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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.

Wee1 Antibody

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CAT. NO.: AMA-0413

Target Information
UniProt ID	P30291

Product Details
Size	100 µL
Reactivity	Human, Monkey
Storage	Store at -20°C. Do not aliquot the antibody.
Purification	Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino-terminus of human Wee1. Antibodies are purified by protein A and peptide affinity chromatography.

Usage
Application	WB, IP, F
Product Usage Information Dilution	Western Blotting (1:1000); Immunoprecipitation (1:50); Flow Cytometry (1:100)
MW (Target)	95 kDa

Background
Entry of all eukaryotic cells into mitosis is regulated by activation of cdc2 kinase. The critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Thr14 Phosphorylation at Tyr15 and Thr14 and inhibition of cdc2 is carried out by Wee1 and Myt1 protein kinases, while Tyr15 dephosphorylation and activation of cdc2 is carried out by the cdc25 phosphatase. Hyperphosphorylation and inactivation of Myt1 in mitosis suggests that one or more kinases activated at the G2/M transition negatively regulates Myt1 activity. Kinases shown to phosphorylate Myt1 include cdc2, p90RSK, Akt, and Plk1Wee1 is inactivated upon mitotic entry by phosphorylation at Ser53 and Ser123 by Plk1 and cdc2, followed by beta-TrCP-mediated ubiquitination and degradation.

Background

Entry of all eukaryotic cells into mitosis is regulated by activation of cdc2 kinase. The critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Thr14 Phosphorylation at Tyr15 and Thr14 and inhibition of cdc2 is carried out by Wee1 and Myt1 protein kinases, while Tyr15 dephosphorylation and activation of cdc2 is carried out by the cdc25 phosphatase. Hyperphosphorylation and inactivation of Myt1 in mitosis suggests that one or more kinases activated at the G2/M transition negatively regulates Myt1 activity. Kinases shown to phosphorylate Myt1 include cdc2, p90RSK, Akt, and Plk1Wee1 is inactivated upon mitotic entry by phosphorylation at Ser53 and Ser123 by Plk1 and cdc2, followed by beta-TrCP-mediated ubiquitination and degradation.

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All of our services and products are intended for preclinical research use only and cannot be used to diagnose, treat or manage patients.