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Phosphothreonine antibody (HRP)

Antigen

Phosphothreonine

Clonality Polyclonal
Host
Alternatives

Rabbit

Reactivity
Alternatives

All Species

Conjugate
Application
Alternatives Western Blotting (WB), ELISA
5 references available
Catalog no. ABIN361681
Quantity 400myl  (250µg/mL)
Price 390.00 $   Plus shipping costs $35.00
Shipping to
Availability Ships within 7 to 10 Business Days

Additional Information

Characteristics Recognizes proteins phosphorylated on threonine residues. Does not cross-react with phosphotyrosine.
Immunogen Phosphothreonine conjugated to KLH
Format Liquid
Description Protein phosphorylation is an important posttranslational modification that serves many key functions to regulate a protein’s activity, localization, and protein-protein interactions. Phosphorylation is catalyzed by various specific protein kinases, which involves removing a phosphate group from ATP and covalently attaching it to to a recipient protein that acts as a substrate. Most kinases act on both serine and threonine, others act on tyrosine, and a number (dual specificity kinases) act on all three. Because phosphorylation can occur at multiple sites on any given protein, it can therefore change the function or localization of that protein at any time (1). Changing the function of these proteins has been linked to a number of diseases, including cancer, diabetes, heart disease, inflammation and neurological disorders (2-4).
Specificity Recognizes proteins phosphorylated on threonine residues. Slightly cross-reacts with phosphoserine but does not cross-react with phosphotyrosine. Species cross-reactivity: Species Independent.

Application Details

Application Notes 1:500 (WB), 1:1000 (ELISA)
Concentration 250µg/mL
Purity Affinity Purified.
Buffer PBS, 50% glycerol, 0.09% sodium azide
Storage -20 °C
Storage Shipping Temp Max Blue Ice or 4 °C
Research Area Cell Signaling
Restrictions For Research Use only

Publications

Publications Ostrovsky, Maloy: "Protein phosphorylation on serine, threonine, and tyrosine residues modulates membrane-protein interactions and transcriptional regulation in Salmonella typhimurium." in: Genes & development, Vol. 9, Issue 16, pp. 2034-41, 1995 (PubMed).

Pawson, Saxton: "Signaling networks--do all roads lead to the same genes?" in: Cell, Vol. 97, Issue 6, pp. 675-8, 1999 (PubMed).

Blume-Jensen, Hunter: "Oncogenic kinase signalling." in: Nature, Vol. 411, Issue 6835, pp. 355-65, 2001 (PubMed).

Downward: "The ins and outs of signalling." in: Nature, Vol. 411, Issue 6839, pp. 759-62, 2001 (PubMed).

Goto, Kiyono, Tomono et al.: "Complex formation of Plk1 and INCENP required for metaphase-anaphase transition." in: Nature cell biology, Vol. 8, Issue 2, pp. 180-7, 2006 (PubMed).