eIF5A cDNA ORF Clone, Human, C-DDK (Flag®) tag

Cat: HG15096-CF
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eIF5A cDNA ORF Clone, Human, C-DDK (Flag®) tag 基本信息
基因
种属
Human
NCBI 参考序列号
参考序列ORF长度
465 bp
描述
Full length Clone DNA of Human eukaryotic translation initiation factor 5A with C terminal Flag tag.
质粒
启动子
Enhanced CMV promoter
载体
pCMV3-C-FLAG
标签序列
FLAG Tag Sequence: GATTACAAGGATGACGACGATAAG
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.**

eIF5A cDNA ORF Clone, Human, C-DDK (Flag®) tag Alternative Names
EIF-5A cDNA ORF Clone, Human;EIF5A1 cDNA ORF Clone, Human;eIF5AI cDNA ORF Clone, Human
eIF5A Background Information

EIF-5A, also known as EIF5, functions in start site selection as a GTPase accelerating protein (GAP) for the eukaryotic translation initiation factor (eIF) 2•GTP•tRNA ternary complex within the ribosome-bound pre-initiation complex. In protein synthesis initiation, eIF2 functions in its GTP-bound state to deliver initiator methionyl-tRNA to the small ribosomal subunit and is necessary for protein synthesis in all cells. EIF-5A stabilizes the binding of GDP to eIF2 and is therefore a bi-functional protein that acts as a GDP dissociation inhibitor (GDI). EIF-5A also interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 40S ribosome subunit.

Full Name
eukaryotic translation initiation factor 5A
References
  • Jenkins ZA. et al., 2001, Genomics. 71 (1): 101-9.
  • Guan XY. et al., 2001, Cancer Res. 61 (9): 3806-9.
  • Strausberg RL. et al., 2003, Proc Natl Acad Sci. 99 (26): 16899-903.
  • Clement PM. et al., 2003, Eur J Biochem. 270 (21): 4254-63.
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