Product Pathways - Protein Folding
Phospho-DNAJC2/MPP11 (Ser47) Antibody #12397
|12397S||100 µl (10 western blots)||---||In Stock||---|
|12397||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||80||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Specificity / Sensitivity
Phospho-DNAJC2/MPP11 (Ser47) Antibody recognizes endogenous levels of DNAJC2/MPP11 protein only when phosphorylated at Ser47.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser47 of human and mouse DNAJC2/MPP11 protein. Antibodies are purified by protein A and peptide affinity chromatography.
DnaJ/Hsp40 proteins are a conserved family of J-domain-containing chaperone proteins that assist in protein folding and stability through their interactions with Hsp70 chaperone proteins (reviewed in 1). DNAJC2, also known as MPP11 (M-phase phosphoprotein 11 protein), is a component of the ribosome-associated complex (RAC). The RAC is localized to the cytoplasm, where it assists in maintaining appropriate folding of nascent polypeptides by stimulating the ATPase activity of Hsp70 chaperone proteins (2,3). In the nucleus, MPP11 is involved in the activation of transcription through mediation of the switch from polycomb-repressed to active chromatin (4). Previous studies have shown MPP11 is overexpressed in leukemia and head and neck cancer, leading researchers to suggest MPP11 may be a potential therapeutic target (5-7).
Phospho-DNAJC2/MPP11 (Ser47) Antibody is directed at a site that was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for modification site discovery. Please visit PhosphoSitePlus®, CST's modification site knowledgebase, at www.phosphosite.org for more information.
- Qiu, X.B. et al. (2006) Cell Mol Life Sci 63, 2560-70.
- Hundley, H.A. et al. (2005) Science 308, 1032-4.
- Otto, H. et al. (2005) Proc Natl Acad Sci U S A 102, 10064-9.
- Richly, H. et al. (2010) Nature 468, 1124-8.
- Greiner, J. et al. (2003) Int J Cancer 106, 224-31.
- Resto, V.A. et al. (2000) Cancer Res 60, 5529-35.
- Tabarkiewicz, J. and Giannopoulos, K. (2010) Transplant Proc 42, 3293-6.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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