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tinatm software, version 2.0  (Raytest GmbH)
90
Raytest GmbH tinatm software, version 2.0
Tinatm Software, Version 2.0, supplied by Raytest GmbH, 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/product/without+borders+binary+file+v2/10__1074_slash_jbc__m006221200-78-16-20?v=Raytest+GmbH
Average 90 stars, based on 1 article reviews
tinatm software, version 2.0 - by Bioz Stars, 2026-08
90/100 stars
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geneworks v2.5.1  (GeneWorks)
90
GeneWorks geneworks v2.5.1
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Geneworks V2.5.1, supplied by GeneWorks, 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/product/without+borders+binary+file+v2/pmc02174577-60-6-5?v=GeneWorks
Average 90 stars, based on 1 article reviews
geneworks v2.5.1 - by Bioz Stars, 2026-08
90/100 stars
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splicesitefinder-like scoring system alamut version 2.0  (Interactive Biosoftware)
90
Interactive Biosoftware splicesitefinder-like scoring system alamut version 2.0
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Splicesitefinder Like Scoring System Alamut Version 2.0, supplied by Interactive Biosoftware, 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/product/without+borders+binary+file+v2/pmc03330208-266-4-10?v=Interactive+Biosoftware
Average 90 stars, based on 1 article reviews
splicesitefinder-like scoring system alamut version 2.0 - by Bioz Stars, 2026-08
90/100 stars
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poisson modelling statsdirect v2.7.8  (StatsDirect ltd)
90
StatsDirect ltd poisson modelling statsdirect v2.7.8
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Poisson Modelling Statsdirect V2.7.8, supplied by StatsDirect ltd, 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/product/without+borders+binary+file+v2/pmc03289670-46-6-7?v=StatsDirect+ltd
Average 90 stars, based on 1 article reviews
poisson modelling statsdirect v2.7.8 - by Bioz Stars, 2026-08
90/100 stars
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7500 v2.0.1  (3i - Intelligent Imaging)
90
3i - Intelligent Imaging 7500 v2.0.1
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
7500 V2.0.1, supplied by 3i - Intelligent Imaging, 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/product/without+borders+binary+file+v2/pmc03317409-116-15-17?v=3i+-+Intelligent+Imaging
Average 90 stars, based on 1 article reviews
7500 v2.0.1 - by Bioz Stars, 2026-08
90/100 stars
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balance assessment computer software package v.2.0  (MotionSoft Inc)
90
MotionSoft Inc balance assessment computer software package v.2.0
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Balance Assessment Computer Software Package V.2.0, supplied by MotionSoft Inc, 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/product/without+borders+binary+file+v2/pmc02465155-148-17-23?v=MotionSoft+Inc
Average 90 stars, based on 1 article reviews
balance assessment computer software package v.2.0 - by Bioz Stars, 2026-08
90/100 stars
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alt-rtm hdr enhancer v2 reagent  (STEMCELL Technologies Inc)
90
STEMCELL Technologies Inc alt-rtm hdr enhancer v2 reagent
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Alt Rtm Hdr Enhancer V2 Reagent, supplied by STEMCELL Technologies Inc, 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/product/without+borders+binary+file+v2/pm40055648-66-45-41?v=STEMCELL+Technologies+Inc
Average 90 stars, based on 1 article reviews
alt-rtm hdr enhancer v2 reagent - by Bioz Stars, 2026-08
90/100 stars
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macbas v.2.0 image analysis software  (FUJIFILM)
90
FUJIFILM macbas v.2.0 image analysis software
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Macbas V.2.0 Image Analysis Software, supplied by FUJIFILM, 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/product/without+borders+binary+file+v2/pmc01370476-561-17-22?v=FUJIFILM
Average 90 stars, based on 1 article reviews
macbas v.2.0 image analysis software - by Bioz Stars, 2026-08
90/100 stars
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hrt imaging software v2.01  (heidelberg engineering)
90
heidelberg engineering hrt imaging software v2.01
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Hrt Imaging Software V2.01, supplied by heidelberg engineering, 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/product/without+borders+binary+file+v2/pmc01771663-66-1-5?v=heidelberg+engineering
Average 90 stars, based on 1 article reviews
hrt imaging software v2.01 - by Bioz Stars, 2026-08
90/100 stars
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ranco v2  (Invensys Systems Inc)
90
Invensys Systems Inc ranco v2
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Ranco V2, supplied by Invensys Systems Inc, 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/product/without+borders+binary+file+v2/us09057547-65-6-14?v=Invensys+Systems+Inc
Average 90 stars, based on 1 article reviews
ranco v2 - by Bioz Stars, 2026-08
90/100 stars
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smart-seq v2  (Vienna Biocenter Core Facilities GmbH)
90
Vienna Biocenter Core Facilities GmbH smart-seq v2
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Smart Seq V2, supplied by Vienna Biocenter Core Facilities GmbH, 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/product/without+borders+binary+file+v2/pmc11997658-247-0-25?v=Vienna+Biocenter+Core+Facilities+GmbH
Average 90 stars, based on 1 article reviews
smart-seq v2 - by Bioz Stars, 2026-08
90/100 stars
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allertop v2.0  (Innovagen AB)
90
Innovagen AB allertop v2.0
Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks <t>v2.5.1</t> software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.
Allertop V2.0, supplied by Innovagen AB, 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/product/without+borders+binary+file+v2/pmc11402771-94-13-15?v=Innovagen+AB
Average 90 stars, based on 1 article reviews
allertop v2.0 - by Bioz Stars, 2026-08
90/100 stars
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Image Search Results


Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks v2.5.1 software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.

Journal: The Journal of Cell Biology

Article Title: Caenorhabditis elegans β-G Spectrin Is Dispensable for Establishment of Epithelial Polarity, but Essential for Muscular and Neuronal Function

doi:

Figure Lengend Snippet: Three spectrin genes of C . elegans . (A) Domain organization of α and β spectrin polypeptides. C . elegans orthologues are indicated. Spectrin is an (α-β) 2 tetramer; an α-β-G tetramer is shown. (B) Evolutionary relationship of β spectrin subunits. A UPGMA tree showing relative homology between five β-spectrin subunits from different species was plotted using Geneworks v2.5.1 software. Of the three identified human β-spectrin proteins (SPTB, SPTBN1, and SPTBN2), the two nonerythroid β-spectrins SPTBN1 and SPTBN2 are more closely related (65% identity). The two invertebrate β-G spectrins show ∼58% identity, whereas ∼32% of β-spectrin residues are conserved among all five proteins. (C) Dot matrix alignments of C . elegans predicted spectrin polypeptides with their human (α and β-G) or Drosophila (β H ) orthologues. Note the additional diagonals that arise from the multiple spectrin repeats that make up the bulk of each subunit. (D) Comparison of PH domains of β G -spectrins from Homo sapiens (SPTBN1), Drosophila (DROBSPEC), and C . elegans (BGS-1, shorter spliceform). Residues used in the alignment are indicated. Note that conserved residues fall in loop regions that determine the substrate specificity of PH domains.

Article Snippet: Sequence alignments were made using Geneworks v2.5.1.

Techniques: Software