We narrowed to 121 results for: mEos3.2
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Plasmid#57483PurposeLocalization: Mitochondrial Membrane, Excitation: 507 / 572, Emission: 516 / 580DepositorAvailable SinceFeb. 5, 2015AvailabilityIndustry, Academic Institutions, and Nonprofits
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mEos3.2-Actin-C-18
Plasmid#57443PurposeLocalization: Actin, Excitation: 507 / 572, Emission: 516 / 580DepositorAvailable SinceMarch 12, 2015AvailabilityIndustry, Academic Institutions, and Nonprofits -
trLATmEos3.2
Plasmid#203745PurposeEncodes the transmembrane domain from human LAT with mEos3.2 fused on the C terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2-cortactin
Plasmid#193287Purposemammalian transient expression of mEos3.2-cortactinDepositorAvailable SinceDec. 16, 2022AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trCD45
Plasmid#203753PurposeEncodes the transmembrane domain from CD45 with mEos3.2 fused on the N terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
PMmEos3.2
Plasmid#203755PurposeEncodes the membrane anchor of Lyn including the first 10 residues of the N terminus, with 1 myristoylation and 1 palmitoylation, with mEos3.2 fused to the C terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2GPI
Plasmid#203759PurposeEncodes the fluorescent protein mEos3.2 followed by the C-terminal sequence derived from CD58 encoding a GPI-attachment signal. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 16, 2023AvailabilityAcademic Institutions and Nonprofits only -
trPAGmEos3.2
Plasmid#203752PurposeEncodes the transmembrane domain from PAG/CSK, including its 2 palmitoylation sites, with mEos3.2 fused on the C terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
MmEos3.2
Plasmid#203754PurposeEncodes the membrane anchor of Src including the first 15 resideues of the N terminus, with 1 myristoylation and short polybasic sequence, with mEos3.2 fused to the C terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2FPP
Plasmid#203758PurposeEncodes the membrane anchor of HRas, including the last 10 residues of the C terminus with 1 farnesylation and 2 palmitoylations, with mEos3.2 fused to the N terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceJuly 9, 2024AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2FP
Plasmid#203757PurposeEncodes the membrane anchor of NRas, including the last 10 residues of the C terminus with 1 farnesylation and 1 palmitoylation, with mEos3.2 fused to the N terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2GG
Plasmid#203756PurposeEncodes a modified version of the membrane anchor of KRas, including the last 16 residues of the C terminus, with mEos3.2 fused to the N terminus. The base pairs encoding the CAAX box for KRas were replaced by the CAAX box from rap1B, resulting in a geranylgeranylation instead of farnesylation. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 16, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trLAT-2P
Plasmid#203748PurposeEncodes the transmembrane domain from mouse LAT with mEos3.2 fused on the N terminus. Palmitoylation sites at C27 and C30 mutated to A. Used as a fluorescent plasma membrane probe.DepositorInserttrLAToC27AC30A (Lat Mouse)
TagsER translocation signal - mEos3.2ExpressionMammalianMutationC27A, C30AAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trCD4o
Plasmid#203751PurposeEncodes the transmembrane domain from CD4, including its 2 palmitoylation sites, with mEos3.2 fused on the N terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trLATo
Plasmid#203746PurposeEncodes the transmembrane domain from mouse LAT with mEos3.2 fused on the N terminus. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trLAT-P
Plasmid#203747PurposeEncodes the transmembrane domain from mouse LAT with mEos3.2 fused on the N terminus. The palmitoylation site at C27 is mutated to A. Used as a fluorescent plasma membrane probe.DepositorInserttrLAToC27A (Lat Mouse)
TagsER translocation signal - mEos3.2ExpressionMammalianMutationC27AAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
pCAG_Xph20-mEos3.2-CCR5TC
Plasmid#135532PurposeEncodes a specific PSD-95 binder (Xph20) fused to mEos3.2, CCR5 left-handed zinc finger, and KRAB(A) transcriptional repressor domainDepositorInsertXph20
TagsmEos3.2ExpressionMammalianPromoterCAGAvailable SinceApril 9, 2021AvailabilityAcademic Institutions and Nonprofits only -
trLATm1PtoLmEos3.2
Plasmid#203749PurposeEncodes the transmembrane domain from human LAT with mEos3.2 fused on the C terminus. Prolines P8 and P17 in the LAT transmembrane domain mutated to L. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2trLATm2allL+A
Plasmid#203750PurposeEncodes the transmembrane domain from human LAT with mEos3.2 fused on the C terminus. Residues within the transmembrane domain mutated to L and A to increase the TMD interfacial surface area with the membrane. Used as a fluorescent plasma membrane probe.DepositorAvailable SinceAug. 7, 2023AvailabilityAcademic Institutions and Nonprofits only -
mEos3.2-ER-5
Plasmid#57455PurposeLocalization: Endoplasmic Reticulum, Excitation: 507 / 572, Emission: 516 / 580DepositorAvailable SinceMarch 4, 2015AvailabilityIndustry, Academic Institutions, and Nonprofits