p19INK4d 蛋白, Human (His)

The p19INK4d protein, a potent inhibitor, strongly interacts with CDK4 and CDK6, effectively impeding their activity. Specifically interacting with CDK6, p19INK4d reinforces its role as a regulator of cyclin-dependent kinase activity. This crucial role in cell cycle regulation involves restraining CDK4 and CDK6 functions, contributing to the modulation of key cellular processes. p19INK4d Protein, Human (GST) is the recombinant human-derived p19INK4d protein, expressed by E. coli , with N-GST labeled tag. The total length of p19INK4d Protein, Human (GST) is 166 a.a., with molecular weight of ~46 kDa.

p19INK4d 蛋白通过与 CDK4 和 CDK6 强烈相互作用，充当有效的抑制剂，有效阻碍它们的活性。此外，p19INK4d 与 CDK6 特异性相互作用，增强其作为细胞周期蛋白依赖性激酶活性调节剂的作用。通过这些相互作用，p19INK4d 通过抑制 CDK4 和 CDK6 的功能，在细胞周期调节中发挥至关重要的作用，从而有助于关键细胞过程的调节。

Measured by its binding ability in a functional ELISA. When Recombinant human p19INK4d at 10 μg/mL (100 μL/well) can bind biotinylated human CDK4. The ED₅₀ for this effect is 0.9121 μg/mL.

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  Measured by its binding ability in a functional ELISA. When Recombinant human p19INK4d at 10 μg/ml (100 μL/well) can bind biotinylated human CDK4. The ED₅₀ for this effect is 0.9121 μg/mL.

Human

E. coli

N-6*His

P55273 (D10-L166)

1032  [NCBI]

DRLSGAAARGDVQEVRRLLHRELVHPDALNRFGKTALQVMMFGSTAIALELLKQGASPNVQDTSGTSPVHDAARTGFLDTLKVLVEHGADVNVPDGTGALPIHLAVQEGHTAVVSFLAAESDLHRRDARGLTPLELALQRGAQDLVDILQGHMVAPL

Approximately 19 kDa

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

无菌粉末

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.