Product Pathways - Nuclear Receptor Signaling
PELP1 (D5Q4W) Rabbit mAb #96986
|96986S||100 µl ( 10 western blots )||￥3,100.00 现货查询||购买询价|
|96986||carrier free & custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation, IHC-P=Immunohistochemistry (Paraffin),
Specificity / Sensitivity
PELP1 (D5Q4W) Rabbit mAb recognizes endogenous levels of total PELP1 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly966 of human PELP1 protein.
Western blot analysis of extracts from various cell lines using PELP1 (D5Q4W) Rabbit mAb.
Immunoprecipitation of PELP1 from SW620 cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is PELP1 (D5Q4W) Rabbit mAb. Western blot analysis was performed using PELP1 (D5Q4W) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human colon carcinoma using PELP1 (D5Q4W) Rabbit mAb.
Immunohistochemical analysis of paraffin-embedded human ovarian carcinoma using PELP1 (D5Q4W) Rabbit mAb.
The transcription factor proline, glutamic acid, and leucine rich protein 1 (PELP1, MNAR) mediates cell signaling through direct interaction with hormone nuclear receptors to regulate target gene transcription. This versatile protein also regulates gene expression by participating in chromatin remodeling, and acts as a cytoplasmic scaffold protein to mediate growth factor and hormone signaling (1). Following its original description as an estrogen receptor α (ERα) coactivator (2), additional research showed that PELP1 corepresses multiple nuclear hormone receptors and transcriptional regulators, including progesterone receptor, glucocorticoid receptor, AP1, and Stat3 (3). PELP1 also acts cooperatively with the secondary coactivator CARM1 at ERα target gene promoters to increase ERα-mediated transactivation (4). The PELP1 protein contains several leucine-rich repeats, important for interaction with nuclear receptors, and a carboxy-terminal glutamic acid-rich domain responsible for histone protein interaction (2). The glutamic acid-rich region of PELP1 binds to hypoacetylated histones H3 and H4 to block interaction between histone proteins and acetyltransferases. This interaction maintains histones in a hypoacetylated state and suppresses serum-response gene activation. Interaction between PELP1 and ERα relieves this repression and promotes acetylation of histone proteins (3).
Research studies demonstrate altered regulation of PELP1 in several distinct hormone-dependent cancers, such as ovarian, breast, and prostate cancers (5-7). As a result, PELP1 may be a promising prognostic marker for hormone-dependent cancers, and inhibiting PELP1 expression or activity may prove beneficial in disrupting hormonal cancer initiation, progression, and metastasis (8).
- Girard, B.J. et al. (2014) Mol Cell Endocrinol 382, 642-51.
- Vadlamudi, R.K. et al. (2001) J Biol Chem 276, 38272-9.
- Choi, Y.B. et al. (2004) J Biol Chem 279, 50930-41.
- Mann, M. et al. (2013) Carcinogenesis 34, 1468-75.
- Dimple, C. et al. (2008) Cancer Res 68, 4902-9.
- Vadlamudi, R.K. et al. (2005) Cancer Res 65, 7724-32.
- Nair, S.S. et al. (2007) Mol Endocrinol 21, 613-24.
- Chakravarty, D. et al. (2010) IUBMB Life 62, 162-9.
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
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- 9999 Nonfat Dry Milk
For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
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SignalStain is a trademark of Cell Signaling Technology, Inc.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
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