Structured Review

Santa Cruz Biotechnology sc 13139
Sc 13139, supplied by Santa Cruz Biotechnology, 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/result/sc 13139/product/Santa Cruz Biotechnology
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
sc 13139 - by Bioz Stars, 2024-07
86/100 stars

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Structured Review

Santa Cruz Biotechnology wasp
a Representative western blot of WIP, <t>N-WASP</t> <t>and</t> <t>Nck</t> expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.
Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wasp/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
wasp - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "WIP Regulates Persistence of Cell Migration and Ruffle Formation in Both Mesenchymal and Amoeboid Modes of Motility"

Article Title: WIP Regulates Persistence of Cell Migration and Ruffle Formation in Both Mesenchymal and Amoeboid Modes of Motility

Journal: PLoS ONE

doi: 10.1371/journal.pone.0070364

a Representative western blot of WIP, N-WASP and Nck expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.
Figure Legend Snippet: a Representative western blot of WIP, N-WASP and Nck expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.

Techniques Used: Western Blot, Expressing, Derivative Assay, Labeling

a WIP −/− primary murine fibroblasts were transduced with recombinant lentivirus coding for GFP, WIP-GFP, WIPΔNBD-GFP (missing the Nck binding domain) or WIPΔWBD-GFP (missing the N-WASP binding site). Soluble protein extracts were subjected to western blot analysis, using anti-GFP as probe, and developed with ECL detection kit. b Transduced WIP −/− murine fibroblasts were serum starved and stimulated with PDGF-AA for increasing times (8 and 15 min). Fixed and permeabilised cells were stained with anti-cortactin and FITC-secondary antibody and imaged in a Zeiss microscope. The percentage of GFP-positive cells forming dorsal ruffles after PDGF-AA stimulation is plotted against incubation times. One way ANOVA test and Test of Tukey * p<0,05; ** p<0,001.
Figure Legend Snippet: a WIP −/− primary murine fibroblasts were transduced with recombinant lentivirus coding for GFP, WIP-GFP, WIPΔNBD-GFP (missing the Nck binding domain) or WIPΔWBD-GFP (missing the N-WASP binding site). Soluble protein extracts were subjected to western blot analysis, using anti-GFP as probe, and developed with ECL detection kit. b Transduced WIP −/− murine fibroblasts were serum starved and stimulated with PDGF-AA for increasing times (8 and 15 min). Fixed and permeabilised cells were stained with anti-cortactin and FITC-secondary antibody and imaged in a Zeiss microscope. The percentage of GFP-positive cells forming dorsal ruffles after PDGF-AA stimulation is plotted against incubation times. One way ANOVA test and Test of Tukey * p<0,05; ** p<0,001.

Techniques Used: Transduction, Recombinant, Binding Assay, Western Blot, Staining, Microscopy, Incubation


Structured Review

Santa Cruz Biotechnology wasp
PBMC of the younger brother (patient 2) were stained intracellularly <t>with</t> <t>B9</t> monoclonal antibody to <t>WASP</t> and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wasp/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
wasp - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome"

Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

Journal: PLoS ONE

doi: 10.1371/journal.pone.0003444

PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
Figure Legend Snippet: PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.

Techniques Used: Staining, Marker

(A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).
Figure Legend Snippet: (A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).

Techniques Used: Mutagenesis, Binding Assay, Staining, Marker

Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.
Figure Legend Snippet: Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.

Techniques Used: Transformation Assay, Expressing, Flow Cytometry, Staining, Amplification, Western Blot


Structured Review

Santa Cruz Biotechnology wasp
PBMC of the younger brother (patient 2) were stained intracellularly <t>with</t> <t>B9</t> monoclonal antibody to <t>WASP</t> and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wasp/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
wasp - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome"

Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

Journal: PLoS ONE

doi: 10.1371/journal.pone.0003444

PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
Figure Legend Snippet: PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.

Techniques Used: Staining, Marker

(A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).
Figure Legend Snippet: (A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).

Techniques Used: Mutagenesis, Binding Assay, Staining, Marker

Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.
Figure Legend Snippet: Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.

Techniques Used: Transformation Assay, Expressing, Flow Cytometry, Staining, Amplification, Western Blot


Structured Review

Santa Cruz Biotechnology b9 anti wasp monoclonal antibody
PBMC of the younger brother (patient 2) were stained intracellularly with <t>B9</t> monoclonal antibody to <t>WASP</t> and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
B9 Anti Wasp Monoclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/b9 anti wasp monoclonal antibody/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
b9 anti wasp monoclonal antibody - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome"

Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

Journal: PLoS ONE

doi: 10.1371/journal.pone.0003444

PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
Figure Legend Snippet: PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.

Techniques Used: Staining, Marker

(A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).
Figure Legend Snippet: (A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).

Techniques Used: Mutagenesis, Binding Assay, Staining, Marker

Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.
Figure Legend Snippet: Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.

Techniques Used: Transformation Assay, Expressing, Flow Cytometry, Staining, Amplification, Western Blot


Structured Review

Santa Cruz Biotechnology wasp
Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wasp/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
wasp - by Bioz Stars, 2024-07
93/100 stars

Images


Structured Review

Santa Cruz Biotechnology wasp
Immunoblotting analysis of the levels of transduced proteins in osteoclasts with HA-antibody . Osteoclasts were transduced with the <t>WASP</t> peptides as shown below the figures. Osteoclast lysates (~200 μg) were immunoblotted with an antibody to HA to determine the levels of transduced proteins (Top panel). The immunoblot shown in the top panel was stripped and blotted with a GAPDH antibody for normalization (bottom panel). The results shown are representative of three independent experiments.
Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/wasp/product/Santa Cruz Biotechnology
Average 93 stars, based on 1 article reviews
Price from $9.99 to $1999.99
wasp - by Bioz Stars, 2024-07
93/100 stars

Images

1) Product Images from "Dramatic inhibition of osteoclast sealing ring formation and bone resorption in vitro by a WASP-peptide containing pTyr294 amino acid"

Article Title: Dramatic inhibition of osteoclast sealing ring formation and bone resorption in vitro by a WASP-peptide containing pTyr294 amino acid

Journal: Journal of Molecular Signaling

doi: 10.1186/1750-2187-3-4

Immunoblotting analysis of the levels of transduced proteins in osteoclasts with HA-antibody . Osteoclasts were transduced with the WASP peptides as shown below the figures. Osteoclast lysates (~200 μg) were immunoblotted with an antibody to HA to determine the levels of transduced proteins (Top panel). The immunoblot shown in the top panel was stripped and blotted with a GAPDH antibody for normalization (bottom panel). The results shown are representative of three independent experiments.
Figure Legend Snippet: Immunoblotting analysis of the levels of transduced proteins in osteoclasts with HA-antibody . Osteoclasts were transduced with the WASP peptides as shown below the figures. Osteoclast lysates (~200 μg) were immunoblotted with an antibody to HA to determine the levels of transduced proteins (Top panel). The immunoblot shown in the top panel was stripped and blotted with a GAPDH antibody for normalization (bottom panel). The results shown are representative of three independent experiments.

Techniques Used: Western Blot, Transduction

Analysis of the interaction of Arp2 with the endogenous WASP and transduced peptides . Osteoclasts were transduced with the WASP peptides as shown below the figures. Lysates were immunoprecipitated with a WASP (A and B) or HA (C and D) antibody. A and B: WASP immunoprecipitates were first immunoblotted with an antibody to Arp2 (A) and subsequently stripped and blotted with an antibody to WASP (B). C and D: HA-immunoprecipitates were divided into two halves; one half was immunoblotted with an Arp 2 antibody (C) and the other half was subjected to 8% (D, lane 1) and 15% (D, lanes 2–5) SDS-PAGE. Immunoblotting was performed with a HA-antibody (D) to detect the levels of transduced proteins immunoprecipitated in each lane. Immunoprecipitation with a nonimmune serum is shown in lane 6 (A-D). The results represent one of three experiments performed from three separate osteoclast preparations.
Figure Legend Snippet: Analysis of the interaction of Arp2 with the endogenous WASP and transduced peptides . Osteoclasts were transduced with the WASP peptides as shown below the figures. Lysates were immunoprecipitated with a WASP (A and B) or HA (C and D) antibody. A and B: WASP immunoprecipitates were first immunoblotted with an antibody to Arp2 (A) and subsequently stripped and blotted with an antibody to WASP (B). C and D: HA-immunoprecipitates were divided into two halves; one half was immunoblotted with an Arp 2 antibody (C) and the other half was subjected to 8% (D, lane 1) and 15% (D, lanes 2–5) SDS-PAGE. Immunoblotting was performed with a HA-antibody (D) to detect the levels of transduced proteins immunoprecipitated in each lane. Immunoprecipitation with a nonimmune serum is shown in lane 6 (A-D). The results represent one of three experiments performed from three separate osteoclast preparations.

Techniques Used: Transduction, Immunoprecipitation, SDS Page, Western Blot

Analysis of the interaction of c-Src with the endogenous WASP and transduced peptides . A-D: Osteoclasts were transduced with the WASP peptides as shown below the figures. Lysates were immunoprecipitated with a WASP (A and B) or HA (C and D) antibody. Immunoprecipitates were first immunoblotted with an antibody to Src pTy418 (A and C). Subsequently, blots were stripped and blotted with an antibody to c-Src (B and D) to detect the levels of c-Src coprecipitated with WASP or HA immunoprecipitates. Immunoprecipitation with a non-immune serum (NI) is shown in lane 5 (A-D). E and F: HA-immunoprecipitates were subjected to 15% SDS-PAGE. Immunoblotting was performed with a phosphotyrosine (p-Tyrosine; panel E) to detect the phosphorylation levels of transduced proteins. Subsequently, blot was stripped and blotted with a HA- antibody (F) to determine the levels of transduced proteins immunoprecipitated in each lane. An asterisk in Fig. 5E indicates coprecipitation of a non-specific protein with HA and non-immune (NI) immunoprecipitates (lanes 1–4). Immunoprecipitation with a non-immune serum (NI) is shown in lane 1 (E and F). The results represent one of three experiments performed from three separate osteoclast preparations.
Figure Legend Snippet: Analysis of the interaction of c-Src with the endogenous WASP and transduced peptides . A-D: Osteoclasts were transduced with the WASP peptides as shown below the figures. Lysates were immunoprecipitated with a WASP (A and B) or HA (C and D) antibody. Immunoprecipitates were first immunoblotted with an antibody to Src pTy418 (A and C). Subsequently, blots were stripped and blotted with an antibody to c-Src (B and D) to detect the levels of c-Src coprecipitated with WASP or HA immunoprecipitates. Immunoprecipitation with a non-immune serum (NI) is shown in lane 5 (A-D). E and F: HA-immunoprecipitates were subjected to 15% SDS-PAGE. Immunoblotting was performed with a phosphotyrosine (p-Tyrosine; panel E) to detect the phosphorylation levels of transduced proteins. Subsequently, blot was stripped and blotted with a HA- antibody (F) to determine the levels of transduced proteins immunoprecipitated in each lane. An asterisk in Fig. 5E indicates coprecipitation of a non-specific protein with HA and non-immune (NI) immunoprecipitates (lanes 1–4). Immunoprecipitation with a non-immune serum (NI) is shown in lane 1 (E and F). The results represent one of three experiments performed from three separate osteoclast preparations.

Techniques Used: Transduction, Immunoprecipitation, SDS Page, Western Blot


Structured Review

Santa Cruz Biotechnology mab against wasp
(A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained <t>for</t> <t>synaptophysin</t> (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and <t>sh-WASP</t> on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.
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1) Product Images from "Regulation of Spine Density and Morphology by IQGAP1 Protein Domains"

Article Title: Regulation of Spine Density and Morphology by IQGAP1 Protein Domains

Journal: PLoS ONE

doi: 10.1371/journal.pone.0056574

(A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained for synaptophysin (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and sh-WASP on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.
Figure Legend Snippet: (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained for synaptophysin (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and sh-WASP on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.

Techniques Used: Cell Culture, Transfection, Staining, Expressing, Standard Deviation


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Santa Cruz Biotechnology n wasp
N Wasp, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology mouse anti wasp d1
Mouse Anti Wasp D1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology sc 13139
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    a Representative western blot of WIP, <t>N-WASP</t> <t>and</t> <t>Nck</t> expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.
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    PBMC of the younger brother (patient 2) were stained intracellularly with <t>B9</t> monoclonal antibody to <t>WASP</t> and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.
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    (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained <t>for</t> <t>synaptophysin</t> (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and <t>sh-WASP</t> on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.
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    (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained <t>for</t> <t>synaptophysin</t> (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and <t>sh-WASP</t> on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.
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    (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained <t>for</t> <t>synaptophysin</t> (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and <t>sh-WASP</t> on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.
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    Image Search Results


    a Representative western blot of WIP, N-WASP and Nck expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.

    Journal: PLoS ONE

    Article Title: WIP Regulates Persistence of Cell Migration and Ruffle Formation in Both Mesenchymal and Amoeboid Modes of Motility

    doi: 10.1371/journal.pone.0070364

    Figure Lengend Snippet: a Representative western blot of WIP, N-WASP and Nck expression in soluble lysates of lung-derived fibroblasts from WIP +/+ and WIP −/− mice. Numbers indicate relative expression levels of each protein to GAPDH content and control fibroblasts determined by densitometry. GAPDH labeling confirmed equivalent protein loading control. b FACS analysis of forward and side scatter in control (WIP +/+ ) and WIP −/− fibroblasts. c Phase-contrast images from plated control (WIP +/+ ) and WIP −/− murine fibroblasts do not show evident morphological differences between both populations. Scale bar 50 µm.

    Article Snippet: PDGFRα, WASP and N-WASP rabbit antibodies and monoclonal antibody to Nck were obtained from Santa Cruz Biotech.

    Techniques: Western Blot, Expressing, Derivative Assay, Labeling

    a WIP −/− primary murine fibroblasts were transduced with recombinant lentivirus coding for GFP, WIP-GFP, WIPΔNBD-GFP (missing the Nck binding domain) or WIPΔWBD-GFP (missing the N-WASP binding site). Soluble protein extracts were subjected to western blot analysis, using anti-GFP as probe, and developed with ECL detection kit. b Transduced WIP −/− murine fibroblasts were serum starved and stimulated with PDGF-AA for increasing times (8 and 15 min). Fixed and permeabilised cells were stained with anti-cortactin and FITC-secondary antibody and imaged in a Zeiss microscope. The percentage of GFP-positive cells forming dorsal ruffles after PDGF-AA stimulation is plotted against incubation times. One way ANOVA test and Test of Tukey * p<0,05; ** p<0,001.

    Journal: PLoS ONE

    Article Title: WIP Regulates Persistence of Cell Migration and Ruffle Formation in Both Mesenchymal and Amoeboid Modes of Motility

    doi: 10.1371/journal.pone.0070364

    Figure Lengend Snippet: a WIP −/− primary murine fibroblasts were transduced with recombinant lentivirus coding for GFP, WIP-GFP, WIPΔNBD-GFP (missing the Nck binding domain) or WIPΔWBD-GFP (missing the N-WASP binding site). Soluble protein extracts were subjected to western blot analysis, using anti-GFP as probe, and developed with ECL detection kit. b Transduced WIP −/− murine fibroblasts were serum starved and stimulated with PDGF-AA for increasing times (8 and 15 min). Fixed and permeabilised cells were stained with anti-cortactin and FITC-secondary antibody and imaged in a Zeiss microscope. The percentage of GFP-positive cells forming dorsal ruffles after PDGF-AA stimulation is plotted against incubation times. One way ANOVA test and Test of Tukey * p<0,05; ** p<0,001.

    Article Snippet: PDGFRα, WASP and N-WASP rabbit antibodies and monoclonal antibody to Nck were obtained from Santa Cruz Biotech.

    Techniques: Transduction, Recombinant, Binding Assay, Western Blot, Staining, Microscopy, Incubation

    PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.

    Journal: PLoS ONE

    Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

    doi: 10.1371/journal.pone.0003444

    Figure Lengend Snippet: PBMC of the younger brother (patient 2) were stained intracellularly with B9 monoclonal antibody to WASP and, where indicated, were stained with surface marker antibodies. (A) Monocytes and lymphocytes. Shown are patient monocytes (left), total lymphocytes (middle), and T lymphocytes (CD3 + cells) (right) indicated by filled histograms; cells of a normal individual are indicated by black outlines and isotype control by green outlines. (B) T and NK lymphocytes. CD4 (CD4 + ) and CD8 (CD8 bright ) cells, and NK cells (CD56 + CD3 − ) stained for WASP and, where indicated, for CD45RA to distinguish T cell subsets. Numbers within quadrants indicate the percentage of cells. (C) B-lymphocytes. B cells (CD19 + ) were stained with isotype control antibody (left) or WASP antibody (middle, right) and for CD27 to distinguish B-cell subsets (right). (D) Shown are the percent WASP-positive cells in different populations averaged across the two brothers. ND, not determined.

    Article Snippet: After washing with 3 ml PBS-FCS, the cells were incubated in 250 µl of Fix/Perm solution (Pharmingen, San Diego, CA) for 20 min on ice, washed twice, stained with 5 µg/ml of B9 anti-WASP monoclonal antibody (Santa Cruz, Santa Cruz, CA) or IgG2a isotype control (Pharmingen) for 30 min on ice, and washed twice with Perm/Wash solution.

    Techniques: Staining, Marker

    (A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).

    Journal: PLoS ONE

    Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

    doi: 10.1371/journal.pone.0003444

    Figure Lengend Snippet: (A) Schematic of (top) normal WASP (502 amino acids) and (bottom) WASP encoded by the patients' germ line mutation (1305delG in exon 10, arrow) with the frameshifted region (424–443) (fs) indicated. Shown are the upstream regulatory domains: EVH-1, GBD (GTPase binding), and proline-rich region (binding sites for adapter proteins and tyrosine kinases), and the downstream verprolin homology (V) (exon 10), cofilin homology (C) (exon 11) and acidic (A) (exon 12) domains that function in generating actin filaments. The intramolecular bond of autoinhibited WASP is indicated by a dotted line. (B) PBMC, neutrophils and lymphocytes (5×10 5 cells) of normal individuals (N) and patients 1 (P1) and 2 (P2) were stained as indicated with B9 and D1 antibodies to WASP residues 1–250 and W485 antibody to the C-terminal peptide. The numbers on the right indicate apparent mass (kDa) of WASP bands relative to marker proteins. The asterisk (*) in the W485 blot indicates the position of a 40 kDa marker protein, which was used to verify inclusion of the 47 kDa region. The blots were restained with actin antibodies, which verified equal protein loading (not shown).

    Article Snippet: After washing with 3 ml PBS-FCS, the cells were incubated in 250 µl of Fix/Perm solution (Pharmingen, San Diego, CA) for 20 min on ice, washed twice, stained with 5 µg/ml of B9 anti-WASP monoclonal antibody (Santa Cruz, Santa Cruz, CA) or IgG2a isotype control (Pharmingen) for 30 min on ice, and washed twice with Perm/Wash solution.

    Techniques: Mutagenesis, Binding Assay, Staining, Marker

    Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.

    Journal: PLoS ONE

    Article Title: Evolution of Highly Polymorphic T Cell Populations in Siblings with the Wiskott-Aldrich Syndrome

    doi: 10.1371/journal.pone.0003444

    Figure Lengend Snippet: Cryopreserved cells from the earliest freeze of the transformed cell line were placed in culture and sampled at the indicated times. (A) WASP expression analyzed by flow cytometry after intracellular staining with B9 WASP antibody or isotype control. The insert shows the relative frequency of WASP + and WASP − populations on a log scale. (B) Fragment length analysis of amplified exon 10 of a normal B cell line (top), the patient B cell line at 6 weeks (middle) and after long term culture (bottom). (C) Western blot of cells harvested at 2, 5 or 7 weeks and stained with B9 antibody to reveal full-length (63 kDa) WASP and 47 kDa truncated WASP.

    Article Snippet: After washing with 3 ml PBS-FCS, the cells were incubated in 250 µl of Fix/Perm solution (Pharmingen, San Diego, CA) for 20 min on ice, washed twice, stained with 5 µg/ml of B9 anti-WASP monoclonal antibody (Santa Cruz, Santa Cruz, CA) or IgG2a isotype control (Pharmingen) for 30 min on ice, and washed twice with Perm/Wash solution.

    Techniques: Transformation Assay, Expressing, Flow Cytometry, Staining, Amplification, Western Blot

    (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained for synaptophysin (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and sh-WASP on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.

    Journal: PLoS ONE

    Article Title: Regulation of Spine Density and Morphology by IQGAP1 Protein Domains

    doi: 10.1371/journal.pone.0056574

    Figure Lengend Snippet: (A) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with myc-tagged Δ-CHD IQGAP1 plus GFP (green) and double stained with MAP2 (red). (B) A high magnification view of dendritic segments from another neuron of the same culture; note the long filopodial-like protrusions merging from dendritic shafts (arrowheads). (C) A 3-D reconstruction of dendritic shafts from a sister culture; note the morphology and density of filopodial-like protrusions (arrowheads). (D–E) Confocal images showing a dendritic segment from a neuron co-transfected with myc-tagged-Δ-CHD-IQGAP1 (blue) plus GFP-PSD95 (green) and stained for synaptophysin (red). (G) Merge image; note that GFP-PSD95 (+) protrusions colocalize with synaptophysin puncta (arrowheads). (H) Graphs showing effects of the ectopic expression of myc-tagged Δ-CHD-IQGAP1 on the number of different types of dendritic spines; note that Δ-CHD-IQGAP1 significantly increases the number of thin spines and filopodial extensions, while decreases the number of mushroom-shaped spines. (I) Graphs showing the effect of scrambled-sh-Arp3, sh-Arp3, and sh-WASP on the number of dendritic protrusions. For this experiment, cultures were transfected with the corresponding GFP-or HcRed-sh plasmids at 17 DIV and fixed 24 h later. Note the significant decrease in the total number of dendritic protrusions in the sh-Arp3 and sh-WASP-treated groups. (J) Graphs showing the number of dendritic protrusions contacting synaptophysin puncta in neurons transfected with IQGAP1 WT, Δ-CHD-IQGAP1 and sh-Arp3 plus myc-tagged-IQGAP1 WT. Note the dramatic decrease in the number of dendritic protrusions contacting synaptophysin puncta in the cells treated with sh-Arp3 plus IQGAP1 WT; most of these protrusion resemble filopodial extensions. (K) Confocal image showing an example of a 17 DIV cultured hippocampal neuron transfected with HcRed-sh-Arp3 (red) plus myc-tagged IQGAP1 WT (green). (L) A high magnification view of a dendritic segment from another neuron of the same culture. (M) A 3-D reconstruction of dendritic shafts from a sister culture; note the presence of many filopodial-like protrusions. (N-P) Confocal images showing a segment of a dendritic shaft of a neuron co-transfected with myc-tagged-IQGAP1 WT (blue) plus GFP-sh-Arp3 (green) and stained for synaptophysin (red). (Q) Merge image. Note that many filopodial protrusions are not contacted by synaptophysin puncta. Bars represent mean ± standard deviation. * p<0.0001.

    Article Snippet: The following primary antibodies were used in this study: a monoclonal antibody (mAb) against MAP2 (clone AP-20) diluted 1∶1000; an affinity purified rabbit polyclonal antibody against IQGAP1 (Santa Cruz Biotechnology, H-109, sc-10792) diluted 1∶100 for immunofluorescence or 1∶2000 for immunoblotting; a rabbit polyclonal antibody or a mouse mAb against myc (Santa Cruz Biotechnology) diluted 1∶300; a mAb against synaptophysin (Chemicon International); a mAb against WASP (Santa Cruz Biotechnology) diluted 1∶2000; a rabbit polyclonal antibody against GFP (Molecular Probes, A 1122) diluted 1∶500; a mAb against PSD95 (AbCam, AB 2723) diluted 1∶250; and a rabbit polyclonal antibody against Arp2 (Santa Cruz Biotechnology) diluted 1∶2000.

    Techniques: Cell Culture, Transfection, Staining, Expressing, Standard Deviation