fbf1 rabbit Search Results


k76 rrid ab 531836  (Developmental Studies Hybridoma Bank)
95
Developmental Studies Hybridoma Bank k76 rrid ab 531836
K76 Rrid Ab 531836, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/k76 rrid ab 531836/product/Developmental Studies Hybridoma Bank
Average 95 stars, based on 1 article reviews
k76 rrid ab 531836 - by Bioz Stars, 2026-03
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dzip1l  (Proteintech)
93
Proteintech dzip1l
Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens <t>DZIP1/DZIP1L</t> and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to
Dzip1l, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/dzip1l/product/Proteintech
Average 93 stars, based on 1 article reviews
dzip1l - by Bioz Stars, 2026-03
93/100 stars
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anti fbf1  (Proteintech)
93
Proteintech anti fbf1
Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens <t>DZIP1/DZIP1L</t> and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to
Anti Fbf1, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/anti fbf1/product/Proteintech
Average 93 stars, based on 1 article reviews
anti fbf1 - by Bioz Stars, 2026-03
93/100 stars
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fbf1 rabbit  (Millipore)
90
Millipore fbf1 rabbit
Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens <t>DZIP1/DZIP1L</t> and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to
Fbf1 Rabbit, supplied by Millipore, 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/result/fbf1 rabbit/product/Millipore
Average 90 stars, based on 1 article reviews
fbf1 rabbit - by Bioz Stars, 2026-03
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1 ap  (Proteintech)
93
Proteintech 1 ap
Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens <t>DZIP1/DZIP1L</t> and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to
1 Ap, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/1 ap/product/Proteintech
Average 93 stars, based on 1 article reviews
1 ap - by Bioz Stars, 2026-03
93/100 stars
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fbf1 antibody  (Novus Biologicals)
N/A
The FBF1 Antibody from Novus is a FBF1 antibody to FBF1. This antibody reacts with Human. The FBF1 antibody has been validated for the following applications: Western Blot, Immunoprecipitation.
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fbf 1 fbf1 rabbit polyclonal antibody  (OriGene)
N/A
FBF1 Antibody middle region
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anti fbf1 monoclonal antibody  (Creative BioMart)
N/A
FBF1 Fas TNFRSF6 binding factor 1 is a protein coding gene Diseases associated with FBF1 include nocardiosis and hypermobility syndrome GO annotations related to this gene include protein binding Keratin binding protein required for epithelial
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fbf1 antibody rabbit pab antigen affinity purified  (Sino Biological)
N/A
Produced in rabbits immunized with E coli derived Human FBF1 fragment and purified by antigen affinity chromatography
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anti fbf1 antibody  (St Johns Laboratory)
N/A
Unconjugated Rabbit polyclonal to FBF1 Conjugation note Unconjugated Application note WB ELISA Reactivity note Human Mouse
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rabbit anti human lsp1 monoclonal clone fbf-12  (Innovative Research Inc)
N/A
Rabbit Anti Human LSP1 Monoclonal Clone FBF-12 from Innovative Research is a monoclonal antibody in a Liquid format, buffered in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA.
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Image Search Results


Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens DZIP1/DZIP1L and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: The ARPKD Protein DZIP1L Regulates Ciliary Protein Entry by Modulating the Architecture and Function of Ciliary Transition Fibers.

doi: 10.1002/advs.202308820

Figure Lengend Snippet: Figure 1. C. elegans DZIP-1 is an evolutionarily conserved basal body protein. A) The sequence alignment of two evolutionarily conserved domain (DZIP- like domain and the C2H2 zine finger domain) within C. elegans DZIP-1, H. sapiens DZIP1/DZIP1L and M. musculus DZIP1/DZIP1L. The Dzip-like_N domain (red line) is the most conserved domain in DZIP1/DZIP1L proteins. The ZnF_C2H2 domain is indicated by an orange line. And the highly conserved region is enclosed in the purple box. Asterisks are used to indicate the residues that, when mutated, can cause human ARPKD. B) DZIP-1 localizes to the ciliary base in C. elegans. The schematic diagram of phasmid cilia is depicted on the left, GFP-tagged DZIP-1 specifically localizes to

Article Snippet: Protein localization was confirmed by immunofluorescence imaging. gRNA sequence was as follows: DZIP1L gRNA#1, 5′- TGATCATCTTGCGACGCCGG-3′; DZIP1L gRNA#2, 5′- CAGTCCATGCTATCATGGCG-3′; ANKRD26 gRNA#1, 5′-GGGTAGCTCACAATCCTCTG-3′; ANKRD26 gRNA#2, 5′- AAATTCTTGTAACTAGAGTG-3′; Antibodies: The following primary antibodies were used in this study: ANKRD26 (rabbit, GeneTex, GTX128255, 1:500), DZIP1L (rabbit, Proteintech, 17474-1-AP, 1:500), FBF1 (rabbit, Proteintech, 11531-1-AP, 1:500), ARL13B (rabbit, Proteintech, 17711-1-AP, 1:500), KIAA0586/TALPID3 (rabbit, Proteintech, 24421-1-AP, 1:500), SCLT1 (rabbit, Proteintech, 14875- 1-AP, 1:500), CEP164 (rabbit, Proteintech, 22227-1-AP, 1:500), CEP89 (rabbit, Abcam, ab204410, 1:500), ODF2 (rabbit, Abcam, ab43840, 1:500), ODF2 (mouse, Abnova, H00004957-M01, 1:500), γ-tublin (mouse, Sigma-Aldrich, T6557, 1:1,000), FAM92A (rabbit, Proteintech, 24803-1- AP, 1:500), CBY1 (rabbit, Proteintech, 12239-1-AP, 1:500), GFP(mouse, Roche, 11814460001,1:200), IFT140 (rabbit, Proteintech, 17460-1-AP, 1:500), GT335(mouse, adipogen life science, A40251903), GLI3 (AF3690, R&D Systems), PC2 (Baltimore Polycystic Kidney Disease (PKD) Research and Clinical Core Center), Ac-tubulin (mouse, sigma, T7451, 1:300), Flag (mouse, sigma, F1804, 1:300), CEP290 (rabbit, abcam, ab84870).

Techniques: Sequencing

Figure 6. The precise localization of DZIP1L in human RPE cells. Spatial localization of DZIP1L was examined using a combination of Ultrastructure expansion microscopy (ExM) and confocal microscopy. As our DZIP1L polyclonal antibody is derived from rabbits, and most of our antibodies for TF and TZ markers are also polyclonal antibodies from rabbit, co-labeling them with antibodies is not feasible. To assess their co-localization, we employed transgenic FLAG-DZIP1L and utilized a mouse monoclonal FLAG antibody (IgG1 isotype) to label DZIP1L. While cilia were marked using anti-Ac-tubulin, a mouse monoclonal antibody with IgG2b isotype. A) FLAG-DZIP1L was localized beneath the classical TZ component CEP290 in both ciliated and non-

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: The ARPKD Protein DZIP1L Regulates Ciliary Protein Entry by Modulating the Architecture and Function of Ciliary Transition Fibers.

doi: 10.1002/advs.202308820

Figure Lengend Snippet: Figure 6. The precise localization of DZIP1L in human RPE cells. Spatial localization of DZIP1L was examined using a combination of Ultrastructure expansion microscopy (ExM) and confocal microscopy. As our DZIP1L polyclonal antibody is derived from rabbits, and most of our antibodies for TF and TZ markers are also polyclonal antibodies from rabbit, co-labeling them with antibodies is not feasible. To assess their co-localization, we employed transgenic FLAG-DZIP1L and utilized a mouse monoclonal FLAG antibody (IgG1 isotype) to label DZIP1L. While cilia were marked using anti-Ac-tubulin, a mouse monoclonal antibody with IgG2b isotype. A) FLAG-DZIP1L was localized beneath the classical TZ component CEP290 in both ciliated and non-

Article Snippet: Protein localization was confirmed by immunofluorescence imaging. gRNA sequence was as follows: DZIP1L gRNA#1, 5′- TGATCATCTTGCGACGCCGG-3′; DZIP1L gRNA#2, 5′- CAGTCCATGCTATCATGGCG-3′; ANKRD26 gRNA#1, 5′-GGGTAGCTCACAATCCTCTG-3′; ANKRD26 gRNA#2, 5′- AAATTCTTGTAACTAGAGTG-3′; Antibodies: The following primary antibodies were used in this study: ANKRD26 (rabbit, GeneTex, GTX128255, 1:500), DZIP1L (rabbit, Proteintech, 17474-1-AP, 1:500), FBF1 (rabbit, Proteintech, 11531-1-AP, 1:500), ARL13B (rabbit, Proteintech, 17711-1-AP, 1:500), KIAA0586/TALPID3 (rabbit, Proteintech, 24421-1-AP, 1:500), SCLT1 (rabbit, Proteintech, 14875- 1-AP, 1:500), CEP164 (rabbit, Proteintech, 22227-1-AP, 1:500), CEP89 (rabbit, Abcam, ab204410, 1:500), ODF2 (rabbit, Abcam, ab43840, 1:500), ODF2 (mouse, Abnova, H00004957-M01, 1:500), γ-tublin (mouse, Sigma-Aldrich, T6557, 1:1,000), FAM92A (rabbit, Proteintech, 24803-1- AP, 1:500), CBY1 (rabbit, Proteintech, 12239-1-AP, 1:500), GFP(mouse, Roche, 11814460001,1:200), IFT140 (rabbit, Proteintech, 17460-1-AP, 1:500), GT335(mouse, adipogen life science, A40251903), GLI3 (AF3690, R&D Systems), PC2 (Baltimore Polycystic Kidney Disease (PKD) Research and Clinical Core Center), Ac-tubulin (mouse, sigma, T7451, 1:300), Flag (mouse, sigma, F1804, 1:300), CEP290 (rabbit, abcam, ab84870).

Techniques: Microscopy, Confocal Microscopy, Derivative Assay, Labeling, Transgenic Assay

Figure 7. Conserved role of DZIP1L-ANKRD26 module in cilia gating in human RPE cells. A) The genetic interaction between DZIP1L and ANKRD26 in cilia formation is conserved in mammalian cells. The knockouts of either DZIP1L or ANKRD26 led to a moderate decrease in ciliation ratio. However, when both DZIP1L and ANKRD26 were knocked out, cilia formation was nearly completely blocked. The ciliation ratio was shown in the lower panel. Data are presented as mean ± SEM. n > 300 cells from three independent experiments. Significant differences were determined by two tailed t-test analysis. Scale bars: 5μm. B) Ciliary entry of the IFT component IFT140 was compromised in double mutants of DZIP1L and ANKRD26, compared to either of

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: The ARPKD Protein DZIP1L Regulates Ciliary Protein Entry by Modulating the Architecture and Function of Ciliary Transition Fibers.

doi: 10.1002/advs.202308820

Figure Lengend Snippet: Figure 7. Conserved role of DZIP1L-ANKRD26 module in cilia gating in human RPE cells. A) The genetic interaction between DZIP1L and ANKRD26 in cilia formation is conserved in mammalian cells. The knockouts of either DZIP1L or ANKRD26 led to a moderate decrease in ciliation ratio. However, when both DZIP1L and ANKRD26 were knocked out, cilia formation was nearly completely blocked. The ciliation ratio was shown in the lower panel. Data are presented as mean ± SEM. n > 300 cells from three independent experiments. Significant differences were determined by two tailed t-test analysis. Scale bars: 5μm. B) Ciliary entry of the IFT component IFT140 was compromised in double mutants of DZIP1L and ANKRD26, compared to either of

Article Snippet: Protein localization was confirmed by immunofluorescence imaging. gRNA sequence was as follows: DZIP1L gRNA#1, 5′- TGATCATCTTGCGACGCCGG-3′; DZIP1L gRNA#2, 5′- CAGTCCATGCTATCATGGCG-3′; ANKRD26 gRNA#1, 5′-GGGTAGCTCACAATCCTCTG-3′; ANKRD26 gRNA#2, 5′- AAATTCTTGTAACTAGAGTG-3′; Antibodies: The following primary antibodies were used in this study: ANKRD26 (rabbit, GeneTex, GTX128255, 1:500), DZIP1L (rabbit, Proteintech, 17474-1-AP, 1:500), FBF1 (rabbit, Proteintech, 11531-1-AP, 1:500), ARL13B (rabbit, Proteintech, 17711-1-AP, 1:500), KIAA0586/TALPID3 (rabbit, Proteintech, 24421-1-AP, 1:500), SCLT1 (rabbit, Proteintech, 14875- 1-AP, 1:500), CEP164 (rabbit, Proteintech, 22227-1-AP, 1:500), CEP89 (rabbit, Abcam, ab204410, 1:500), ODF2 (rabbit, Abcam, ab43840, 1:500), ODF2 (mouse, Abnova, H00004957-M01, 1:500), γ-tublin (mouse, Sigma-Aldrich, T6557, 1:1,000), FAM92A (rabbit, Proteintech, 24803-1- AP, 1:500), CBY1 (rabbit, Proteintech, 12239-1-AP, 1:500), GFP(mouse, Roche, 11814460001,1:200), IFT140 (rabbit, Proteintech, 17460-1-AP, 1:500), GT335(mouse, adipogen life science, A40251903), GLI3 (AF3690, R&D Systems), PC2 (Baltimore Polycystic Kidney Disease (PKD) Research and Clinical Core Center), Ac-tubulin (mouse, sigma, T7451, 1:300), Flag (mouse, sigma, F1804, 1:300), CEP290 (rabbit, abcam, ab84870).

Techniques: Two Tailed Test