| Description : |
There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. The protein encoded by this gene is phosphorylated and activated by ROCK, a downstream effector of Rho, and the encoded protein, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the actin cytoskeleton. At least three transcript variants encoding different isoforms have been found for this gene. |
| Source : |
HEK293 |
| Species : |
Human |
| Tag : |
Myc/DDK |
| Molecular Mass : |
69.7 kDa |
| AA Sequence : |
MGSYLSVPAYFTSRDLFRCSECQDS LTNWYYEKDGKLYCPKDYWGKFGEF CHGCSLLMTGPFMVAGEFKYHPECF ACMSCKVIIEDGDAYALVQHATLYC GKCHNEVVLAPMFERLSTESVQEQL PYSVTLISMPATTEGRRGFSVSVES ACSNYATTVQVKEVNRMHISPNNRN AIHPGDRILEINGTPVRTLRVEEVE DAISQTSQTLQLLIEHDPVSQRLDQ LRLEARLAPHMQNAGHPHALSTLDT KENLEGTLRRRSLRRSNSISKSPGP SSPKEPLLFSRDISRSESLRCSSSY SQQIFRPCDLIHGEVLGKGFFGQAI KVTHKATGKVMVMKELIRCDEETQK TFLTEVKVMRSLDHPNVLKFIGVLY KDKKLNLLTEYIEGGTLKDFLRSMD PFPWQQKVRFAKGIASGMAYLHSMC IIHRDLNSHNCLIKLDKTVVVADFG LSRLIVEERKRAPMEKATTKKRTLR KNDRKKRYTVVGNPYWMAPEMLNGK SYDETVDIFSFGIVLCEIIGQVYAD PDCLPRTLDFGLNVKLFWEKFVPTD CPPAFFPLAAICCRLEPESRPAFSK LEDSFEALSLYLGELGIPLPAELEE LDHTVSMQYGLTRDSPPTRTRPLEQ KLISEEDLAANDILDYKDDDDKV |
| Purity : |
> 80% as determined by SDS-PAGE and Coomassie blue staining |
| Stability : |
Stable for 3 months from receipt of products under proper storage and handling conditions. |
| Storage : |
Store at -80 centigrade. Avoid repeated freeze-thaw cycles. |
| Concentration : |
50 μg/mL as determined by BCA |
| Storage Buffer : |
100 mM glycine, 25 mM Tris-HCl, pH 7.3. |
