Trim72 (NM_001079932) Mouse Tagged ORF Clone Lentiviral Particle
CAT#: MR226036L4V
- LentiORF®
Lenti ORF particles, Trim72 (GFP-tagged) - Mouse tripartite motif-containing 72 (Trim72), 200ul, >10^7 TU/mL
Lentiviral Particles: DDK DDK w/ Puro mGFP
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Specifications
Product Data | |
Type | Mouse Tagged ORF Clone Lentiviral Particle |
Tag | mGFP |
Symbol | Trim72 |
Synonyms | BC067209; MG53 |
Mammalian Cell Selection | Puromycin |
Vector | pLenti-C-mGFP-P2A-Puro |
ACCN | NM_001079932 |
ORF Size | 1434 bp |
Sequence Data |
The ORF insert of this clone is exactly the same as(MR226036).
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OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Reference Data | |
RefSeq | NM_001079932.3, NP_001073401.1 |
RefSeq Size | 2472 bp |
RefSeq ORF | 1434 bp |
Locus ID | 434246 |
UniProt ID | Q1XH17 |
Cytogenetics | 7 F3 |
Gene Summary | Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles.[UniProtKB/Swiss-Prot Function] |
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