trxr1 variants Search Results


trxr1 domain  (Santa Cruz Biotechnology)
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SCHEME 1. Overview of the alternatively spliced transcripts of the TXNRD1 gene studied here. Transcrip- tion of the -transcripts is initiated at the core promoter located upstream of exon I, whereas an alternative promoter upstream of exon -VIII regulates transcription of the 1 splice variant. The 1 transcript is translated into the third isoform of <t>TrxR1</t> (TXNRD1_v3, or v3) containing an atypical N-terminal Grx domain fused to the common TrxR1 module. Arrowheads connected by a dotted line indicate primer pairs used to identify the respective splice variant, and the length of the amplified fragment is given in parentheses. The dashed part of exon I shown in this scheme in transcripts 7,8 indicates an alternative splice donor site within that exon, resulting in either 7,8 encoding TXNRD1_v1 or 1,2 encoding TXNRD1_v2. Filled exons of larger width indicate the open reading frame (ORF) of each transcript. The common TrxR1 module is shown in green, the unique part of the Grx domain of the 1 transcript is indicated in red, and the sequences shared between the Grx domain and the N-terminal part of TXNRD1_v2 are hatched. The scheme is drawn approximately to scale, as indicated in the figure. Note that the complete TrxR domain is encoded by additional exons downstream of exon V. The scheme has been modified from an earlier report, to which the reader is referred for further information including sequences and accession numbers (7). UTR, untranslated region.
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SCHEME 1. Overview of the alternatively spliced transcripts of the TXNRD1 gene studied here. Transcrip- tion of the -transcripts is initiated at the core promoter located upstream of exon I, whereas an alternative promoter upstream of exon -VIII regulates transcription of the 1 splice variant. The 1 transcript is translated into the third isoform of TrxR1 (TXNRD1_v3, or v3) containing an atypical N-terminal Grx domain fused to the common TrxR1 module. Arrowheads connected by a dotted line indicate primer pairs used to identify the respective splice variant, and the length of the amplified fragment is given in parentheses. The dashed part of exon I shown in this scheme in transcripts 7,8 indicates an alternative splice donor site within that exon, resulting in either 7,8 encoding TXNRD1_v1 or 1,2 encoding TXNRD1_v2. Filled exons of larger width indicate the open reading frame (ORF) of each transcript. The common TrxR1 module is shown in green, the unique part of the Grx domain of the 1 transcript is indicated in red, and the sequences shared between the Grx domain and the N-terminal part of TXNRD1_v2 are hatched. The scheme is drawn approximately to scale, as indicated in the figure. Note that the complete TrxR domain is encoded by additional exons downstream of exon V. The scheme has been modified from an earlier report, to which the reader is referred for further information including sequences and accession numbers (7). UTR, untranslated region.

Journal: Journal of Biological Chemistry

Article Title: Induction of Cell Membrane Protrusions by the N-terminal Glutaredoxin Domain of a Rare Splice Variant of Human Thioredoxin Reductase 1

doi: 10.1074/jbc.m708939200

Figure Lengend Snippet: SCHEME 1. Overview of the alternatively spliced transcripts of the TXNRD1 gene studied here. Transcrip- tion of the -transcripts is initiated at the core promoter located upstream of exon I, whereas an alternative promoter upstream of exon -VIII regulates transcription of the 1 splice variant. The 1 transcript is translated into the third isoform of TrxR1 (TXNRD1_v3, or v3) containing an atypical N-terminal Grx domain fused to the common TrxR1 module. Arrowheads connected by a dotted line indicate primer pairs used to identify the respective splice variant, and the length of the amplified fragment is given in parentheses. The dashed part of exon I shown in this scheme in transcripts 7,8 indicates an alternative splice donor site within that exon, resulting in either 7,8 encoding TXNRD1_v1 or 1,2 encoding TXNRD1_v2. Filled exons of larger width indicate the open reading frame (ORF) of each transcript. The common TrxR1 module is shown in green, the unique part of the Grx domain of the 1 transcript is indicated in red, and the sequences shared between the Grx domain and the N-terminal part of TXNRD1_v2 are hatched. The scheme is drawn approximately to scale, as indicated in the figure. Note that the complete TrxR domain is encoded by additional exons downstream of exon V. The scheme has been modified from an earlier report, to which the reader is referred for further information including sequences and accession numbers (7). UTR, untranslated region.

Article Snippet: Those testis sections were derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotechnology, catalog number sc-28321) generated against amino acids 71–340, encoded by exon V (Scheme 1), of the TrxR1 domain.

Techniques: Variant Assay, Amplification, Modification

FIGURE 1. Expression of v3 in testis, in particular the Leydig cells. A, a Northernblotusingav3-specificprobe,containingthefirstthreeexonsofthe Grx domain unique to v3, identified a single transcript in testis, whereas all other analyzed tissues were negative. P.B.L., peripheral blood leukocytes. B, spe- cific analysis of first-strand cDNA using the F-VIII/R2 primer pair (Scheme 1) showed a PCR product corresponding to 468 bp with the strongest expres- sion in testis and weak expression in heart, liver, kidney, pancreas, spleen, and ovary.Skel.Muscle,skeletalmuscle;Sm.Intestine,smallintestine;Pos.Ctrl,positive control; Neg. Ctrl, negative control. C and D, immunohistochemical staining of tissue sections from testis, derived from a donor in his mid-40s, are shown. C, a polyclonal antibody, -v3, generated against a synthetic peptide contained in the unique part in the Grx domain of v3, showed a strong signal in the interstitial Leydig cells. D shows a preabsorption control done with the synthetic peptide usedtogeneratetheantibody,diminishingthesignalinLeydigcellsandillustrat- ingthespecificityinthestainingpattern.EandF,testistissuesectionstakenfrom theHumanProteinAtlas,accordingtoitsacademicusagepermission(seeRef.13 andwww.proteinatlas.org),areshownforcomparison.Thosetestissectionswere derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotech- nology, catalog number sc-28321) generated against amino acids 71–340, encodedbyexonV(Scheme1),oftheTrxR1domain.Hence,thatantibodybinds all three isoforms TXNRD1_v1–3, and staining is seen in Leydig cells as well as Sertoli cells and seminiferous tubules.

Journal: Journal of Biological Chemistry

Article Title: Induction of Cell Membrane Protrusions by the N-terminal Glutaredoxin Domain of a Rare Splice Variant of Human Thioredoxin Reductase 1

doi: 10.1074/jbc.m708939200

Figure Lengend Snippet: FIGURE 1. Expression of v3 in testis, in particular the Leydig cells. A, a Northernblotusingav3-specificprobe,containingthefirstthreeexonsofthe Grx domain unique to v3, identified a single transcript in testis, whereas all other analyzed tissues were negative. P.B.L., peripheral blood leukocytes. B, spe- cific analysis of first-strand cDNA using the F-VIII/R2 primer pair (Scheme 1) showed a PCR product corresponding to 468 bp with the strongest expres- sion in testis and weak expression in heart, liver, kidney, pancreas, spleen, and ovary.Skel.Muscle,skeletalmuscle;Sm.Intestine,smallintestine;Pos.Ctrl,positive control; Neg. Ctrl, negative control. C and D, immunohistochemical staining of tissue sections from testis, derived from a donor in his mid-40s, are shown. C, a polyclonal antibody, -v3, generated against a synthetic peptide contained in the unique part in the Grx domain of v3, showed a strong signal in the interstitial Leydig cells. D shows a preabsorption control done with the synthetic peptide usedtogeneratetheantibody,diminishingthesignalinLeydigcellsandillustrat- ingthespecificityinthestainingpattern.EandF,testistissuesectionstakenfrom theHumanProteinAtlas,accordingtoitsacademicusagepermission(seeRef.13 andwww.proteinatlas.org),areshownforcomparison.Thosetestissectionswere derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotech- nology, catalog number sc-28321) generated against amino acids 71–340, encodedbyexonV(Scheme1),oftheTrxR1domain.Hence,thatantibodybinds all three isoforms TXNRD1_v1–3, and staining is seen in Leydig cells as well as Sertoli cells and seminiferous tubules.

Article Snippet: Those testis sections were derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotechnology, catalog number sc-28321) generated against amino acids 71–340, encoded by exon V (Scheme 1), of the TrxR1 domain.

Techniques: Expressing, Positive Control, Negative Control, Immunohistochemical staining, Staining, Derivative Assay, Generated, Control

FIGURE 2. Expression of TrxR1 splice variant in different cancer cell lines. A, first-strand reverse transcription-PCR of various cancer cell lines was per- formed to identify the potential concomitant transcription of different splice variants of TrxR1 (Scheme 1). The 1 variant showed a distinct transcription pattern in some of the cell lines, whereas the 7,8 transcripts were expressed at a high level in all of the investigated cancer cell lines, and 1,2 was weakly but consistently detected except in HCC1937 and Jurkat. B, PCR results using cDNA from treated HeLa cells showed an up-regulation of 1 by estradiol or testosterone. Estradiol, estradiol (1 M); Testost., testosterone (0.1 M); No FCS, medium without fetal calf serum; HU (10), hydroxyurea (10 M); HU (100), hydroxyurea (100 M); Pos. Ctrl., positive control; Neg. Ctrl., negative control. The cDNA of v3 in a plasmid was used as a positive template control.

Journal: Journal of Biological Chemistry

Article Title: Induction of Cell Membrane Protrusions by the N-terminal Glutaredoxin Domain of a Rare Splice Variant of Human Thioredoxin Reductase 1

doi: 10.1074/jbc.m708939200

Figure Lengend Snippet: FIGURE 2. Expression of TrxR1 splice variant in different cancer cell lines. A, first-strand reverse transcription-PCR of various cancer cell lines was per- formed to identify the potential concomitant transcription of different splice variants of TrxR1 (Scheme 1). The 1 variant showed a distinct transcription pattern in some of the cell lines, whereas the 7,8 transcripts were expressed at a high level in all of the investigated cancer cell lines, and 1,2 was weakly but consistently detected except in HCC1937 and Jurkat. B, PCR results using cDNA from treated HeLa cells showed an up-regulation of 1 by estradiol or testosterone. Estradiol, estradiol (1 M); Testost., testosterone (0.1 M); No FCS, medium without fetal calf serum; HU (10), hydroxyurea (10 M); HU (100), hydroxyurea (100 M); Pos. Ctrl., positive control; Neg. Ctrl., negative control. The cDNA of v3 in a plasmid was used as a positive template control.

Article Snippet: Those testis sections were derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotechnology, catalog number sc-28321) generated against amino acids 71–340, encoded by exon V (Scheme 1), of the TrxR1 domain.

Techniques: Expressing, Variant Assay, Reverse Transcription, Positive Control, Negative Control, Plasmid Preparation, Control

FIGURE 4. Dotted cytosolic and membrane-associated localization pattern of v3 compared with actin and tubulin. The fluorescence microscope pictures show HeLa (A and B) or HEK293 cells (C–G) transfected with either the complete isoform v3 fused to GFP (v3-GFP) or the Grx domain of v3 fused to GFP (v3(Grx)-GFP) and also stained for actin, tubulin, and nuclei using DAPI. Cells transfected with a TrxR1-GFP construct or the GFP protein alone were used as control (GFP control).

Journal: Journal of Biological Chemistry

Article Title: Induction of Cell Membrane Protrusions by the N-terminal Glutaredoxin Domain of a Rare Splice Variant of Human Thioredoxin Reductase 1

doi: 10.1074/jbc.m708939200

Figure Lengend Snippet: FIGURE 4. Dotted cytosolic and membrane-associated localization pattern of v3 compared with actin and tubulin. The fluorescence microscope pictures show HeLa (A and B) or HEK293 cells (C–G) transfected with either the complete isoform v3 fused to GFP (v3-GFP) or the Grx domain of v3 fused to GFP (v3(Grx)-GFP) and also stained for actin, tubulin, and nuclei using DAPI. Cells transfected with a TrxR1-GFP construct or the GFP protein alone were used as control (GFP control).

Article Snippet: Those testis sections were derived from a 26-year-old male (E) and a 68-year-old male (F) and stained with a commercial mouse monoclonal -TrxR1 primary antibody (Santa Cruz Biotechnology, catalog number sc-28321) generated against amino acids 71–340, encoded by exon V (Scheme 1), of the TrxR1 domain.

Techniques: Membrane, Fluorescence, Microscopy, Transfection, Staining, Construct, Control