PAH cDNA ORF Clone, Human, C-HA tag

Cat: HG12081-CY
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PAH cDNA ORF Clone, Human, C-HA tag 基本信息
基因
种属
Human
NCBI 参考序列号
参考序列ORF长度
1359 bp
序列描述
Identical with the Gene Bank Ref. ID sequence except for the point mutations: 696 A/G, 735 G/A not causing the amino acid variation.
描述
Full length Clone DNA of Human phenylalanine hydroxylase with C terminal HA tag.
质粒
启动子
Enhanced CMV promoter
载体
pCMV3-C-HA
限制性酶切位点
KpnI + NotI (6kb + 1.4kb)
标签序列
HA Tag Sequence: TATCCTTACGACGTGCCTGACTACGCC
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.
PAH cDNA ORF 核苷酸序列及氨基酸序列信息

**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.**

PAH cDNA ORF Clone, Human, C-HA tag Validated Images
Rhesus TLR4 / TLR-4 Gene Plasmid Map 5626
PAH cDNA ORF Clone, Human, C-HA tag Alternative Names
PH cDNA ORF Clone, Human;PKU cDNA ORF Clone, Human;PKU1 cDNA ORF Clone, Human
PAH Background Information

PAH (phenylalanine hydroxylase), also known as PH, belongs to the biopterin-dependent aromatic amino acid hydroxylase family. It contains 1 ACT domain, N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule. In humans, PAH is expressed both in the liver and the kidney, and there is some indication that it may be differentially regulated in these tissues. PAH catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. It is one of three members of the pterin-dependent amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin and a non-heme iron for catalysis. Defects in PAH are the cause of phenylketonuria (PKU). PKU is an autosomal recessive inborn error of phenylalanine metabolism, due to severe phenylalanine hydroxylase deficiency. It is characterized by blood concentrations of phenylalanine persistently above 1200 mumol.

Full Name
phenylalanine hydroxylase
References
  • Fitzpatrick PF, et al. (1999) Tetrahydropterin-dependent amino acid hydroxylases. Annu Rev Biochem. 68:355-81.
  • Olsson E, et al. (2011) Formation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases. Chemistry. 17(13):3746-58.
  • Bassan A, et al. (2003) Mechanism of aromatic hydroxylation by an activated FeIVO core in tetrahydrobiopterin-dependent hydroxylases. Chemistry. 9(17):4055-67.
  • Panay AJ, et al. (2011) Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. Biochemistry. 50(11):1928-33.
  • Bassan A, et al. (2003) Mechanism of dioxygen cleavage in tetrahydrobiopterin-dependent amino acid hydroxylases. Chemistry. 9(1):106-15.
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