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human full length asc  (OriGene)


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    Structured Review

    OriGene human full length asc
    a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
    Human Full Length Asc, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human full length asc/product/OriGene
    Average 90 stars, based on 3 article reviews
    human full length asc - by Bioz Stars, 2026-06
    90/100 stars

    Images

    1) Product Images from "Structure of zebrafish NLRP3 reveals a novel mode of inflammasome activation"

    Article Title: Structure of zebrafish NLRP3 reveals a novel mode of inflammasome activation

    Journal: bioRxiv

    doi: 10.64898/2026.04.17.719140

    a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
    Figure Legend Snippet: a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.

    Techniques Used: Sequencing, SDS Page



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    a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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    a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within <t>the</t> <t>full-length</t> sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.
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    Image Search Results


    a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.

    Journal: bioRxiv

    Article Title: Structure of zebrafish NLRP3 reveals a novel mode of inflammasome activation

    doi: 10.64898/2026.04.17.719140

    Figure Lengend Snippet: a , Position and sequence of the PYD-FISNA linker in human and zebrafish NLRP3, and zebrafish NLRP3 containing human PYD-FISNA linker sequence encoded by the exon 3 of human NLRP3 gene (red dashed box). Sequences corresponding to FISNA domain and polybasic region are indicated with black lines. Cys130 palmitoylated in human NLRP3 is highlighted in blue. b , SDS-PAGE gels of sucrose gradient fractions of zebrafish NLRP3 WT and zebrafish NLRP3 containing human linker sequence. c , Sequence alignment of zebrafish and human NLRP3. Domains are indicated with lines and color-coded. Residues forming a “face-to-face” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with red and orange stars, respectively. Residues forming a “back-to-back” interface according to the human (PDB: 7PZC) and mouse (PDB: 7LFH) NLRP3 “cage” structures are indicated with blue and violet stars, respectively. Numbers correspond to alignment positions within the full-length sequence alignment. d , Position and sequence of known palmitoylation sites in human and zebrafish NLRP3. Palmitoylated residues are highlighted in blue.

    Article Snippet: Human full-length ASC was cloned into pLenti-EF1a-C-tGFP (Origene, PS100072) and tGFP was exchanged with YFP.

    Techniques: Sequencing, SDS Page