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human proil 1β  (OriGene)


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    Structured Review

    OriGene human proil 1β
    The same volume of in vitro synthesized proIL1β and proIL1β[D 100 A] were used and loaded on the gel. Fragments 1, 2 and 3 are labeled. Putative mature in vitro synthesized sea bass IL1β (MS 101 -Q 261 ) has been loaded as control. Numbers on the left indicate the mass of the molecular weight markers in kDa. The double bands corresponding to the highest molecular weight form (fragment 1) suggested cleavage at the C-terminal end of <t>proIL-1β.</t> This interpretation was supported by N-terminal sequencing of fragment 1′ , which revealed that this fragment has the N-terminal sequence of proIL-1β (M 1 ESEMKC). Furthermore, mutation of D 252 results in a proIL-1β protein that no longer yields fragment 1 upon incubation with caspase-1 .
    Human Proil 1β, supplied by OriGene, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+proil+1%CE%B2/pmc03511578-104-17-51?v=OriGene
    Average 92 stars, based on 2 article reviews
    human proil 1β - by Bioz Stars, 2026-07
    92/100 stars

    Images

    1) Product Images from "Caspase-1 and IL-1β Processing in a Teleost Fish"

    Article Title: Caspase-1 and IL-1β Processing in a Teleost Fish

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0050450

    The same volume of in vitro synthesized proIL1β and proIL1β[D 100 A] were used and loaded on the gel. Fragments 1, 2 and 3 are labeled. Putative mature in vitro synthesized sea bass IL1β (MS 101 -Q 261 ) has been loaded as control. Numbers on the left indicate the mass of the molecular weight markers in kDa. The double bands corresponding to the highest molecular weight form (fragment 1) suggested cleavage at the C-terminal end of proIL-1β. This interpretation was supported by N-terminal sequencing of fragment 1′ , which revealed that this fragment has the N-terminal sequence of proIL-1β (M 1 ESEMKC). Furthermore, mutation of D 252 results in a proIL-1β protein that no longer yields fragment 1 upon incubation with caspase-1 .
    Figure Legend Snippet: The same volume of in vitro synthesized proIL1β and proIL1β[D 100 A] were used and loaded on the gel. Fragments 1, 2 and 3 are labeled. Putative mature in vitro synthesized sea bass IL1β (MS 101 -Q 261 ) has been loaded as control. Numbers on the left indicate the mass of the molecular weight markers in kDa. The double bands corresponding to the highest molecular weight form (fragment 1) suggested cleavage at the C-terminal end of proIL-1β. This interpretation was supported by N-terminal sequencing of fragment 1′ , which revealed that this fragment has the N-terminal sequence of proIL-1β (M 1 ESEMKC). Furthermore, mutation of D 252 results in a proIL-1β protein that no longer yields fragment 1 upon incubation with caspase-1 .

    Techniques Used: In Vitro, Synthesized, Labeling, Molecular Weight, Sequencing, Mutagenesis, Incubation

    ( A ) Processing of in vitro translated chicken proIL-1β and mutants by sea bass caspase-1. The same volume of in vitro translated chicken proIL-1β, proIL1β[D 77 A], proIL1β[D 80 A] and proIL1β[D 82 A] were loaded on the gel. In vitro translated putative mature chicken IL-1β forms (MI 119 -R 267 , MI 122 -R 267 and MS 81 -R 267 ) were loaded as controls. ( B ) Processing of in vitro translated human proIL-1β and mutants by sea bass caspase-1. ( C ) Processing of in vitro translated human proIL-1β and mutants by human caspase-1. The same volume of in vitro tranlsated proIL-1β , proIL1β[D 116 A], proIL1β[D 128 A] and proIL1β[D 116 A/D 128 A] was loaded on the gel. In vitro translated mature human IL-1β (MA 117 -S 269 ) and human IL-1β form (MS 129 -S 269 ) starting at S 129 , homologue to sea bass S 101 , were loaded as controls. Mature forms are highlighted by arrow heads. Numbers on the left indicate the mass of the molecular weight markers in kDa.
    Figure Legend Snippet: ( A ) Processing of in vitro translated chicken proIL-1β and mutants by sea bass caspase-1. The same volume of in vitro translated chicken proIL-1β, proIL1β[D 77 A], proIL1β[D 80 A] and proIL1β[D 82 A] were loaded on the gel. In vitro translated putative mature chicken IL-1β forms (MI 119 -R 267 , MI 122 -R 267 and MS 81 -R 267 ) were loaded as controls. ( B ) Processing of in vitro translated human proIL-1β and mutants by sea bass caspase-1. ( C ) Processing of in vitro translated human proIL-1β and mutants by human caspase-1. The same volume of in vitro tranlsated proIL-1β , proIL1β[D 116 A], proIL1β[D 128 A] and proIL1β[D 116 A/D 128 A] was loaded on the gel. In vitro translated mature human IL-1β (MA 117 -S 269 ) and human IL-1β form (MS 129 -S 269 ) starting at S 129 , homologue to sea bass S 101 , were loaded as controls. Mature forms are highlighted by arrow heads. Numbers on the left indicate the mass of the molecular weight markers in kDa.

    Techniques Used: In Vitro, Molecular Weight



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    Image Search Results


    The same volume of in vitro synthesized proIL1β and proIL1β[D 100 A] were used and loaded on the gel. Fragments 1, 2 and 3 are labeled. Putative mature in vitro synthesized sea bass IL1β (MS 101 -Q 261 ) has been loaded as control. Numbers on the left indicate the mass of the molecular weight markers in kDa. The double bands corresponding to the highest molecular weight form (fragment 1) suggested cleavage at the C-terminal end of proIL-1β. This interpretation was supported by N-terminal sequencing of fragment 1′ , which revealed that this fragment has the N-terminal sequence of proIL-1β (M 1 ESEMKC). Furthermore, mutation of D 252 results in a proIL-1β protein that no longer yields fragment 1 upon incubation with caspase-1 .

    Journal: PLoS ONE

    Article Title: Caspase-1 and IL-1β Processing in a Teleost Fish

    doi: 10.1371/journal.pone.0050450

    Figure Lengend Snippet: The same volume of in vitro synthesized proIL1β and proIL1β[D 100 A] were used and loaded on the gel. Fragments 1, 2 and 3 are labeled. Putative mature in vitro synthesized sea bass IL1β (MS 101 -Q 261 ) has been loaded as control. Numbers on the left indicate the mass of the molecular weight markers in kDa. The double bands corresponding to the highest molecular weight form (fragment 1) suggested cleavage at the C-terminal end of proIL-1β. This interpretation was supported by N-terminal sequencing of fragment 1′ , which revealed that this fragment has the N-terminal sequence of proIL-1β (M 1 ESEMKC). Furthermore, mutation of D 252 results in a proIL-1β protein that no longer yields fragment 1 upon incubation with caspase-1 .

    Article Snippet: HSpCMV-XL5proIL1β[D 116 A], HSpCMV-XL5proIL1β[D 128 A] and HSpCMV-XL5proIL1β[D 116 A/D 128 A], for producing mutated forms of human proIL-1β in D 116 , D 128 or D 116 /D 128 : each aspartate was mutated to alanine by site-directed mutagenesis using HSpCMV-XL5proIL1β (IL-1β Human cDNA clone (NM_000576.2) in pCMV-XL5 plasmid from Origene (#SC122566)) as template and the primers listed in .

    Techniques: In Vitro, Synthesized, Labeling, Molecular Weight, Sequencing, Mutagenesis, Incubation

    ( A ) Processing of in vitro translated chicken proIL-1β and mutants by sea bass caspase-1. The same volume of in vitro translated chicken proIL-1β, proIL1β[D 77 A], proIL1β[D 80 A] and proIL1β[D 82 A] were loaded on the gel. In vitro translated putative mature chicken IL-1β forms (MI 119 -R 267 , MI 122 -R 267 and MS 81 -R 267 ) were loaded as controls. ( B ) Processing of in vitro translated human proIL-1β and mutants by sea bass caspase-1. ( C ) Processing of in vitro translated human proIL-1β and mutants by human caspase-1. The same volume of in vitro tranlsated proIL-1β , proIL1β[D 116 A], proIL1β[D 128 A] and proIL1β[D 116 A/D 128 A] was loaded on the gel. In vitro translated mature human IL-1β (MA 117 -S 269 ) and human IL-1β form (MS 129 -S 269 ) starting at S 129 , homologue to sea bass S 101 , were loaded as controls. Mature forms are highlighted by arrow heads. Numbers on the left indicate the mass of the molecular weight markers in kDa.

    Journal: PLoS ONE

    Article Title: Caspase-1 and IL-1β Processing in a Teleost Fish

    doi: 10.1371/journal.pone.0050450

    Figure Lengend Snippet: ( A ) Processing of in vitro translated chicken proIL-1β and mutants by sea bass caspase-1. The same volume of in vitro translated chicken proIL-1β, proIL1β[D 77 A], proIL1β[D 80 A] and proIL1β[D 82 A] were loaded on the gel. In vitro translated putative mature chicken IL-1β forms (MI 119 -R 267 , MI 122 -R 267 and MS 81 -R 267 ) were loaded as controls. ( B ) Processing of in vitro translated human proIL-1β and mutants by sea bass caspase-1. ( C ) Processing of in vitro translated human proIL-1β and mutants by human caspase-1. The same volume of in vitro tranlsated proIL-1β , proIL1β[D 116 A], proIL1β[D 128 A] and proIL1β[D 116 A/D 128 A] was loaded on the gel. In vitro translated mature human IL-1β (MA 117 -S 269 ) and human IL-1β form (MS 129 -S 269 ) starting at S 129 , homologue to sea bass S 101 , were loaded as controls. Mature forms are highlighted by arrow heads. Numbers on the left indicate the mass of the molecular weight markers in kDa.

    Article Snippet: HSpCMV-XL5proIL1β[D 116 A], HSpCMV-XL5proIL1β[D 128 A] and HSpCMV-XL5proIL1β[D 116 A/D 128 A], for producing mutated forms of human proIL-1β in D 116 , D 128 or D 116 /D 128 : each aspartate was mutated to alanine by site-directed mutagenesis using HSpCMV-XL5proIL1β (IL-1β Human cDNA clone (NM_000576.2) in pCMV-XL5 plasmid from Origene (#SC122566)) as template and the primers listed in .

    Techniques: In Vitro, Molecular Weight