Mical1 (GeneName), [F-actin]-monooxygenase MICAL1 (ProteinName), MICA1_RAT.
Rat Mical1/ [F-actin]-monooxygenase MICAL1 ELISA Kit
Molecule interacting with CasL protein 1, MICAL-1
Natural and recombinant rat [F-actin]-monooxygenase MICAL1
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Interacts with STK38 and STK38L. Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B, RAB8A, RAB10, RAB13 and RAB15 (in their GTP-bound forms); binding to RAB1B is of low affinity compared to other Rab proteins; at least in case of RAB8A and RAB10 can bind 2 molecules of the Rab proteins simultaneously.
Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of secretory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels. May act as Rab effector protein and play a role in vesicle trafficking.
Cytoplasm Cytoplasm Cytoskeleton
MASPTSTNPA | HDHFETFVQA | QLCQDVLSSF | QGLCRALGVE | SGGGLPQYHK |
IKAQLNYWSA | KSLWAKLDK | RASQPAYQQG | QACTNTKCLV | VGAGPCGLRA |
AVELALLGAR | VVLVEKRTKF | S RHNVLHLW | PFTIHDLRAL | GAKKFYGRFC |
TGTLDHISIR | QLQLLLLKVA | LLLGVEIHWG | FT FTGLQPP | PKKGSGWRAR |
IQPSPPAQLA | SYEFDVLISA | GGGKFVPEGF | TIREMRGKLA | IGI TANFVN |
GRTVEETQVP | EISGVARIYN | QKFFQSLLKA | TGIDLENIVY | YKDDTHYFVM |
TAKK QCLLR | LGVLRQDLPE | TDQLLGKANV | VPEALQQFAR | AAADFATQGK |
LGKLEFAQDA | RGRPD VAAF | DFTSMMRSES | SARIQEKHGA | RLLLGLVGDC |
LVEPFWPLGT | GVARGFLAAF | DAAWMV KRW | AEGTGPLELL | AERESLYQLL |
SQTSPENMHR | NVAQYGLDPA | TRYPNLNLRA | VTPNQVQ DL | YDIMDKEHAR |
KKSDETDARK | TTTGSAGTEE | LLHWCQEQTA | GFPGVSVTDF | SSSWADGR A |
LCALVHRLQP | GLLEPSELQG | MSALEATAWA | LRVAEYELGI | IPVLSAQAVV |
AGSDPLGLI | AYLSHFHSAF | KNTPHSSGLV | SQPHGTPSAI | LFLGKLQRSL |
QRTRTKVEEE | TPCTEEPPVS | EPSVPPALP | SEHEEAGAED | VCELCGKRLY |
ILERFCVDGH | FFHRGCFCCR | TCEATLRPGG | Y GQYPGDGY | FYCLQHLPQE |
DQKEADNNGS | PENQELPTPG | DSTTQSGPSS | PVPPVTEASP | VP SPSQPAR |
RLIRLSSVER | LRLSSLNIIP | DSGVEPPPKP | PRSCLDLAQE | SLKSSFMGWG |
VLR APQVPE | AIEKGEEEEE | EEEEEEEEEE | ELPPPLALEV | EQSLLTLAKN |
SGDMTKYPTW | RRTL MRRAK | EEEMKRFCKA | QAIQRRLNEI | EAAMRELETE |
GMKLEVALRK | ESSSPEKQKK | LWLEQ LLQL | IQKKNSLVTE | EAELMITVQE |
LDLEEKQRQL | DHEFRGINRE | ETLKTQADRL | SEDRVL RKL | LDVVNQRDAL |
IQFQEERRLR | EMPV
This product has not yet been referenced specifically in any publications.
"MICAL, a novel CasL interacting molecule, associates with vimentin."
"Oxidation of F-actin controls the terminal steps of cytokinesis."
"Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains."
"Redox modification of nuclear actin by MICAL-2 regulates SRF signaling."
"Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1."
"Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study."
"Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein."
"Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain."
"Solution structure of calponin homology domain of Human MICAL-1."
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
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