Rac1 cDNA ORF Clone, Mouse, C-His tag

Cat: MG50789-CH
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Rac1 cDNA ORF Clone, Mouse, C-His tag 基本信息
基因
种属
Mouse
NCBI 参考序列号
参考序列ORF长度
579 bp
描述
Full length Clone DNA of Mouse RAS-related C3 botulinum substrate 1 with C terminal His tag.
质粒
启动子
Enhanced CMV promoter
载体
pCMV3-C-His
标签序列
His Tag Sequence: CACCATCACCACCATCATCACCACCATCAC
测序引物
T7( 5' TAATACGACTCACTATAGGG 3' )
BGH( 5' TAGAAGGCACAGTCGAGG 3' )
质控
The plasmid is confirmed by full-length sequencing.
筛选
抗生素(大肠杆菌)
Kanamycin
抗生素(哺乳动物细胞)
Hygromycin
应用
Stable or Transient mammalian expression
储存 & 运输
运输
Each tube contains lyophilized plasmid.
储存
The lyophilized plasmid can be stored at ambient temperature for three months.

**Sino Biological guarantees 100% sequence accuracy of all synthetic DNA constructs we deliver, but we do not guarantee protein expression in your experimental system. Protein expression is influenced by many factors that may vary between experiments or laboratories.**

Rac1 cDNA ORF Clone, Mouse, C-His tag Alternative Names
AL023026 cDNA ORF Clone, Mouse;D5Ertd559e cDNA ORF Clone, Mouse
Rac1 Background Information

RAC1 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins. Members of this superfamily appear to regulate a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization, and the activation of protein kinases. Two transcript variants encoding different isoforms have been found for RAC1 gene. RAC1 is a plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization and growth-factor induced formation of membrane ruffles. RAC1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophage. RAC1 is essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. RAC1's isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.

Stat3 is an important transcription factor that regulates both proinflammatory and anit-apoptotic pathways in the heart. It forms a multiprotein complex with RAC1 and PKC in an H/R-dependent manner by expression of constitutively active Rac1 mutant protein, and by RNA silencing of RAC1. Selective inhibition of PKC with calphostin C produces a marked suppression of Stat3 S727 phosphorylation. The association of Stat3 with Rax1 occurs predominantly at the cell membrane, but also inside the nucleus, and occurs through the binding of the coiled-coil domain of Stat3 to the 54 NH(2)-terminal residues of RAC1. Transfection with a peptide comprising the NH(2)-terminal 17 amino acid residues of RAC1-dependent signaling pathways resulting in physical association between Rac1 and Stat3 and the formation of a novel multiprotein complex with PKC.

Full Name
ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)
References
  • Kogai T, et al.. (2012) Regulation of sodium iodide symporter gene expression by Rac1/p38β mitogen-activated protein kinase signaling pathway in MCF-7 breast cancer cells. J Biol Chem. 287(5):3292-300.
  • Osborn-Heaford HL, et al. (2012) Mitochondrial Rac1 GTPase import and electron transfer from cytochrome c are required for pulmonary fibrosis. J Biol Chem. 287(5):3301-12.
  • Chang MH, et al. (2012) Prognostic role of integrin β1, E-cadherin, and rac1 expression in small cell lung cancer. APMIS. 120(1):28-38.
  • Osborn-Heaford HL, et al. (2012) Mitochondrial Rac1 GTPase import and electron transfer from cytochrome c are required for pulmonary fibrosis. J Biol Chem. 287(5):3301-12.
  • Mattagajasingh SN, et al. (2012) Activation of Stat3 in endothelial cells following hypoxia-reoxygenation is mediated by Rac1 and protein Kinase C. Biochim Biophys Acta. 1823(5):997-1006.
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