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dnah2 pa5-64309 antibody  (Thermo Fisher)


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    Thermo Fisher dnah2 pa5-64309 antibody
    A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human <t>DNAH1</t> (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.
    Dnah2 Pa5 64309 Antibody, supplied by Thermo Fisher, 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/dnah2 pa5-64309 antibody/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
    dnah2 pa5-64309 antibody - by Bioz Stars, 2025-12
    90/100 stars

    Images

    1) Product Images from "Genetic Defects in DNAH2 Underlie Male Infertility With Multiple Morphological Abnormalities of the Sperm Flagella in Humans and Mice"

    Article Title: Genetic Defects in DNAH2 Underlie Male Infertility With Multiple Morphological Abnormalities of the Sperm Flagella in Humans and Mice

    Journal: Frontiers in Cell and Developmental Biology

    doi: 10.3389/fcell.2021.662903

    A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human DNAH1 (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.
    Figure Legend Snippet: A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human DNAH1 (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.

    Techniques Used: Variant Assay, Sequencing, Staining, Mutagenesis, Binding Assay

    Flagellar ultrastructure is disorganized, and axonemal proteins express abnormally in Dnah2 -null sperm. (A,B) Scanning electron microscopy images of Dnah2 +/Δ (A) and Dnah2 Δ/Δ (B) sperm. Dnah2 Δ/Δ sperm display absence of ( left ) or an irregular ( right ) mitochondrial helical sheath in the midpiece of the sperm tail, along with abnormal head shapes. Arrowheads indicate annulus. H, head; MP, midpiece; and PP, principal piece. (C,D) Transmission electron microscopy images of Dnah2 +/Δ (C) and Dnah2 Δ/Δ (D) sperm. Representative cross-section images of TEM reveal conformational defects in the midpiece of Dnah2 Δ/Δ sperm. Incomplete 9+2 axonemal structure ( left ), delocalized outer dense fibers (ODF, arrow) and microtubule doublet ( middle , arrowhead), and lack of the axonemal components ( right ) were observed in the Dnah2 Δ/Δ sperm. Inner (yellow asterisk) and outer (white asterisk) dynein arm structure were observed from microtubule doublet occasionally ( left , inset; scale bar = 50 nm). Microtubule doublets are numbered with the absence of the corresponding microtubule doublet in red. M, mitochondria. (E) Confocal fluorescence images of axonemal proteins in WT and Dnah2 Δ/Δ sperm. Dnah2 Δ/Δ sperm do not express another IDA component (DNAH1, magenta) and a radial spoke protein (RSPH3, green) but an ODA protein (DNAH9, yellow). Flagella microtubules (AcTub, white) and sperm heads (Hoechst, blue) serve as controls. The corresponding DIC images are shown together for Dnah2 Δ/Δ sperm.
    Figure Legend Snippet: Flagellar ultrastructure is disorganized, and axonemal proteins express abnormally in Dnah2 -null sperm. (A,B) Scanning electron microscopy images of Dnah2 +/Δ (A) and Dnah2 Δ/Δ (B) sperm. Dnah2 Δ/Δ sperm display absence of ( left ) or an irregular ( right ) mitochondrial helical sheath in the midpiece of the sperm tail, along with abnormal head shapes. Arrowheads indicate annulus. H, head; MP, midpiece; and PP, principal piece. (C,D) Transmission electron microscopy images of Dnah2 +/Δ (C) and Dnah2 Δ/Δ (D) sperm. Representative cross-section images of TEM reveal conformational defects in the midpiece of Dnah2 Δ/Δ sperm. Incomplete 9+2 axonemal structure ( left ), delocalized outer dense fibers (ODF, arrow) and microtubule doublet ( middle , arrowhead), and lack of the axonemal components ( right ) were observed in the Dnah2 Δ/Δ sperm. Inner (yellow asterisk) and outer (white asterisk) dynein arm structure were observed from microtubule doublet occasionally ( left , inset; scale bar = 50 nm). Microtubule doublets are numbered with the absence of the corresponding microtubule doublet in red. M, mitochondria. (E) Confocal fluorescence images of axonemal proteins in WT and Dnah2 Δ/Δ sperm. Dnah2 Δ/Δ sperm do not express another IDA component (DNAH1, magenta) and a radial spoke protein (RSPH3, green) but an ODA protein (DNAH9, yellow). Flagella microtubules (AcTub, white) and sperm heads (Hoechst, blue) serve as controls. The corresponding DIC images are shown together for Dnah2 Δ/Δ sperm.

    Techniques Used: Electron Microscopy, Transmission Assay, Fluorescence



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    dnah2 pa5-64309 antibody  (Thermo Fisher)
    90
    Thermo Fisher dnah2 pa5-64309 antibody
    A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human <t>DNAH1</t> (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.
    Dnah2 Pa5 64309 Antibody, supplied by Thermo Fisher, 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/dnah2 pa5-64309 antibody/product/Thermo Fisher
    Average 90 stars, based on 1 article reviews
    dnah2 pa5-64309 antibody - by Bioz Stars, 2025-12
    90/100 stars
    		  Buy from Supplier

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    A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human DNAH1 (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: Genetic Defects in DNAH2 Underlie Male Infertility With Multiple Morphological Abnormalities of the Sperm Flagella in Humans and Mice

    doi: 10.3389/fcell.2021.662903

    Figure Lengend Snippet: A novel bi-allelic DNAH2 variant identified from a consanguineous family with oligoasthenozoospermia. (A) Pedigree of a consanguineous family with four infertile males (IV-1, IV-2, IV-3, and V-1). WES was performed with IV-3 and V-1 (arrows). Sanger sequencing verified segregation of the variant (red) in the infertile males. A plus (+) indicates a wild-type allele and an asterisk (*) denotes a sample not available for this study. (B) PAP-stained semen from patients IV-1 and IV-3. Multiple morphological defects including near absence of a tail or a short tail (arrowheads), and spherical heads (arrows) are prominent from both patients. (C) Mapping of the DNAH2 variant. Mutation of G to T in exon 82 of DNAH2 cDNA (c.12720G > T; NCBI RefSeq identifier NM_020877) results in a tryptophan-to-cysteine (p.W4240C) substitution in the dynein heavy chain domain. Previously reported pathogenic variants are also marked (black). (D) Chromatograms of the DNAH2 non-synonymous variant in an infertile sibling (IV-1) and his mother (III-1). The variant is underlined, and the resulting amino acid substitution is marked in red. (E) A sequence alignment of the DNAH2 protein across multiple species. The tryptophan at position 4240 (arrow) is conserved in multiple organisms. An asterisk (*) indicates positions fully conserved and a period (.) indicates positions with weakly similar amino acids. (F,G) Structural modeling of the DNAH2 mutation from this study. (F) Ribbon structure of human DNAH1 (PDB ID: 5NUG), a homolog of human DNAH2. ATP-binding sites are colored in green ( left) . The enlarged area is the region corresponding to that of W4240 in DNAH2 ( right ). DNAH1 W4464, which is homologous to W4240, is represented in a space-filling model. (G) Ribbon diagram shows mutation of tryptophan at position 4464 (W4464, orange) to cysteine (W4464C, pink) is predicted to form disulfide bond with nearby C4454 and distort protein backbone structure.

    Article Snippet: Rabbit polyclonal DNAH1 (PA5-57826), DNAH2 (PA5-64309), and DNAH9 (PA5-45744) antibodies were purchased from Thermo Fisher Scientific.

    Techniques: Variant Assay, Sequencing, Staining, Mutagenesis, Binding Assay

    Flagellar ultrastructure is disorganized, and axonemal proteins express abnormally in Dnah2 -null sperm. (A,B) Scanning electron microscopy images of Dnah2 +/Δ (A) and Dnah2 Δ/Δ (B) sperm. Dnah2 Δ/Δ sperm display absence of ( left ) or an irregular ( right ) mitochondrial helical sheath in the midpiece of the sperm tail, along with abnormal head shapes. Arrowheads indicate annulus. H, head; MP, midpiece; and PP, principal piece. (C,D) Transmission electron microscopy images of Dnah2 +/Δ (C) and Dnah2 Δ/Δ (D) sperm. Representative cross-section images of TEM reveal conformational defects in the midpiece of Dnah2 Δ/Δ sperm. Incomplete 9+2 axonemal structure ( left ), delocalized outer dense fibers (ODF, arrow) and microtubule doublet ( middle , arrowhead), and lack of the axonemal components ( right ) were observed in the Dnah2 Δ/Δ sperm. Inner (yellow asterisk) and outer (white asterisk) dynein arm structure were observed from microtubule doublet occasionally ( left , inset; scale bar = 50 nm). Microtubule doublets are numbered with the absence of the corresponding microtubule doublet in red. M, mitochondria. (E) Confocal fluorescence images of axonemal proteins in WT and Dnah2 Δ/Δ sperm. Dnah2 Δ/Δ sperm do not express another IDA component (DNAH1, magenta) and a radial spoke protein (RSPH3, green) but an ODA protein (DNAH9, yellow). Flagella microtubules (AcTub, white) and sperm heads (Hoechst, blue) serve as controls. The corresponding DIC images are shown together for Dnah2 Δ/Δ sperm.

    Journal: Frontiers in Cell and Developmental Biology

    Article Title: Genetic Defects in DNAH2 Underlie Male Infertility With Multiple Morphological Abnormalities of the Sperm Flagella in Humans and Mice

    doi: 10.3389/fcell.2021.662903

    Figure Lengend Snippet: Flagellar ultrastructure is disorganized, and axonemal proteins express abnormally in Dnah2 -null sperm. (A,B) Scanning electron microscopy images of Dnah2 +/Δ (A) and Dnah2 Δ/Δ (B) sperm. Dnah2 Δ/Δ sperm display absence of ( left ) or an irregular ( right ) mitochondrial helical sheath in the midpiece of the sperm tail, along with abnormal head shapes. Arrowheads indicate annulus. H, head; MP, midpiece; and PP, principal piece. (C,D) Transmission electron microscopy images of Dnah2 +/Δ (C) and Dnah2 Δ/Δ (D) sperm. Representative cross-section images of TEM reveal conformational defects in the midpiece of Dnah2 Δ/Δ sperm. Incomplete 9+2 axonemal structure ( left ), delocalized outer dense fibers (ODF, arrow) and microtubule doublet ( middle , arrowhead), and lack of the axonemal components ( right ) were observed in the Dnah2 Δ/Δ sperm. Inner (yellow asterisk) and outer (white asterisk) dynein arm structure were observed from microtubule doublet occasionally ( left , inset; scale bar = 50 nm). Microtubule doublets are numbered with the absence of the corresponding microtubule doublet in red. M, mitochondria. (E) Confocal fluorescence images of axonemal proteins in WT and Dnah2 Δ/Δ sperm. Dnah2 Δ/Δ sperm do not express another IDA component (DNAH1, magenta) and a radial spoke protein (RSPH3, green) but an ODA protein (DNAH9, yellow). Flagella microtubules (AcTub, white) and sperm heads (Hoechst, blue) serve as controls. The corresponding DIC images are shown together for Dnah2 Δ/Δ sperm.

    Article Snippet: Rabbit polyclonal DNAH1 (PA5-57826), DNAH2 (PA5-64309), and DNAH9 (PA5-45744) antibodies were purchased from Thermo Fisher Scientific.

    Techniques: Electron Microscopy, Transmission Assay, Fluorescence