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| Plasmid Name | Proper Citation | Insert Name | Organism | Bacterial Resistance | Defining Citation |
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pCMV-OptoTGFBRs Resource Report Resource Website 1+ mentions |
RRID:Addgene_118942 | OptoTGFBRs | Mus musculus | Kanamycin | PMID:29241005 | Backbone Marker:Clontech; Backbone Size:3925; Vector Backbone:ptdToamto-N1; Vector Types:Mammalian Expression; Bacterial Resistance:Kanamycin | 2026-08-15 01:03:08 | 1 | ||
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mPLD2-PX (62-192) Resource Report Resource Website |
RRID:Addgene_119128 | mPLD2-PX (62-192) | Mus musculus | Ampicillin | PMID:30948714 | Vector Backbone:pGEX4T2; Vector Types:Bacterial Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:10 | 0 | ||
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mSNX13-PX (558-677) Resource Report Resource Website |
RRID:Addgene_119094 | mSNX13-PX (558-677) | Mus musculus | Ampicillin | PMID:30948714 | Amino Acid Sequence: GVPVIAQVVGTERYTSGSKVGTCTLYSVRLTHGDFTWTTKKKFRHFQELHRDLQRHKVLMSLLPLARFAVTHSPAREAAAEDIPSLPRGGSEGSARHTASKQKYLENYLNRLLTMSFYRNYHAMTEFLEVS | Vector Backbone:pGEX4T2; Vector Types:Bacterial Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:10 | 0 | |
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SNX19-PX (528-664) (mouse) Resource Report Resource Website |
RRID:Addgene_119100 | SNX19-PX (528-664) | Mus musculus | Ampicillin | PMID:30948714 | Amino Acid Sequence: SPDGPVVIQNLRITGTITAREHSGTGFHPYTLYTVKYETVLNGENSSGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIKNVKGPKKLFPDLPFGNMDSDRVEARKSLLESFLKQLCAIPEIGNSEEVQEFLALN | Vector Backbone:pGEX4T2; Vector Types:Bacterial Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:10 | 0 | |
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pcDNA3.1-m-Flt4 Resource Report Resource Website |
RRID:Addgene_119232 | Vegfr3 | Mus musculus | Ampicillin | Vector Backbone:pCDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:11 | 0 | |||
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psubCMV-mVEGF-D-WPRE Resource Report Resource Website 1+ mentions |
RRID:Addgene_119226 | Vegfd | Mus musculus | Ampicillin | Vector Backbone:psubCMV-WPRE; Vector Types:AAV; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:12 | 1 | |||
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psubCMV-WPRE-IL3SP-mVEGF-D-dNdC Resource Report Resource Website |
RRID:Addgene_119229 | IL3SP-Vegfd-dNdC | Mus musculus | Ampicillin | Vector Backbone:psubCMV-WPRE; Vector Types:AAV; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:12 | 0 | |||
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ID1GFP Donor Resource Report Resource Website |
RRID:Addgene_119282 | Id1GFP + homology arms | Mus musculus | Ampicillin | PMID:31582374 | Backbone Size:2700; Vector Backbone:pUC19; Vector Types:Reporter; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:12 | 0 | ||
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ID1-pLVXT Resource Report Resource Website |
RRID:Addgene_119280 | Id1 | Mus musculus | Ampicillin | PMID:31582374 | Backbone Marker:Clontech; Backbone Size:7800; Vector Backbone:pLVX-tight-Puro; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:13 | 0 | ||
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eGFP-proα2(I)-G610C Resource Report Resource Website 1+ mentions |
RRID:Addgene_119827 | Type I procollagen α2 chain | Mus musculus | Ampicillin | PMID:30287488 | These plasmids were constructed after the G610C mouse model of OI in which the Gly610 residue (starting from the N-terminal end of the triple helix) was substituted with Cys. These mouse type I procollagen plasmids were designed for immortalized and primary murine osteoblasts and fibroblasts. Their expression in other cells might cause significant disruption of assembly, folding and trafficking of type I procollagen, resulting in artifacts. Even in osteoblasts and fibroblasts a fraction of transfected chains, particularly proα2, might be trafficked/degraded as monomers instead of being integrated into procollagen heterotrimers. In our experience, the best evidence of normal behavior of the transfected chains is the appearance of fluorescent extracellular collagen fibers ~ 12 h after transfection. Fluorescent molecules should be incorporated into fibers even when the transfected chains contain the N-propeptide cleavage site, because the cleavage is highly conformation sensitive and always incomplete. We recommend following these guidelines when using the plasmids 1) Only mouse cells that have high expression of endogenous type I procollagen are suitable for studies of physiologically-relevant processes with these constructs. 2) At least 100 μM ascorbic acid at and after transfection is required to ensure proper procollagen folding (for some cells, preincubation with ascorbic acid before transfection might be needed). 3) Optimization of transfection efficiency is needed for all cell types. 4) Experiments beyond 24h after transfection are not recommended, to avoid excessive accumulation of aggregates and cell malfunction caused by increased procollagen synthesis. 5) Lack of extracellular fluorescent fibers 12-24 h after transfection indicates improper procollagen synthesis/trafficking or cellular malfunction. 6) Excessive expression of transfected chains might cause rapid accumulation of large procollagen aggregates in the ER, resulting in cellular malfunction and death. Contact information: Shakib Omari ([email protected]), Sergey Leikin ([email protected]). | Backbone Size:5400; Vector Backbone:pcDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | Col1a2 exons 2-5 replaced by fluorescent tag, Glycine 610 mutated to Cysteine | 2026-08-15 01:03:16 | 2 |
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pAAV-HDR-mEGFP-Actin Resource Report Resource Website 1+ mentions |
RRID:Addgene_119870 | beta Actin | Mus musculus | Ampicillin | PMID:29056297 | Backbone Size:2905; Vector Backbone:PX551; Vector Types:Mouse Targeting, AAV, CRISPR; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:16 | 3 | ||
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pBS C-ret Resource Report Resource Website |
RRID:Addgene_119900 | ret | Mus musculus | Ampicillin | PMID:20064391 | This plasmid can be used to generate an in situ hybridization antisense probe for mouse C-ret. Linearize the plasmid with NotI and use T7 to transcribe the ~1kb probe. | Vector Backbone:pBS; Vector Types:in situ hybridization probe; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:16 | 0 | |
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eGFP-proα1(I) Resource Report Resource Website |
RRID:Addgene_119843 | Type I procollagen α1 chain | Mus musculus | Ampicillin | PMID:30287488 | These mouse type I procollagen plasmids were designed for immortalized and primary murine osteoblasts and fibroblasts. Their expression in other cells might cause significant disruption of assembly, folding and trafficking of type I procollagen, resulting in artifacts. Even in osteoblasts and fibroblasts a fraction of transfected chains, particularly proα2, might be trafficked/degraded as monomers instead of being integrated into procollagen heterotrimers. In our experience, the best evidence of normal behavior of the transfected chains is the appearance of fluorescent extracellular collagen fibers ~ 12 h after transfection. Fluorescent molecules should be incorporated into fibers even when the transfected chains contain the N-propeptide cleavage site, because the cleavage is highly conformation sensitive and always incomplete. We recommend following these guidelines when using the plasmids 1) Only mouse cells that have high expression of endogenous type I procollagen are suitable for studies of physiologically-relevant processes with these constructs. 2) At least 100 μM ascorbic acid at and after transfection is required to ensure proper procollagen folding (for some cells, preincubation with ascorbic acid before transfection might be needed). 3) Optimization of transfection efficiency is needed for all cell types. 4) Experiments beyond 24h after transfection are not recommended, to avoid excessive accumulation of aggregates and cell malfunction caused by increased procollagen synthesis. 5) Lack of extracellular fluorescent fibers 12-24 h after transfection indicates improper procollagen synthesis/trafficking or cellular malfunction. 6) Excessive expression of transfected chains might cause rapid accumulation of large procollagen aggregates in the ER, resulting in cellular malfunction and death. Contact information: Shakib Omari ([email protected]), Sergey Leikin ([email protected]). | Backbone Size:5300; Vector Backbone:pcDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | Col1a1 exons 2-3 replaced by fluorescent tag | 2026-08-15 01:03:17 | 0 |
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mApple-proα1(I) Resource Report Resource Website |
RRID:Addgene_119844 | Type I procollagen α1 chain | Mus musculus | Ampicillin | PMID:30287488 | These mouse type I procollagen plasmids were designed for immortalized and primary murine osteoblasts and fibroblasts. Their expression in other cells might cause significant disruption of assembly, folding and trafficking of type I procollagen, resulting in artifacts. Even in osteoblasts and fibroblasts a fraction of transfected chains, particularly proα2, might be trafficked/degraded as monomers instead of being integrated into procollagen heterotrimers. In our experience, the best evidence of normal behavior of the transfected chains is the appearance of fluorescent extracellular collagen fibers ~ 12 h after transfection. Fluorescent molecules should be incorporated into fibers even when the transfected chains contain the N-propeptide cleavage site, because the cleavage is highly conformation sensitive and always incomplete. We recommend following these guidelines when using the plasmids 1) Only mouse cells that have high expression of endogenous type I procollagen are suitable for studies of physiologically-relevant processes with these constructs. 2) At least 100 μM ascorbic acid at and after transfection is required to ensure proper procollagen folding (for some cells, preincubation with ascorbic acid before transfection might be needed). 3) Optimization of transfection efficiency is needed for all cell types. 4) Experiments beyond 24h after transfection are not recommended, to avoid excessive accumulation of aggregates and cell malfunction caused by increased procollagen synthesis. 5) Lack of extracellular fluorescent fibers 12-24 h after transfection indicates improper procollagen synthesis/trafficking or cellular malfunction. 6) Excessive expression of transfected chains might cause rapid accumulation of large procollagen aggregates in the ER, resulting in cellular malfunction and death. Contact information: Shakib Omari ([email protected]), Sergey Leikin ([email protected]). | Backbone Size:5300; Vector Backbone:pcDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | Col1a1 exons 2-3 replaced by fluorescent tag | 2026-08-15 01:03:16 | 0 |
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mCerulean-proα1(I) Resource Report Resource Website |
RRID:Addgene_119842 | Type I procollagen α1 chain | Mus musculus | Ampicillin | PMID:30287488 | These mouse type I procollagen plasmids were designed for immortalized and primary murine osteoblasts and fibroblasts. Their expression in other cells might cause significant disruption of assembly, folding and trafficking of type I procollagen, resulting in artifacts. Even in osteoblasts and fibroblasts a fraction of transfected chains, particularly proα2, might be trafficked/degraded as monomers instead of being integrated into procollagen heterotrimers. In our experience, the best evidence of normal behavior of the transfected chains is the appearance of fluorescent extracellular collagen fibers ~ 12 h after transfection. Fluorescent molecules should be incorporated into fibers even when the transfected chains contain the N-propeptide cleavage site, because the cleavage is highly conformation sensitive and always incomplete. We recommend following these guidelines when using the plasmids 1) Only mouse cells that have high expression of endogenous type I procollagen are suitable for studies of physiologically-relevant processes with these constructs. 2) At least 100 μM ascorbic acid at and after transfection is required to ensure proper procollagen folding (for some cells, preincubation with ascorbic acid before transfection might be needed). 3) Optimization of transfection efficiency is needed for all cell types. 4) Experiments beyond 24h after transfection are not recommended, to avoid excessive accumulation of aggregates and cell malfunction caused by increased procollagen synthesis. 5) Lack of extracellular fluorescent fibers 12-24 h after transfection indicates improper procollagen synthesis/trafficking or cellular malfunction. 6) Excessive expression of transfected chains might cause rapid accumulation of large procollagen aggregates in the ER, resulting in cellular malfunction and death. Contact information: Shakib Omari ([email protected]), Sergey Leikin ([email protected]). | Backbone Size:5300; Vector Backbone:pcDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | Col1a1 exons 2-3 replaced by fluorescent tag | 2026-08-15 01:03:16 | 0 |
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mApple-proα2(I) Resource Report Resource Website |
RRID:Addgene_119840 | Type I procollagen α2 chain | Mus musculus | Ampicillin | PMID:30287488 | These mouse type I procollagen plasmids were designed for immortalized and primary murine osteoblasts and fibroblasts. Their expression in other cells might cause significant disruption of assembly, folding and trafficking of type I procollagen, resulting in artifacts. Even in osteoblasts and fibroblasts a fraction of transfected chains, particularly proα2, might be trafficked/degraded as monomers instead of being integrated into procollagen heterotrimers. In our experience, the best evidence of normal behavior of the transfected chains is the appearance of fluorescent extracellular collagen fibers ~ 12 h after transfection. Fluorescent molecules should be incorporated into fibers even when the transfected chains contain the N-propeptide cleavage site, because the cleavage is highly conformation sensitive and always incomplete. We recommend following these guidelines when using the plasmids 1) Only mouse cells that have high expression of endogenous type I procollagen are suitable for studies of physiologically-relevant processes with these constructs. 2) At least 100 μM ascorbic acid at and after transfection is required to ensure proper procollagen folding (for some cells, preincubation with ascorbic acid before transfection might be needed). 3) Optimization of transfection efficiency is needed for all cell types. 4) Experiments beyond 24h after transfection are not recommended, to avoid excessive accumulation of aggregates and cell malfunction caused by increased procollagen synthesis. 5) Lack of extracellular fluorescent fibers 12-24 h after transfection indicates improper procollagen synthesis/trafficking or cellular malfunction. 6) Excessive expression of transfected chains might cause rapid accumulation of large procollagen aggregates in the ER, resulting in cellular malfunction and death. Contact information: Shakib Omari ([email protected]), Sergey Leikin ([email protected]). | Backbone Size:5400; Vector Backbone:pcDNA3.1; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | Col1a2 exons 2-5 replaced by fluorescent tag | 2026-08-15 01:03:17 | 0 |
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LentiV_Neo_Sik3_T142Q Resource Report Resource Website |
RRID:Addgene_119973 | Sik3 | Mus musculus | Ampicillin | PMID:31697837 | Please visit https://www.biorxiv.org/content/10.1101/636969v1 for BioRxiv preprint | Backbone Size:7210; Vector Backbone:LentiV_Neo; Vector Types:Mammalian Expression, Lentiviral; Bacterial Resistance:Ampicillin | change Threonine 142 to Glutamine | 2026-08-15 01:03:19 | 0 |
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LentiV_Neo_Sik3 Resource Report Resource Website |
RRID:Addgene_119972 | Sik3 | Mus musculus | Ampicillin | PMID:31697837 | Please visit https://www.biorxiv.org/content/10.1101/636969v1 for BioRxiv preprint | Backbone Size:7210; Vector Backbone:LentiV_Neo; Vector Types:Mammalian Expression, Lentiviral; Bacterial Resistance:Ampicillin | 2026-08-15 01:03:17 | 0 | |
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pCAGGS-6His-mISG15 Resource Report Resource Website 1+ mentions |
RRID:Addgene_12445 | ISG15 | Mus musculus | Ampicillin | PMID:15485925 | Backbone Size:4790; Vector Backbone:pCAGGS; Vector Types:Mammalian Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:04:07 | 2 | ||
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pET15b-mISG15(GG) Resource Report Resource Website 1+ mentions |
RRID:Addgene_12448 | C-terminal processed form of ISG15 | Mus musculus | Ampicillin | PMID:16275353 | Backbone Size:5708; Vector Backbone:pET15b; Vector Types:Bacterial Expression; Bacterial Resistance:Ampicillin | 2026-08-15 01:04:06 | 2 |
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