not the case for the Ihog form lacking the FN domains. E) Quantifications of Shf accumulation in the dorsal compartment by the expression of the Ihog mutant forms relative to the endogenous control (ventral compartment). (F) Western blots after co-immunoprecipitation assay in salivary gland protein extract expressing Shf:V5 (53 kDa) and Ihog:RFP (135 kDa) and IhogΔIg:RFP (95 kDa) proteins using an anti-RFP antibody. The upper panel shows the immunoprecipitation of Ihog:RFP and IhogΔIg:RFP proteins visualised with an anti-RFP antibody. The lower panel shows the co-immunoprecipitation of WT Shf (Shf:V5) protein visualised with anti-V5 antibody. Note that Shf does not co-immunoprecipitate with the Ihog protein forms lacking the immunoglobulin domains.

    Article Snippet: Protein immunoprecipitation was carried out from the protein extracts using a magnetic matrix (Dyneabeads) to which an antibody against RFP (ChromoTek RFP-Trap® Magnetic Agarose) was bound.

    Techniques: Over Expression, Mutagenesis, Control, Expressing, Western Blot, Co-Immunoprecipitation Assay, Immunoprecipitation