LIMK1 peptide

Name: LIMK1 peptide
SKU: DAG-P1643
Rating: 5 (1 reviews)

Synthetic LIMK1 peptide

COA

SDS

Datasheet

Summary

Specificity

Highest expression in both adult and fetal nervous system. Detected ubiquitously throughout the different regions of adult brain, with highest levels in the cerebral cortex. Expressed to a lesser extent in heart and skeletal muscle.

Nature

Synthetic

Tag/Conjugate

Unconjugated

SequenceSimilarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.Contains 2 LIM zinc-binding domains.Contains 1 PDZ (DHR) domain.Contains 1 protein kinase domain.

Purity

70 - 90% by HPLC.

Format

Liquid

Preservative

None

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. Information available upon request.

Entrez Gene ID

3984

Antigen 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. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. This protein is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. This protein also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Feb 2011]

Function

ATP binding; heat shock protein binding; protein binding; protein heterodimerization activity; protein kinase activity; protein serine/threonine kinase activity; zinc ion binding;

Synonyms

LIMK1; LIM domain kinase 1; LIMK; LIMK-1; LIM motif-containing protein kinase;

Citations

Have you cited DAG-P1643 in a publication? Let us know and earn a reward for your research.

Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

SPARC-like1 mRNA is overexpressed in human uterine leiomyoma

MOLECULAR MEDICINE REPORTS

Authors: Mencalha, Andre Luiz; Levinsphul, Alexandre; Deterling, Louise Calil; Pizzatti, Luciana; Abdelhay, Eliana

Abstract

Uterine leiomyomas (ULs), also known as fibroids, are benign and monoclonal tumors frequently found in the female population. The genetic alterations that contribute to UL tumor development have not been well established, and the goal of this study was to reveal gene expression variation between ULs and healthy uterine tissue. We compared the gene expression profiles of 13 UL tumors with that of their adjacent normal tissue using the Differential Display mRNA assay (DDRT-PCR). Among the genes upregulated in some of the UL samples, several genes previously described in the context of cancer were identified, namely LIMK1, MCM3 and UHRF1. In addition, we identified a cDNA present in UL samples from distinct patients, which was absent from their normal tissue. Direct sequencing of this cDNA revealed a human SPARC-like] (SPARCL1) mRNA homology. Through semi-quantitative PCR, we demonstrated that SPARCL1 was upregulated in approximately 77% of UL samples, but was absent in normal tissue. Real-time PCR (QPCR) revealed that SPARCL1 expression was increased 5-fold in ULs compared to adjacent normal tissue. These results suggest that the SPARCL1 gene is involved in UL development.

Construction of a eukaryotic expression vector pEGFP-C1-BMP-2 and its effect on cell migration

JOURNAL OF ZHEJIANG UNIVERSITY-SCIENCE B

Authors: Wang, Xiao-ying; Chen, Zhong-hua; Zhang, Ru-yi; Liu, Sen-quan; Mei, Zhu; Yu, Ying-ying; Zhang, Xiong; Xia, Qiang; Ding, Yue-min

Abstract

Bone morphogenetic proteins (BMPs) are known to play an important role in bone and cartilage development. Recent research has shown that BMPs may induce tumorigenesis and promote tumor to spread, but the molecular mechanisms have not been elucidated. The aim of the present study was to investigate the regulatory function of BMP-2 in the migration of COS-7 cells and the underlying mechanisms. Human BMP-2 genetic fragment was amplified and introduced into the pEGFP-C1 vector. After being confirmed by XhoI and BamHI digestion analyses and DNA sequencing, the recombinant pEGFP-C1-BMP-2 plasmid was transfected into COS-7 cells. The influence of BMP-2 on cell migration and cofilin activity was detected by cell scratch assay and Western blotting. The recombinant pEGFP-C1-BMP-2 was effectively expressed in COS-7 cells. An increased phosphorylation of both LIMK1 and cofilin and an enhancement of cell migration were observed in cells with overexpression of BMP-2. A recombinant pEGFP-C1-BMP-2 vector was successfully constructed and overexpression of BMP-2 regulated the activities of the downstream molecules of the Rho GTPase signaling pathway, which might contribute to the enhancement of cell migration.