PGD Protein, Human (HEK293, His)

PGD Protein, Human (HEK293, His) is a homodimeric protein, with an N-terminal His tag. Recombinant Human PGD, His (HEK293-expressed) is a key enzyme that converts 6-phosphogluconate into ribulose-5-phosphate with NADP⁺ as cofactor in the pentose phosphate pathway (PPP)^[1].

PGD is commonly upregulated and plays important roles in many human cancers, while the mechanism underlying such roles of PGD remains elusive. This phosphorylation enhances 6PGD activity by increasing its binding affinity to NADP⁺ and therefore activates the PPP for NADPH and ribose-5-phosphate, which consequently detoxifies intracellular reactive oxygen species (ROS) and accelerates DNA synthesis. In addition, 6PGD pY481 is associated with Fyn expression, the malignancy and prognosis of human glioblastoma. These findings establish a critical role of Fyn-dependent 6PGD phosphorylation in EGF-promoted tumor growth and radiation resistance^[1].

Human

HEK293

C-6*His

P52209 (M1-A483)

5226  [NCBI]

MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNAHHHHHH

Approximately 58.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Solution

Supplied as a 0.2 μm filter solution of 20 mM PB, 150 mM NaCl, pH 7.4.

<1 EU/μg, determined by LAL method.

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. Ruilong Liu, et al. Tyrosine Phosphorylation Activates 6-phosphogluconate Dehydrogenase and Promotes Tumor Growth and Radiation Resistance. Nat Commun. 2019 Mar 1;10(1):991.  [Content Brief]