C14orf151 (INF2) (NM_022489) Human Tagged ORF Clone Lentiviral Particle
CAT#: RC216716L3V
- LentiORF®
Lenti ORF particles, INF2 (Myc-DDK-tagged)-Human inverted formin, FH2 and WH2 domain containing (INF2), transcript variant 1, 200ul, >10^7 TU/mL
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CNY 20,900.00
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规格
Cited in 2 publications. |
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经常一起买 (3)
Specifications
Product Data | |
Product Name | C14orf151 (INF2) (NM_022489) Human Tagged ORF Clone Lentiviral Particle |
Synonyms | C14orf151; C14orf173; CMTDIE; FSGS5; pp9484 |
Vector | pLenti-C-Myc-DDK-P2A-Puro |
ACCN | NM_022489 |
ORF Size | 3747 bp |
Sequence Data |
The ORF insert of this clone is exactly the same as(RC216716).
|
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_022489.3, NP_071934.3 |
RefSeq Size | 4725 bp |
RefSeq ORF | 3750 bp |
Locus ID | 64423 |
Domains | WH2 |
Protein Families | Druggable Genome |
MW | 135.4 kDa |
Gene Summary | This gene represents a member of the formin family of proteins. It is considered a diaphanous formin due to the presence of a diaphanous inhibitory domain located at the N-terminus of the encoded protein. Studies of a similar mouse protein indicate that the protein encoded by this locus may function in polymerization and depolymerization of actin filaments. Mutations at this locus have been associated with focal segmental glomerulosclerosis 5.[provided by RefSeq, Aug 2010] |
Citations (2)
The use of this cDNA Clones has been cited in the following citations: |
---|
Actin Monomers Activate Inverted Formin 2 by Competing with Its Autoinhibitory Interaction *
,null,
The Journal of Biological Chemistry
,PubMed ID 23921379
[INF2]
|
Mutations to the Formin Homology 2 Domain of INF2 Protein Have Unexpected Effects on Actin Polymerization and Severing *
,null,
The Journal of Biological Chemistry
,PubMed ID 22879592
[INF2]
|
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