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A) Experimental diagram. B) wnnUMAPs of <t>ASCs</t> colored by tissue (left) or subset (right). Data from HD matched fixed CITEseq. C) Percent subset of total ASCs by sample. Data from HD matched fixed CITEseq. D) Percent subisotype usage by sample. Data from HD matched fixed CITEseq. E) Experimental diagram. F) Representative region of interest from a bone marrow core colored by fluorescence signal (top) or subset labels of segmented cells (bottom). Data from HD BM spatial proteomics. G) <t>Percent</t> <t>ASC</t> subset of total cells by individual. Data from HD BM spatial proteomics. H) Computational diagram. I) Observed (black diamond) and randomly permuted (grey density) percent of ASCs found in homotypic niches (defined as all ASCs in a niche having identical subset identities), by individual. Empirical p-values calculated as the number of permutations with homotypic niche frequencies greater or equal to the observed homotypic niche frequency, divided by the number of permutations plus one. Data from HD BM spatial proteomics. J) Computational diagram. K) Scaled enrichment scores of cell types (x-axis) in ASC subset (y-axis) niches by individual (panel). Q-values<0.1 were colored white. Data from HD BM spatial proteomics. L) Representative images (panels) of ASC-rich regions colored by fluorescence signal (left) or cell type labels of segmented cells (right). Data from HD BM spatial proteomics.
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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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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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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) Experimental diagram. B) wnnUMAPs of ASCs colored by tissue (left) or subset (right). Data from HD matched fixed CITEseq. C) Percent subset of total ASCs by sample. Data from HD matched fixed CITEseq. D) Percent subisotype usage by sample. Data from HD matched fixed CITEseq. E) Experimental diagram. F) Representative region of interest from a bone marrow core colored by fluorescence signal (top) or subset labels of segmented cells (bottom). Data from HD BM spatial proteomics. G) Percent ASC subset of total cells by individual. Data from HD BM spatial proteomics. H) Computational diagram. I) Observed (black diamond) and randomly permuted (grey density) percent of ASCs found in homotypic niches (defined as all ASCs in a niche having identical subset identities), by individual. Empirical p-values calculated as the number of permutations with homotypic niche frequencies greater or equal to the observed homotypic niche frequency, divided by the number of permutations plus one. Data from HD BM spatial proteomics. J) Computational diagram. K) Scaled enrichment scores of cell types (x-axis) in ASC subset (y-axis) niches by individual (panel). Q-values<0.1 were colored white. Data from HD BM spatial proteomics. L) Representative images (panels) of ASC-rich regions colored by fluorescence signal (left) or cell type labels of segmented cells (right). Data from HD BM spatial proteomics.

Journal: bioRxiv

Article Title: Multi-omic profiling of human antibody-secreting cells reveals diverse subsets sustain durable humoral immunity

doi: 10.64898/2026.04.13.717827

Figure Lengend Snippet: A) Experimental diagram. B) wnnUMAPs of ASCs colored by tissue (left) or subset (right). Data from HD matched fixed CITEseq. C) Percent subset of total ASCs by sample. Data from HD matched fixed CITEseq. D) Percent subisotype usage by sample. Data from HD matched fixed CITEseq. E) Experimental diagram. F) Representative region of interest from a bone marrow core colored by fluorescence signal (top) or subset labels of segmented cells (bottom). Data from HD BM spatial proteomics. G) Percent ASC subset of total cells by individual. Data from HD BM spatial proteomics. H) Computational diagram. I) Observed (black diamond) and randomly permuted (grey density) percent of ASCs found in homotypic niches (defined as all ASCs in a niche having identical subset identities), by individual. Empirical p-values calculated as the number of permutations with homotypic niche frequencies greater or equal to the observed homotypic niche frequency, divided by the number of permutations plus one. Data from HD BM spatial proteomics. J) Computational diagram. K) Scaled enrichment scores of cell types (x-axis) in ASC subset (y-axis) niches by individual (panel). Q-values<0.1 were colored white. Data from HD BM spatial proteomics. L) Representative images (panels) of ASC-rich regions colored by fluorescence signal (left) or cell type labels of segmented cells (right). Data from HD BM spatial proteomics.

Article Snippet: For the ASC culture condition screen, total BM ASCs were stimulated for 72 hours with CpG ODN 2006 (10μg/mL, Invivogen) or BCR crosslinker (anti-kappa light chain; 1μg/mL, Southern Biotech) with various combinations of stimulatory reagents, including MEGACD40L (0.1μg/ml, Enzo Life Sciences), BAFF (1μg/mL, PeproTech), CXCL12 (0.1μg/ml, R&D Systems), IL-2 (0.1μg/mL, Biolegend), and IL-21 (0.1μg/mL, PeproTech).

Techniques: Fluorescence, Spatial Proteomics

A) Experimental diagram. B) Serum Ig concentrations of patients with NDMM by timepoint (x-axis), isotype (y-axis), and the isotype of each patient’s malignant cell (shapes). Transparency indicates values outside the healthy reference ranges specified in the clinical reports. Data from clinical quantitative Ig assay. C) Percent ASCs of total BMMCs for HDs (left) and patients with NDMM, by timepoint (x-axis). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to HDs. Data from MM longitudinal BM CITEseq. *Q<0.1; **Q<0.01; ***Q<0.001 D) Percent non-malignant ASCs of total ASCs for patients with NDMM, by timepoint (x-axis). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to PRETX. Data from MM longitudinal BM CITEseq. ***Q<0.001 E) Percent non-malignant ASC subset of total BMMCs for HDs (left) and patients with NDMM, by timepoint (x-axis) and subset (panels). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to HDs. Data from MM longitudinal BM CITEseq. *Q<0.1; **Q<0.01; ***Q<0.001

Journal: bioRxiv

Article Title: Multi-omic profiling of human antibody-secreting cells reveals diverse subsets sustain durable humoral immunity

doi: 10.64898/2026.04.13.717827

Figure Lengend Snippet: A) Experimental diagram. B) Serum Ig concentrations of patients with NDMM by timepoint (x-axis), isotype (y-axis), and the isotype of each patient’s malignant cell (shapes). Transparency indicates values outside the healthy reference ranges specified in the clinical reports. Data from clinical quantitative Ig assay. C) Percent ASCs of total BMMCs for HDs (left) and patients with NDMM, by timepoint (x-axis). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to HDs. Data from MM longitudinal BM CITEseq. *Q<0.1; **Q<0.01; ***Q<0.001 D) Percent non-malignant ASCs of total ASCs for patients with NDMM, by timepoint (x-axis). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to PRETX. Data from MM longitudinal BM CITEseq. ***Q<0.001 E) Percent non-malignant ASC subset of total BMMCs for HDs (left) and patients with NDMM, by timepoint (x-axis) and subset (panels). Crossbar indicates mean. Q-values calculated by Wilcoxon rank sum test with FDR correction, comparing to HDs. Data from MM longitudinal BM CITEseq. *Q<0.1; **Q<0.01; ***Q<0.001

Article Snippet: For the ASC culture condition screen, total BM ASCs were stimulated for 72 hours with CpG ODN 2006 (10μg/mL, Invivogen) or BCR crosslinker (anti-kappa light chain; 1μg/mL, Southern Biotech) with various combinations of stimulatory reagents, including MEGACD40L (0.1μg/ml, Enzo Life Sciences), BAFF (1μg/mL, PeproTech), CXCL12 (0.1μg/ml, R&D Systems), IL-2 (0.1μg/mL, Biolegend), and IL-21 (0.1μg/mL, PeproTech).

Techniques:

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