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Anti-Phosphothreonine

Art Nr.: SPC-154F, StressMarq
Biomol GmbH
Waidmannstr. 35
22769 HAMBURG
info@biomol.de
www.biomol.de
Tel:+49-40 - 85 32 600
0800 - 24 66 651 free call
Fax: +49-40 - 85 32 60-22
0800 - 24 66 652 free call
Product Name
Phosphothreonine Antibody
Catalog #
SPC-154F
Package size
400ul
 
N/A
View Conjugates
Bulk Quote
Type
Polyclonal
Datasheet
SPC 154 Phosphothreonine Cell Signaling
Description
Anti-Phosphothreonine
Research Area
Cell Signaling, Phosphorylation, Post-translational Modifications
Alternative Names
N/A
Clone Number
N/A
Host Species
Rabbit
Isotype
N/A
Immunogen
Phosphothreonine conjugated to KLH
Applications
WB, ELISA, IP
Species Reactivity
Species Independent
Accession Number
N/A
SwissProt
N/A
Background Info
Recognizes proteins phosphorylated on threonine residues. Does not cross-react with phosphotyrosine.
Recommended Dilutions
2 μg/mL (WB), 0.5 μg/mL (ELISA), 10 μg/mg (IP)
Form
Affinity Purified
Storage Buffer
PBS, 50% glycerol, 0.09% sodium azide
Concentration
250µg/mL
Certificate of Analysis
2μg/mL of SPC-154 was sufficient for detection of phosphorylation signal in western blot analysis using mouse spleen extract treated with Vanadium.
Storage Temp
-20°C
Shipping Temp
Blue Ice or 4°C

This antibody is available conjugated to several dyes. Please select one of the conjugates from the lists below or contact your distributor directly about these conjugation options:

ATTO Conjugates:

ATTO-Conjugates.pdf

Enzyme & Fluorescent Conjugates:

Enzyme-Fluorescent-Conjugate.pdf
Western blot analysis of mouse brain extract cells with rabbit anti-pT.  Left: Treated with Vanadium, Right: Non-treated.
Research Background
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).
References
1. Goto H. et al. (2005). Nature Cell Biology 8: 180-187. 2. Blume-Jensen P. and Hunter T. (2001). Nature 411: 355- 365. 3. Downward J. (2001). Nature 411: 759-762. 4. Pawson T. and Saxton T.M. (1999). Cell 97: 675-678. 5. Ostrovsky PC. (1995). Genes Dev. 9(16): 2034-2041.

This product is offered by Biomol for research purposes only. Not for diagnostic purposes or human use. It may not be resold or used to manufacture commercial products without written approval of Biomol GmbH.

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