Phospho-Myt1 (Ser83) Antibody

INQUIRY

CAT. NO.: AMA-0369

Target Information
UniProt ID	Q99640

Product Details
Size	20 µL/100 µL
Reactivity	Human
Storage	Store at -20°C. Do not aliquot the antibody.
Purification	Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser83 of human Myt1. Antibodies are purified by protein A and peptide affinity chromatography.

Usage
Application	WB
Product Usage Information Dilution	Western Blotting (1:1000)
MW (Target)	70 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 Plk1Although Akt has been shown to phosphorylate Asterina (starfish) Myt1 at a consensus Akt phosphorylation site the orthologous site, Ser83, in human Myt1 may be phosphorylated by a different kinase.

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 Plk1Although Akt has been shown to phosphorylate Asterina (starfish) Myt1 at a consensus Akt phosphorylation site the orthologous site, Ser83, in human Myt1 may be phosphorylated by a different kinase.

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