134 amino acid peptide Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 84
    Millipore polyclonal anti zyxin
    Polyclonal Anti Zyxin, supplied by Millipore, used in various techniques. Bioz Stars score: 84/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyclonal anti zyxin/product/Millipore
    Average 84 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    polyclonal anti zyxin - by Bioz Stars, 2020-08
    84/100 stars
      Buy from Supplier

    94
    BioLegend αsyn ps129
    Human <t>αSyn</t> transduction induces synucleinopathies. (a) VenusYFP fluorescence in the striatum, venusYFP fluorescence and its colacalization with TH in the SN 8 weeks following venus or V1SSV2 injection. Arrows indicate beaded, dystrophic neurites. Scale bars: 100 μm (left), 10 μm (right). (b) VenusYFP before and after proteinase K treatment in the SN 12 weeks following V1SSV2 injection. Scale bars: 20 μm. (c) Immunohistochemistry for <t>pSer129</t> αSyn in the SN 12 weeks following V1SSV2 injection. Scale bars: 50 μm (left), 10 μm (right). (d) Accumulation of high-molecular-weight-αSyn species in the ventral midbrain and the striatum 8 weeks following V1SSV2 injection by Western blot analysis using anti-human αSyn antibody. Tissue sequential extractions were prepared using Triton X-100 and SDS.
    αsyn Ps129, supplied by BioLegend, used in various techniques. Bioz Stars score: 94/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/αsyn ps129/product/BioLegend
    Average 94 stars, based on 27 article reviews
    Price from $9.99 to $1999.99
    αsyn ps129 - by Bioz Stars, 2020-08
    94/100 stars
      Buy from Supplier

    85
    WuXi AppTec gapdhs
    Human <t>αSyn</t> transduction induces synucleinopathies. (a) VenusYFP fluorescence in the striatum, venusYFP fluorescence and its colacalization with TH in the SN 8 weeks following venus or V1SSV2 injection. Arrows indicate beaded, dystrophic neurites. Scale bars: 100 μm (left), 10 μm (right). (b) VenusYFP before and after proteinase K treatment in the SN 12 weeks following V1SSV2 injection. Scale bars: 20 μm. (c) Immunohistochemistry for <t>pSer129</t> αSyn in the SN 12 weeks following V1SSV2 injection. Scale bars: 50 μm (left), 10 μm (right). (d) Accumulation of high-molecular-weight-αSyn species in the ventral midbrain and the striatum 8 weeks following V1SSV2 injection by Western blot analysis using anti-human αSyn antibody. Tissue sequential extractions were prepared using Triton X-100 and SDS.
    Gapdhs, supplied by WuXi AppTec, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/gapdhs/product/WuXi AppTec
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    gapdhs - by Bioz Stars, 2020-08
    85/100 stars
      Buy from Supplier

    91
    Peptide 2.0 bb0173
    In vitro analysis of truncated <t>BB0173</t> constructs. To monitor the membrane orientation of truncated BB0173 molecules a glycosylatable (NSTMSM) tag (white rectangle) was added at position 56 (56mer), 162 (162mer), 278 (278 mer) and 341 (341mer). a Schematic representation of the constructs used in the assay. The position of the glycosylation sites is marked with a Y symbol. The presence of a TM segment identified by the ΔG prediction server ( http://dgpred.cbr.su.se /) in each construct and the required linker sequence preceding the glycosylatable tag to allow glycosylation is also included for 341mer truncates. b In vitro translation of the 56mer, 162mer, 278mer and 341mer truncates in the presence (+) or absence (−) of rough microsomes (RM). A white dot marks the non-glycosylated form of the protein while a black dot indicates glycosylation of the C-terminal tag. c In vitro translations in the presence or absence of RM of 162mer truncated constructs were performed bearing an acceptor (NST) or non-acceptor (QST) at N-terminal and/or C-terminal glycosylation tag. White and black dots indicate non-glycosylated and glycosylated molecules respectively, as in panel b . d Schematic representation of the membrane topology of 341mer truncates. A hydrophobic region is noted as a blue box when inserted in the membrane, or as a red box if it is not recognized by the translocon as a TM domain. The position of the glycosylatable tag (white rectangle) and its glycosylation status (white and black dots, represents non-glycosylated and glycosylated respectively) is also shown
    Bb0173, supplied by Peptide 2.0, used in various techniques. Bioz Stars score: 91/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bb0173/product/Peptide 2.0
    Average 91 stars, based on 4 article reviews
    Price from $9.99 to $1999.99
    bb0173 - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    90
    WuXi AppTec anti p21 ps146
    In vitro analysis of truncated <t>BB0173</t> constructs. To monitor the membrane orientation of truncated BB0173 molecules a glycosylatable (NSTMSM) tag (white rectangle) was added at position 56 (56mer), 162 (162mer), 278 (278 mer) and 341 (341mer). a Schematic representation of the constructs used in the assay. The position of the glycosylation sites is marked with a Y symbol. The presence of a TM segment identified by the ΔG prediction server ( http://dgpred.cbr.su.se /) in each construct and the required linker sequence preceding the glycosylatable tag to allow glycosylation is also included for 341mer truncates. b In vitro translation of the 56mer, 162mer, 278mer and 341mer truncates in the presence (+) or absence (−) of rough microsomes (RM). A white dot marks the non-glycosylated form of the protein while a black dot indicates glycosylation of the C-terminal tag. c In vitro translations in the presence or absence of RM of 162mer truncated constructs were performed bearing an acceptor (NST) or non-acceptor (QST) at N-terminal and/or C-terminal glycosylation tag. White and black dots indicate non-glycosylated and glycosylated molecules respectively, as in panel b . d Schematic representation of the membrane topology of 341mer truncates. A hydrophobic region is noted as a blue box when inserted in the membrane, or as a red box if it is not recognized by the translocon as a TM domain. The position of the glycosylatable tag (white rectangle) and its glycosylation status (white and black dots, represents non-glycosylated and glycosylated respectively) is also shown
    Anti P21 Ps146, supplied by WuXi AppTec, 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/anti p21 ps146/product/WuXi AppTec
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti p21 ps146 - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    90
    WuXi AppTec rabbit polyclonal anti blimp 1
    In vitro analysis of truncated <t>BB0173</t> constructs. To monitor the membrane orientation of truncated BB0173 molecules a glycosylatable (NSTMSM) tag (white rectangle) was added at position 56 (56mer), 162 (162mer), 278 (278 mer) and 341 (341mer). a Schematic representation of the constructs used in the assay. The position of the glycosylation sites is marked with a Y symbol. The presence of a TM segment identified by the ΔG prediction server ( http://dgpred.cbr.su.se /) in each construct and the required linker sequence preceding the glycosylatable tag to allow glycosylation is also included for 341mer truncates. b In vitro translation of the 56mer, 162mer, 278mer and 341mer truncates in the presence (+) or absence (−) of rough microsomes (RM). A white dot marks the non-glycosylated form of the protein while a black dot indicates glycosylation of the C-terminal tag. c In vitro translations in the presence or absence of RM of 162mer truncated constructs were performed bearing an acceptor (NST) or non-acceptor (QST) at N-terminal and/or C-terminal glycosylation tag. White and black dots indicate non-glycosylated and glycosylated molecules respectively, as in panel b . d Schematic representation of the membrane topology of 341mer truncates. A hydrophobic region is noted as a blue box when inserted in the membrane, or as a red box if it is not recognized by the translocon as a TM domain. The position of the glycosylatable tag (white rectangle) and its glycosylation status (white and black dots, represents non-glycosylated and glycosylated respectively) is also shown
    Rabbit Polyclonal Anti Blimp 1, supplied by WuXi AppTec, used in various techniques. Bioz Stars score: 90/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal anti blimp 1/product/WuXi AppTec
    Average 90 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal anti blimp 1 - by Bioz Stars, 2020-08
    90/100 stars
      Buy from Supplier

    92
    Biorbyt anti t2r10
    <t>T2R10</t> expression in tumor derived cell lines. A Agarose gel electrophoresis analysis of PCR products. T2R10 mRNA was determined in eight pancreatic tumor cell lines. B T2R10 expression was assessed by Western blotting the cell lines BxPC3 and PANC-1 C Flow cytometry analysis was used to detect T2R10 surface expression in BxPC-3 and PANC-1 cell lines (bold line indicates binding of anti-T2R10, dotted line is IgG isotype control).
    Anti T2r10, supplied by Biorbyt, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti t2r10/product/Biorbyt
    Average 92 stars, based on 8 article reviews
    Price from $9.99 to $1999.99
    anti t2r10 - by Bioz Stars, 2020-08
    92/100 stars
      Buy from Supplier

    91
    WuXi AppTec rabbit anti human sost
    Co-expression of <t>DKK-1</t> and <t>SOST</t> in OA trabecular bone. Representative staining of serial sections of trabecular bone in core taken from region of partial cartilage defect. a H E staining, b IgG negative staining, c, e, g SOST immunostaining, d, f, h DKK-1 immunostaining. a, b ×4 and c – f ×10, g – h ×20 magnification
    Rabbit Anti Human Sost, supplied by WuXi AppTec, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti human sost/product/WuXi AppTec
    Average 91 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    rabbit anti human sost - by Bioz Stars, 2020-08
    91/100 stars
      Buy from Supplier

    Image Search Results


    Human αSyn transduction induces synucleinopathies. (a) VenusYFP fluorescence in the striatum, venusYFP fluorescence and its colacalization with TH in the SN 8 weeks following venus or V1SSV2 injection. Arrows indicate beaded, dystrophic neurites. Scale bars: 100 μm (left), 10 μm (right). (b) VenusYFP before and after proteinase K treatment in the SN 12 weeks following V1SSV2 injection. Scale bars: 20 μm. (c) Immunohistochemistry for pSer129 αSyn in the SN 12 weeks following V1SSV2 injection. Scale bars: 50 μm (left), 10 μm (right). (d) Accumulation of high-molecular-weight-αSyn species in the ventral midbrain and the striatum 8 weeks following V1SSV2 injection by Western blot analysis using anti-human αSyn antibody. Tissue sequential extractions were prepared using Triton X-100 and SDS.

    Journal: EBioMedicine

    Article Title: Bimolecular Fluorescence Complementation of Alpha-synuclein Demonstrates its Oligomerization with Dopaminergic Phenotype in Mice

    doi: 10.1016/j.ebiom.2018.01.035

    Figure Lengend Snippet: Human αSyn transduction induces synucleinopathies. (a) VenusYFP fluorescence in the striatum, venusYFP fluorescence and its colacalization with TH in the SN 8 weeks following venus or V1SSV2 injection. Arrows indicate beaded, dystrophic neurites. Scale bars: 100 μm (left), 10 μm (right). (b) VenusYFP before and after proteinase K treatment in the SN 12 weeks following V1SSV2 injection. Scale bars: 20 μm. (c) Immunohistochemistry for pSer129 αSyn in the SN 12 weeks following V1SSV2 injection. Scale bars: 50 μm (left), 10 μm (right). (d) Accumulation of high-molecular-weight-αSyn species in the ventral midbrain and the striatum 8 weeks following V1SSV2 injection by Western blot analysis using anti-human αSyn antibody. Tissue sequential extractions were prepared using Triton X-100 and SDS.

    Article Snippet: Primary antibodies were: mouse monoclonal antibody against αSyn (Thermo Fisher Scientific Cat# AHB0261, RRID: AB_2536241 , at 1:500), mouse monoclonal antibody against pSer129-αSyn (BioLegend Cat# 825701, RRID: AB_2564891 , at 1:500), mouse monoclonal antibody against astrocytes marker glial fibrillary acidic protein (GFAP, Sigma-Aldrich Cat# G3893, RRID: AB_477010 , at 1:2500), rabbit monoclonal antibody against microglia marker ionized calcium-binding adapter molecule 1 (iba-1, Abcam Cat# ab178846, RRID: AB_2636859 , at 1:2000), and rabbit polyclonal antibody against dopaminergic neuron marker tyrosine hydroxylase (TH, Enzo Life Sciences Cat# BML-SA497-0100, RRID: AB_2052772 , at 1:1000).

    Techniques: Transduction, Fluorescence, Injection, Immunohistochemistry, Molecular Weight, Western Blot

    A53T hNs transmit mitochondrial pathology to corrected hNs. a , b Micrographs of co-cultured GFP +ve -corrected and GFP −ve -A53T-mutant hNs antigenically labeled for ubiquitin (Ubq) and PS129; scale bar: 10 μm ( a ). Enlarged regions of GFP +ve neurites and GFP −ve neurites show that both display equal Ubq/PS129 colocalization. Boolean operation was employed to label regions of colocalization in blue, scale bar: 50 μm. Quantifications of PS129 +ve neurons within the GFP +ve and GFP −ve populations ( b ). Data represent mean ± s.e.m. P = 0.8919 by t -test, 10 coverslips over 3 independent differentiations, DIV: 60. c , d Micrographs of GFP +ve -corrected and GFP −ve -A53T-mutant hNs expressing mitoDSRed and antigenically labeled for endogenous LC3. GFP +ve neurites ( i ) and GFP −ve neurites ( ii ) are enlarged and show LC3 punctate colocalizes with mitochondria. Arrows show areas where LC3 colocalizes with MitoDSRed. Boolean operation was employed to label regions of colocalization in blue, scale bar: 10 μm. d Quantification of percentage of total GFP +ve and GFP −ve hNs that have fragmented mitochondria. Data represent mean ± s.e.m. P = 0.1479 by t -test, n = 8 coverslips over 3 independent differentiations, DIV: 60. e Co-cultures were labeled with 200 nM TMRE, and mitochondrial potential (Δ Ψ m ) was measured by flow cytometry using the dequench method in GFP +ve (red trace) and GFP −ve (black trace) populations. Representative plot illustrating that GFP +ve corrected cells within co-cultures have adopted a pattern indicative of mitochondrial depolarization. Representative trace from 3 independent experiments (10,000 events per experiment), DIV: 60. f Corrected cells expressing CL-GFP and RPRE-RFP were differentiated in co-cultured with either RFP -ve /GFP −ve Corrected or RFP -ve /GFP −ve A53T hNs. Translocation of cardiolipin from the IMM to the OMM was assessed by visualizing the redistribution of RPRE-RFP from the plasma membrane to the cardiolipin-GFP +ve mitochondria. Magnified insets show CL-GFP colocalization with RPRE-RFP in Corrected hNs when differentiated in co-culture, scale bar: 10 μm. g , h Fluorescence resonance energy transfer (FRET) from CL-GFP to RPRE-RFP in hiPSC-derived A53T and corrected hNs or hESC-derived WT, A53T and E46K hNs was assessed ( g ) and mean FRET intensity was quantified ( h ). Data represent mean ± s.e.m. ** P

    Journal: Nature Communications

    Article Title: Cardiolipin exposure on the outer mitochondrial membrane modulates α-synuclein

    doi: 10.1038/s41467-018-03241-9

    Figure Lengend Snippet: A53T hNs transmit mitochondrial pathology to corrected hNs. a , b Micrographs of co-cultured GFP +ve -corrected and GFP −ve -A53T-mutant hNs antigenically labeled for ubiquitin (Ubq) and PS129; scale bar: 10 μm ( a ). Enlarged regions of GFP +ve neurites and GFP −ve neurites show that both display equal Ubq/PS129 colocalization. Boolean operation was employed to label regions of colocalization in blue, scale bar: 50 μm. Quantifications of PS129 +ve neurons within the GFP +ve and GFP −ve populations ( b ). Data represent mean ± s.e.m. P = 0.8919 by t -test, 10 coverslips over 3 independent differentiations, DIV: 60. c , d Micrographs of GFP +ve -corrected and GFP −ve -A53T-mutant hNs expressing mitoDSRed and antigenically labeled for endogenous LC3. GFP +ve neurites ( i ) and GFP −ve neurites ( ii ) are enlarged and show LC3 punctate colocalizes with mitochondria. Arrows show areas where LC3 colocalizes with MitoDSRed. Boolean operation was employed to label regions of colocalization in blue, scale bar: 10 μm. d Quantification of percentage of total GFP +ve and GFP −ve hNs that have fragmented mitochondria. Data represent mean ± s.e.m. P = 0.1479 by t -test, n = 8 coverslips over 3 independent differentiations, DIV: 60. e Co-cultures were labeled with 200 nM TMRE, and mitochondrial potential (Δ Ψ m ) was measured by flow cytometry using the dequench method in GFP +ve (red trace) and GFP −ve (black trace) populations. Representative plot illustrating that GFP +ve corrected cells within co-cultures have adopted a pattern indicative of mitochondrial depolarization. Representative trace from 3 independent experiments (10,000 events per experiment), DIV: 60. f Corrected cells expressing CL-GFP and RPRE-RFP were differentiated in co-cultured with either RFP -ve /GFP −ve Corrected or RFP -ve /GFP −ve A53T hNs. Translocation of cardiolipin from the IMM to the OMM was assessed by visualizing the redistribution of RPRE-RFP from the plasma membrane to the cardiolipin-GFP +ve mitochondria. Magnified insets show CL-GFP colocalization with RPRE-RFP in Corrected hNs when differentiated in co-culture, scale bar: 10 μm. g , h Fluorescence resonance energy transfer (FRET) from CL-GFP to RPRE-RFP in hiPSC-derived A53T and corrected hNs or hESC-derived WT, A53T and E46K hNs was assessed ( g ) and mean FRET intensity was quantified ( h ). Data represent mean ± s.e.m. ** P

    Article Snippet: Phosphoserine 129 (81A) (1:1000) LC3 (1:500), beta-III-Tubulin and Ubiquitin (1:500) were purchased from BioLegend (Cat. no. 825701, 827101, 801202, 840501), while total α-synuclein (1:500) was from BD Biosciences (Cat. no. 610787).

    Techniques: Cell Culture, Mutagenesis, Labeling, Expressing, Flow Cytometry, Cytometry, Translocation Assay, Co-Culture Assay, Fluorescence, Förster Resonance Energy Transfer, Derivative Assay

    α-Syn mutant hNs acquire early signs of α-syn pathology. a , b Accumulation of insoluble Ubq/α-syn PS129 protein in hiPSC-derived A53T and corrected hNs ( a ) or hESC-derived WT, A53T and E46K hNs ( b ) was determined by TX-100 wash-out of soluble protein prior to fixation. DIV: 60. Scale bar: 10 µm. c , d Fluorescence resonance energy transfer (FRET) from Alexa-488-labeled ubiquitin to Alexa-594-labeled α-syn PS129 in hiPSC-derived A53T and corrected hNs or hESC-derived WT, A53T and E46K hNs was assessed and mean FRET intensity was quantified ( d ). Data represent mean ± s.e.m. ** P

    Journal: Nature Communications

    Article Title: Cardiolipin exposure on the outer mitochondrial membrane modulates α-synuclein

    doi: 10.1038/s41467-018-03241-9

    Figure Lengend Snippet: α-Syn mutant hNs acquire early signs of α-syn pathology. a , b Accumulation of insoluble Ubq/α-syn PS129 protein in hiPSC-derived A53T and corrected hNs ( a ) or hESC-derived WT, A53T and E46K hNs ( b ) was determined by TX-100 wash-out of soluble protein prior to fixation. DIV: 60. Scale bar: 10 µm. c , d Fluorescence resonance energy transfer (FRET) from Alexa-488-labeled ubiquitin to Alexa-594-labeled α-syn PS129 in hiPSC-derived A53T and corrected hNs or hESC-derived WT, A53T and E46K hNs was assessed and mean FRET intensity was quantified ( d ). Data represent mean ± s.e.m. ** P

    Article Snippet: Phosphoserine 129 (81A) (1:1000) LC3 (1:500), beta-III-Tubulin and Ubiquitin (1:500) were purchased from BioLegend (Cat. no. 825701, 827101, 801202, 840501), while total α-synuclein (1:500) was from BD Biosciences (Cat. no. 610787).

    Techniques: Mutagenesis, Derivative Assay, Fluorescence, Förster Resonance Energy Transfer, Labeling

    In vitro analysis of truncated BB0173 constructs. To monitor the membrane orientation of truncated BB0173 molecules a glycosylatable (NSTMSM) tag (white rectangle) was added at position 56 (56mer), 162 (162mer), 278 (278 mer) and 341 (341mer). a Schematic representation of the constructs used in the assay. The position of the glycosylation sites is marked with a Y symbol. The presence of a TM segment identified by the ΔG prediction server ( http://dgpred.cbr.su.se /) in each construct and the required linker sequence preceding the glycosylatable tag to allow glycosylation is also included for 341mer truncates. b In vitro translation of the 56mer, 162mer, 278mer and 341mer truncates in the presence (+) or absence (−) of rough microsomes (RM). A white dot marks the non-glycosylated form of the protein while a black dot indicates glycosylation of the C-terminal tag. c In vitro translations in the presence or absence of RM of 162mer truncated constructs were performed bearing an acceptor (NST) or non-acceptor (QST) at N-terminal and/or C-terminal glycosylation tag. White and black dots indicate non-glycosylated and glycosylated molecules respectively, as in panel b . d Schematic representation of the membrane topology of 341mer truncates. A hydrophobic region is noted as a blue box when inserted in the membrane, or as a red box if it is not recognized by the translocon as a TM domain. The position of the glycosylatable tag (white rectangle) and its glycosylation status (white and black dots, represents non-glycosylated and glycosylated respectively) is also shown

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: In vitro analysis of truncated BB0173 constructs. To monitor the membrane orientation of truncated BB0173 molecules a glycosylatable (NSTMSM) tag (white rectangle) was added at position 56 (56mer), 162 (162mer), 278 (278 mer) and 341 (341mer). a Schematic representation of the constructs used in the assay. The position of the glycosylation sites is marked with a Y symbol. The presence of a TM segment identified by the ΔG prediction server ( http://dgpred.cbr.su.se /) in each construct and the required linker sequence preceding the glycosylatable tag to allow glycosylation is also included for 341mer truncates. b In vitro translation of the 56mer, 162mer, 278mer and 341mer truncates in the presence (+) or absence (−) of rough microsomes (RM). A white dot marks the non-glycosylated form of the protein while a black dot indicates glycosylation of the C-terminal tag. c In vitro translations in the presence or absence of RM of 162mer truncated constructs were performed bearing an acceptor (NST) or non-acceptor (QST) at N-terminal and/or C-terminal glycosylation tag. White and black dots indicate non-glycosylated and glycosylated molecules respectively, as in panel b . d Schematic representation of the membrane topology of 341mer truncates. A hydrophobic region is noted as a blue box when inserted in the membrane, or as a red box if it is not recognized by the translocon as a TM domain. The position of the glycosylatable tag (white rectangle) and its glycosylation status (white and black dots, represents non-glycosylated and glycosylated respectively) is also shown

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: In Vitro, Construct, Sequencing

    Localization of the tertiary structures of BB0172 and BB0173 within B. burgdorferi . Models of the tertiary structures of BB0172 and BB0173 were generated and superimposed onto either the inner or outer membrane as predicted from localization studies

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Localization of the tertiary structures of BB0172 and BB0173 within B. burgdorferi . Models of the tertiary structures of BB0172 and BB0173 were generated and superimposed onto either the inner or outer membrane as predicted from localization studies

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Generated

    Localization of BB0173 to the aqueous and inner membrane fractions after treatment with detergent. B. burgdorferi cells disrupted using the detergent Triton X-114 separated into three distinct fractions, the aqueous (AQ), protoplasmic cylinders (PC), and detergent (DT) phases. The phases were separated using SDS-12% PAGE and either stained using Silver Stain Plus (Biorad, Hercules, CA) ( a ) or were transferred to a PVDF membrane and probed using anti-BB0173 T and a secondary anti-chicken HRP-conjugated antibody Lane 1 is B. burgdorferi whole cell lysate. Lane 2 is AQ, Lane 3 is PC, and Lane 4 is DT ( b ). Controls for outer membrane and inner membrane proteins were OspC and FlaB

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Localization of BB0173 to the aqueous and inner membrane fractions after treatment with detergent. B. burgdorferi cells disrupted using the detergent Triton X-114 separated into three distinct fractions, the aqueous (AQ), protoplasmic cylinders (PC), and detergent (DT) phases. The phases were separated using SDS-12% PAGE and either stained using Silver Stain Plus (Biorad, Hercules, CA) ( a ) or were transferred to a PVDF membrane and probed using anti-BB0173 T and a secondary anti-chicken HRP-conjugated antibody Lane 1 is B. burgdorferi whole cell lysate. Lane 2 is AQ, Lane 3 is PC, and Lane 4 is DT ( b ). Controls for outer membrane and inner membrane proteins were OspC and FlaB

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Polyacrylamide Gel Electrophoresis, Staining, Silver Staining

    Protection of BB0173 from protease degradation. Surface proteins of B. burgdorferi are degraded by serine protease Proteinase K (PK). Whole cell lysates were treated with doses ranging from 0 to 200 μg/mL PK prior to separation using SDS-12% PAGE. Gels were either visualized using Coomassie blue staining ( a ) or transferred to a PVDF membrane and probed with antibodies ( b ). BB0173 was detected using anti-BB0173 pep and anti-chicken HRP-conjugated antibody. Controls for PK mediated degradation and cell integrity during treatment included intercellular protein BosR and periplasmic protein FlaB, as well as outer membrane proteins OspC, VlsE, and P66

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Protection of BB0173 from protease degradation. Surface proteins of B. burgdorferi are degraded by serine protease Proteinase K (PK). Whole cell lysates were treated with doses ranging from 0 to 200 μg/mL PK prior to separation using SDS-12% PAGE. Gels were either visualized using Coomassie blue staining ( a ) or transferred to a PVDF membrane and probed with antibodies ( b ). BB0173 was detected using anti-BB0173 pep and anti-chicken HRP-conjugated antibody. Controls for PK mediated degradation and cell integrity during treatment included intercellular protein BosR and periplasmic protein FlaB, as well as outer membrane proteins OspC, VlsE, and P66

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Polyacrylamide Gel Electrophoresis, Staining

    Organization and conservation of bb0173 . a Schematic demonstrating the similarity between the Bat region of Borrelia burgdorferi (BB), Borrelia hermsii (BH), Leptospira interrogans (LB), Leptospira biflexa (LBF), and Bacteroides fragilis (BF). Note the similarities across BB0172 through BB0176. b Map demonstrating the pertinent domains of BB0173. The map demonstrates the three transmembrane domains (amino acids: 7–25, 57–77, 310–328), VWFA domain (amino acids: 87–328), MIDAS motif (amino acids: 99–103), BatA domain (amino acids: 9–86), and N-glycosylation sites (amino acids 170–172, 265–267). Additionally, a 30-mer peptide is denoted, BB0173 pep , which was used to generate chicken anti-BB0173 antibodies. BB0173 T , the truncated BB0173 protein, was also used to generate chicken anti-BB0173 antibodies. c Clustal W (v1.83) alignment of B. burgdorferi B31 BB0173 (bold) against homologues in B. burgdorferi ZS7 (BB0173 BbZS7) Borrelia garinii (BG0172), Borrelia afzelii (BAPKO_0175), and the relapsing fever species Borrelia hermsii (BH0173) and Borrelia turicatae (BT0173). Alignments are also made to B. burgdorferi B31 BB0172 (BB0172 B31), which was found to be very similar in sequence and topology. There is also homology seen to Plasmodium falciparum membrane protein TRAP (Pf TRAP) as well as to the human adhesins LFA-1 (hLFA-1) and CD11b (hCD11b). Conserved residues corresponding to the MIDAS motif are highlighted, including the DXSXS as well as the threonine (T) required for MIDAS function

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Organization and conservation of bb0173 . a Schematic demonstrating the similarity between the Bat region of Borrelia burgdorferi (BB), Borrelia hermsii (BH), Leptospira interrogans (LB), Leptospira biflexa (LBF), and Bacteroides fragilis (BF). Note the similarities across BB0172 through BB0176. b Map demonstrating the pertinent domains of BB0173. The map demonstrates the three transmembrane domains (amino acids: 7–25, 57–77, 310–328), VWFA domain (amino acids: 87–328), MIDAS motif (amino acids: 99–103), BatA domain (amino acids: 9–86), and N-glycosylation sites (amino acids 170–172, 265–267). Additionally, a 30-mer peptide is denoted, BB0173 pep , which was used to generate chicken anti-BB0173 antibodies. BB0173 T , the truncated BB0173 protein, was also used to generate chicken anti-BB0173 antibodies. c Clustal W (v1.83) alignment of B. burgdorferi B31 BB0173 (bold) against homologues in B. burgdorferi ZS7 (BB0173 BbZS7) Borrelia garinii (BG0172), Borrelia afzelii (BAPKO_0175), and the relapsing fever species Borrelia hermsii (BH0173) and Borrelia turicatae (BT0173). Alignments are also made to B. burgdorferi B31 BB0172 (BB0172 B31), which was found to be very similar in sequence and topology. There is also homology seen to Plasmodium falciparum membrane protein TRAP (Pf TRAP) as well as to the human adhesins LFA-1 (hLFA-1) and CD11b (hCD11b). Conserved residues corresponding to the MIDAS motif are highlighted, including the DXSXS as well as the threonine (T) required for MIDAS function

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Sequencing

    Expression of bb0173 cDNA upon temperature shift. B. burgdorferi B31A3 strain was grown under unfed tick conditions (RT/pH 7.6) to late log phase then shifted to fed tick conditions (37 °C/pH 6.8) before collection of mRNA. The purified mRNA was reverse transcribed to cDNA, and PCR was performed to detect bb0173, flaB, p66 , and ospC. Water was used as a negative control (−). a RNA samples were tested for DNA contamination in lanes 3 and 6. Genomic DNA was run in lanes 2 and 5 and served as the positive control. In lanes 1 and 4, cDNA samples were loaded. To confirm functionality of primers, a second genomic DNA sample was applied in lane 7. b The same shifting conditions were used to generate DNA samples as previously. cDNA samples are in lanes 1 and 3, RNA in lanes 2 and 4, and genomic DNA is labeled as (+). Negative control is water, as above. On the left of the figure, the DNA ladder is shown and sizes are denoted in basepairs

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Expression of bb0173 cDNA upon temperature shift. B. burgdorferi B31A3 strain was grown under unfed tick conditions (RT/pH 7.6) to late log phase then shifted to fed tick conditions (37 °C/pH 6.8) before collection of mRNA. The purified mRNA was reverse transcribed to cDNA, and PCR was performed to detect bb0173, flaB, p66 , and ospC. Water was used as a negative control (−). a RNA samples were tested for DNA contamination in lanes 3 and 6. Genomic DNA was run in lanes 2 and 5 and served as the positive control. In lanes 1 and 4, cDNA samples were loaded. To confirm functionality of primers, a second genomic DNA sample was applied in lane 7. b The same shifting conditions were used to generate DNA samples as previously. cDNA samples are in lanes 1 and 3, RNA in lanes 2 and 4, and genomic DNA is labeled as (+). Negative control is water, as above. On the left of the figure, the DNA ladder is shown and sizes are denoted in basepairs

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Expressing, Purification, Polymerase Chain Reaction, Negative Control, Positive Control, Labeling

    Insertion of hydrophobic regions of BB0173 into membranes using Lep as model protein. a The HR sequence in each construct is shown together with the predicted G apparent value, which was estimated using the ∆G prediction algorithm available on the Internet ( http://dgpred.cbr.su.se/) . Glycosylation acceptor site is shown in bold. b Schematic representation of the Lep construct used to report insertion of hydrophobic regions of BB0173 into endoplasmic reticulum membranes. The TM segment under investigation (HR-tested) was introduced into the P2 domain of Lep, flanked by two artificial glycosylation acceptor sites (G1 and G2). Recognition of the tested sequence as a TM domain by the translocon machinery results in the location of only G1 in the luminal side of the ER membrane, preventing G2 glycosylation (left). The Lep chimera will be doubly glycosylated when the sequence being tested is translocated into the lumen of the microsomes (right). c In vitro translation in the presence of membranes of the different Lep constructs. Constructs containing HR1 (residues 7 to 25; lanes 1–3), HR2 (residues 55 to 77; lanes 4–6), HR3 (residues 163 to 185; lanes 7–9) and HR4 (residues 310 to 328; lines 10–12) were translated in the presence (+) and absence (−) of rough microsomes (RM) and proteinase K (PK). Bands of non- glycosylated proteins are indicated by a white dot; singly and doubly glycosylated proteins are indicated by one and two black dots, respectively. In the case of Lep-HR3 construct a triply glycosylated band was observed (lane 8) due to the presence of an acceptor NGS site (residues 169–171) within the (translocated) hydrophobic region. The protected doubly-glycosylated H2/HR3/P2 fragment is indicated by an arrowhead. Control HRs were used to verify sequence translocation (translocated; lanes 13–15)

    Journal: BMC Microbiology

    Article Title: Characterization of the inner membrane protein BB0173 from Borrelia burgdorferi

    doi: 10.1186/s12866-017-1127-y

    Figure Lengend Snippet: Insertion of hydrophobic regions of BB0173 into membranes using Lep as model protein. a The HR sequence in each construct is shown together with the predicted G apparent value, which was estimated using the ∆G prediction algorithm available on the Internet ( http://dgpred.cbr.su.se/) . Glycosylation acceptor site is shown in bold. b Schematic representation of the Lep construct used to report insertion of hydrophobic regions of BB0173 into endoplasmic reticulum membranes. The TM segment under investigation (HR-tested) was introduced into the P2 domain of Lep, flanked by two artificial glycosylation acceptor sites (G1 and G2). Recognition of the tested sequence as a TM domain by the translocon machinery results in the location of only G1 in the luminal side of the ER membrane, preventing G2 glycosylation (left). The Lep chimera will be doubly glycosylated when the sequence being tested is translocated into the lumen of the microsomes (right). c In vitro translation in the presence of membranes of the different Lep constructs. Constructs containing HR1 (residues 7 to 25; lanes 1–3), HR2 (residues 55 to 77; lanes 4–6), HR3 (residues 163 to 185; lanes 7–9) and HR4 (residues 310 to 328; lines 10–12) were translated in the presence (+) and absence (−) of rough microsomes (RM) and proteinase K (PK). Bands of non- glycosylated proteins are indicated by a white dot; singly and doubly glycosylated proteins are indicated by one and two black dots, respectively. In the case of Lep-HR3 construct a triply glycosylated band was observed (lane 8) due to the presence of an acceptor NGS site (residues 169–171) within the (translocated) hydrophobic region. The protected doubly-glycosylated H2/HR3/P2 fragment is indicated by an arrowhead. Control HRs were used to verify sequence translocation (translocated; lanes 13–15)

    Article Snippet: A 30-amino acid peptide derived from BB0173 (BB0173pep , amino acids 105–134) was generated (Peptide 2.0 Inc., Chantilly, VA) from the region found within the large loop predicted to contain the VWFA domain and just beyond the predicted Metal Ion Dependent Adhesion Site (MIDAS) motif (Fig. ).

    Techniques: Sequencing, Construct, In Vitro, Next-Generation Sequencing, Translocation Assay

    T2R10 expression in tumor derived cell lines. A Agarose gel electrophoresis analysis of PCR products. T2R10 mRNA was determined in eight pancreatic tumor cell lines. B T2R10 expression was assessed by Western blotting the cell lines BxPC3 and PANC-1 C Flow cytometry analysis was used to detect T2R10 surface expression in BxPC-3 and PANC-1 cell lines (bold line indicates binding of anti-T2R10, dotted line is IgG isotype control).

    Journal: Journal of Cancer

    Article Title: Overcoming chemoresistance in pancreatic cancer cells: role of the bitter taste receptor T2R10

    doi: 10.7150/jca.21803

    Figure Lengend Snippet: T2R10 expression in tumor derived cell lines. A Agarose gel electrophoresis analysis of PCR products. T2R10 mRNA was determined in eight pancreatic tumor cell lines. B T2R10 expression was assessed by Western blotting the cell lines BxPC3 and PANC-1 C Flow cytometry analysis was used to detect T2R10 surface expression in BxPC-3 and PANC-1 cell lines (bold line indicates binding of anti-T2R10, dotted line is IgG isotype control).

    Article Snippet: For Western blot analysis the following antibodies were used: anti-ABCG2 (EPR2099, abcam); anti-Phospho-Akt Ser473 (D9E, Cell Signaling, Cambridge, UK), anti-pan-Akt (C67E7, Cell Signaling); anti-GAPDH (14C10, Cell signaling); anti-T2R10 (orb 164582; Biorbyt, Cambridge, UK); anti-tubulin (sc-58886, Santa Cruz); goat anti-rabbit IgG-horse radish peroxidase (HRP; Santa Cruz) as secondary antibody.

    Techniques: Expressing, Derivative Assay, Agarose Gel Electrophoresis, Polymerase Chain Reaction, Western Blot, Flow Cytometry, Cytometry, Binding Assay

    siRNA knockdown of T2R10. Flow cytometry analysis was used to determine surface expression of T2R10 in BxPC-3 (A) and PANC-1 cells (C) transfected with either scrambled siRNA (blue line) or siRNA targeted against T2R10 (red line). Thick lines represent antibody binding to T2R10 and dotted lines isotype control. B,D Quantification of the mean fluorescence intensity (MFI) indicates a reduction of T2R10 expression in BxPC-3 and PANC-1 (three independent experiments are shown; MFI for cells treated with scrambled siRNA was set as 100%). E Western blot analysis confirmed silencing of T2R10 on protein level

    Journal: Journal of Cancer

    Article Title: Overcoming chemoresistance in pancreatic cancer cells: role of the bitter taste receptor T2R10

    doi: 10.7150/jca.21803

    Figure Lengend Snippet: siRNA knockdown of T2R10. Flow cytometry analysis was used to determine surface expression of T2R10 in BxPC-3 (A) and PANC-1 cells (C) transfected with either scrambled siRNA (blue line) or siRNA targeted against T2R10 (red line). Thick lines represent antibody binding to T2R10 and dotted lines isotype control. B,D Quantification of the mean fluorescence intensity (MFI) indicates a reduction of T2R10 expression in BxPC-3 and PANC-1 (three independent experiments are shown; MFI for cells treated with scrambled siRNA was set as 100%). E Western blot analysis confirmed silencing of T2R10 on protein level

    Article Snippet: For Western blot analysis the following antibodies were used: anti-ABCG2 (EPR2099, abcam); anti-Phospho-Akt Ser473 (D9E, Cell Signaling, Cambridge, UK), anti-pan-Akt (C67E7, Cell Signaling); anti-GAPDH (14C10, Cell signaling); anti-T2R10 (orb 164582; Biorbyt, Cambridge, UK); anti-tubulin (sc-58886, Santa Cruz); goat anti-rabbit IgG-horse radish peroxidase (HRP; Santa Cruz) as secondary antibody.

    Techniques: Flow Cytometry, Cytometry, Expressing, Transfection, Binding Assay, Fluorescence, Western Blot

    Caffeine inhibits Akt-phosphorylation. A and 1C. Akt activation was measured as ratio between phosphorylated Akt (pAkt) and total Akt. A and E show Western blots and B and F the respective quantification (summary of three experiments). C and G show Western blots of cells silenced for expression of T2R10 (T2R10 siRNA) or for comparison cells treated with scrambled siRNA, all cultivated either in the presence of absence of caffeine. D and H show the respective quantification data (summary of three experiments as indicated by the different symbols (statistical differences between the groups were calculated by ANOVA).

    Journal: Journal of Cancer

    Article Title: Overcoming chemoresistance in pancreatic cancer cells: role of the bitter taste receptor T2R10

    doi: 10.7150/jca.21803

    Figure Lengend Snippet: Caffeine inhibits Akt-phosphorylation. A and 1C. Akt activation was measured as ratio between phosphorylated Akt (pAkt) and total Akt. A and E show Western blots and B and F the respective quantification (summary of three experiments). C and G show Western blots of cells silenced for expression of T2R10 (T2R10 siRNA) or for comparison cells treated with scrambled siRNA, all cultivated either in the presence of absence of caffeine. D and H show the respective quantification data (summary of three experiments as indicated by the different symbols (statistical differences between the groups were calculated by ANOVA).

    Article Snippet: For Western blot analysis the following antibodies were used: anti-ABCG2 (EPR2099, abcam); anti-Phospho-Akt Ser473 (D9E, Cell Signaling, Cambridge, UK), anti-pan-Akt (C67E7, Cell Signaling); anti-GAPDH (14C10, Cell signaling); anti-T2R10 (orb 164582; Biorbyt, Cambridge, UK); anti-tubulin (sc-58886, Santa Cruz); goat anti-rabbit IgG-horse radish peroxidase (HRP; Santa Cruz) as secondary antibody.

    Techniques: Activation Assay, Western Blot, Expressing

    T2R10 expression in PDAC tissue. A RNA Sequencing data showing T2R10 transcripts in PDAC tumor samples of 84 patients (Data are presented as quantified transcript levels in reads per kilobase of exon model per million mapped reads (rpkm). B Representative tissue specimen of PDAC tumors from three patients (upper panel) and of normal pancreas. T2R10 was detected in tumor cells (arrowheads) and immune cells (arrows). High magnification (upper panel, right) shows expression of T2R10 on the cell membrane and in the cytoplasm (asterisk). C Tumor samples (n=62) were categorized according to their T2R10 expression using an immunoreactivity score; negative= score 0, low= score 2-3, medium= score 4-6, high= score 7-8. D Kaplan-Meier survival analysis of PDAC patients with T2R10 negative (n=8) and T2R10 positive PDAC tumors (n=38) E Infiltrated T cells, identified by expression of CD3 are shown; F Inflammation severity scores (0-3) and activity scores (0-2) were related to T2R10 expression, the latter quantified using Allred score. The groups did not differ from each other.

    Journal: Journal of Cancer

    Article Title: Overcoming chemoresistance in pancreatic cancer cells: role of the bitter taste receptor T2R10

    doi: 10.7150/jca.21803

    Figure Lengend Snippet: T2R10 expression in PDAC tissue. A RNA Sequencing data showing T2R10 transcripts in PDAC tumor samples of 84 patients (Data are presented as quantified transcript levels in reads per kilobase of exon model per million mapped reads (rpkm). B Representative tissue specimen of PDAC tumors from three patients (upper panel) and of normal pancreas. T2R10 was detected in tumor cells (arrowheads) and immune cells (arrows). High magnification (upper panel, right) shows expression of T2R10 on the cell membrane and in the cytoplasm (asterisk). C Tumor samples (n=62) were categorized according to their T2R10 expression using an immunoreactivity score; negative= score 0, low= score 2-3, medium= score 4-6, high= score 7-8. D Kaplan-Meier survival analysis of PDAC patients with T2R10 negative (n=8) and T2R10 positive PDAC tumors (n=38) E Infiltrated T cells, identified by expression of CD3 are shown; F Inflammation severity scores (0-3) and activity scores (0-2) were related to T2R10 expression, the latter quantified using Allred score. The groups did not differ from each other.

    Article Snippet: For Western blot analysis the following antibodies were used: anti-ABCG2 (EPR2099, abcam); anti-Phospho-Akt Ser473 (D9E, Cell Signaling, Cambridge, UK), anti-pan-Akt (C67E7, Cell Signaling); anti-GAPDH (14C10, Cell signaling); anti-T2R10 (orb 164582; Biorbyt, Cambridge, UK); anti-tubulin (sc-58886, Santa Cruz); goat anti-rabbit IgG-horse radish peroxidase (HRP; Santa Cruz) as secondary antibody.

    Techniques: Expressing, RNA Sequencing Assay, Activity Assay

    Co-expression of DKK-1 and SOST in OA trabecular bone. Representative staining of serial sections of trabecular bone in core taken from region of partial cartilage defect. a H E staining, b IgG negative staining, c, e, g SOST immunostaining, d, f, h DKK-1 immunostaining. a, b ×4 and c – f ×10, g – h ×20 magnification

    Journal: Calcified Tissue International

    Article Title: Co-expression of DKK-1 and Sclerostin in Subchondral Bone of the Proximal Femoral Heads from Osteoarthritic Hips

    doi: 10.1007/s00223-017-0246-7

    Figure Lengend Snippet: Co-expression of DKK-1 and SOST in OA trabecular bone. Representative staining of serial sections of trabecular bone in core taken from region of partial cartilage defect. a H E staining, b IgG negative staining, c, e, g SOST immunostaining, d, f, h DKK-1 immunostaining. a, b ×4 and c – f ×10, g – h ×20 magnification

    Article Snippet: Representative slides were incubated overnight at 4 °C with rabbit anti-human DKK-1 (Sigma-Aldrich), rabbit anti-human SOST (ABGENT, USA) antibodies (1:200 dilution).

    Techniques: Expressing, Staining, Negative Staining, Immunostaining