Actn4 (GeneName), Alpha-actinin-4 (ProteinName), ACTN4_MOUSE.
Mouse Actn4/ Alpha-actinin-4 ELISA Kit
Non-muscle alpha-actinin 4
Natural and recombinant mouse Alpha-actinin-4
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Homodimer; antiparallel (By similarity). Interacts with BAIAP1 and PDLIM2 (By similarity). Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Binds TRIM3 at the N-terminus. Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation. Interacts with PPARG and RARA (By similarity). Binds to VCL; this interaction triggers VCL conformational changes.
F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (PubMed:18332111). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA.
Nucleus Cytoplasm Cell junction Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers.
MVDYHAANQA | YQYGPNSGGG | NGAGGGGSMG | DYMAQEDDWD | RDLLLDPAWE |
KQQRKTFTAW | CNSHLRKAGT | QIENIDEDFR | DGLKLMLLLE | VISGERLPKP |
ERGKMRVHKI | NNVNKALDFI | ASKGVKLVSI | GAEEIVDGNA | KMTLGMIWTI |
ILRFAIQDIS | VEETSAKEGL | LLWCQRKTAP | YKNVNVQNFH | ISWKDGLAFN |
ALIHRHRPEL | IEYDKLRKDD | PVTNLNNAFE | VAEKYLDIPK | MLDAEDIVNT |
ARPDEKAIMT | YVSSFYHAFS | GAQKAETAAN | RICKVLAVNQ | ENEHLMEDYE |
RLASDLLEWI | RRTIPWLEDR | VPQKTIQEMQ | QKLEDFRDYR | RVHKPPKVQE |
KCQLEINFNT | LQTKLRLSNR | PAFMPSEGRM | VSDINNGWQH | LEQAEKGYEE |
WLLNEIRRLE | RLDHLAEKFR | QKASIHEAWT | DGKEAMLKQR | DYETATLSDI |
KALIRKHEAF | ESDLAAHQDR | VEQIAAIAQE | LNELDYYDSH | NVNTRCQKIC |
DQWDNLGSLT | HSRREALEKT | EKQLETIDQL | HLEYAKRAAP | FNNWMESAME |
DLQDMFIVHT | IEEIEGLISA | HDQFKSTLPD | ADREREAILA | IHKEAQRIAE |
SNHIKLSGSN | PYTTVTPQII | NSKWEKVQQL | VPKRDHALLE | EQSKQQSNEH |
LRRQFASQAN | MVGPWIQTKM | EEIGRISIEM | NGTLEDQLSH | LKQYERSIVD |
YKPSLDLLEQ | QHQLIQEALI | FDNKHTNYTM | EHIRVGWEQL | LTTIARTINE |
VENQILTRDA | KGISQEQMQE | FRASFNHFDK | DHGGALGPEE | FKACLISLGY |
DVENDRQGDA | EFNRIMSVVD | PNHSGLVTFQ | AFIDFMSRET | TDTDTADQVI |
ASFKVLAGDK | NFITAEELRR | ELPPDQAEYC | IARMAPYQGP | DAAPGALDYK |
SFSTALYGES | DL
This product has not yet been referenced specifically in any publications.
"Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis."
"ACTN4 gene mutations and single nucleotide polymorphisms in idiopathic focal segmental glomerulosclerosis."
"Association analysis of podocyte slit diaphragm genes as candidates for diabetic nephropathy."
"Crystal structure of the actin-binding domain of alpha-actinin-4 Lys255Glu mutant implicated in focal segmental glomerulosclerosis."
"Familial focal segmental glomerulosclerosis associated with an ACTN4 mutation and paternal germline mosaicism."
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