PELP1 Antibody [M14C23] | Primary Antibodies

Application: Reactivity: Human

Lane 1: 293T, Lane 2: T-47D, Lane 3: MCF7, Lane 4: Hela

Usage Information

Dilution
WB1:1000 IHC1:250 IF1:250 FCM1:300

Application
WB, IHC, IF, FCM

Reactivity
Human

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
120 kDa 160 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
PELP1 Antibody [M14C23] detects endogenous levels of total PELP1 protein.

Clone
M14C23

Synonym(s)
HMX3, MNAR, PELP1, Modulator of non-genomic activity of estrogen receptor, Transcription factor HMX3

Background
Proline‑, glutamic acid‑, and leucine‑rich protein 1 (PELP1), also termed MNAR, is a large multidomain scaffolding protein that functions as a transcriptional coregulator for multiple nuclear receptors and transcription factors and also serves as a cytoplasmic signaling adaptor linking steroid hormone receptors to kinase pathways. The protein contains numerous LXXLL nuclear receptor–interaction motifs, a histone‑binding region that recognizes specific histone tails and their modifications, and low‑complexity segments that support assembly into large chromatin and ribonucleoprotein complexes, allowing PELP1 to bridge steroid receptors, chromatin modifiers, and transcriptional machinery. Interaction with estrogen receptor alpha positions PELP1 as a coactivator that enhances estrogen‑dependent transcription by recruiting histone acetyltransferases and other chromatin‑remodeling activities to ER‑regulated promoters, while parallel interactions with glucocorticoid, progesterone, androgen, and orphan nuclear receptors place it as a broader coregulator that can act as either coactivator or corepressor depending on receptor and promoter context. In the cytoplasm, PELP1 associates with ER and growth factor receptors together with Src and PI3K, forming signaling modules that couple estrogen or growth factor stimulation to rapid activation of MAPK/ERK and PI3K/AKT pathways and thereby integrate hormonal cues with cell‑cycle entry, survival, and cytoskeletal reorganization. PELP1 acts as a core component of the 5FMC and related nucleolar complexes that participate in late steps of 28S rRNA processing and maturation of the 60S ribosomal subunit, regulating recruitment of the remodeling factor MDN1 and thereby influencing ribosome biogenesis and global translational capacity. Interactions with p53 place PELP1 as a p53 coactivator that modulates expression of p53 target genes during genotoxic stress, linking it to DNA damage response networks and apoptosis regulation. Expression of PELP1 is elevated in several hormone‑driven malignancies, including breast and prostate cancers, where its nuclear and cytoplasmic signaling functions correlate with enhanced proliferation, migration, and metastatic behavior, and with decreased sensitivity to endocrine therapies through promotion of ER/growth factor cross‑talk and activation of kinase pathways that support hormone‑independent receptor signaling.

Background

Proline‑, glutamic acid‑, and leucine‑rich protein 1 (PELP1), also termed MNAR, is a large multidomain scaffolding protein that functions as a transcriptional coregulator for multiple nuclear receptors and transcription factors and also serves as a cytoplasmic signaling adaptor linking steroid hormone receptors to kinase pathways. The protein contains numerous LXXLL nuclear receptor–interaction motifs, a histone‑binding region that recognizes specific histone tails and their modifications, and low‑complexity segments that support assembly into large chromatin and ribonucleoprotein complexes, allowing PELP1 to bridge steroid receptors, chromatin modifiers, and transcriptional machinery. Interaction with estrogen receptor alpha positions PELP1 as a coactivator that enhances estrogen‑dependent transcription by recruiting histone acetyltransferases and other chromatin‑remodeling activities to ER‑regulated promoters, while parallel interactions with glucocorticoid, progesterone, androgen, and orphan nuclear receptors place it as a broader coregulator that can act as either coactivator or corepressor depending on receptor and promoter context. In the cytoplasm, PELP1 associates with ER and growth factor receptors together with Src and PI3K, forming signaling modules that couple estrogen or growth factor stimulation to rapid activation of MAPK/ERK and PI3K/AKT pathways and thereby integrate hormonal cues with cell‑cycle entry, survival, and cytoskeletal reorganization. PELP1 acts as a core component of the 5FMC and related nucleolar complexes that participate in late steps of 28S rRNA processing and maturation of the 60S ribosomal subunit, regulating recruitment of the remodeling factor MDN1 and thereby influencing ribosome biogenesis and global translational capacity. Interactions with p53 place PELP1 as a p53 coactivator that modulates expression of p53 target genes during genotoxic stress, linking it to DNA damage response networks and apoptosis regulation. Expression of PELP1 is elevated in several hormone‑driven malignancies, including breast and prostate cancers, where its nuclear and cytoplasmic signaling functions correlate with enhanced proliferation, migration, and metastatic behavior, and with decreased sensitivity to endocrine therapies through promotion of ER/growth factor cross‑talk and activation of kinase pathways that support hormone‑independent receptor signaling.

References
https://pubmed.ncbi.nlm.nih.gov/26997260/ https://pubmed.ncbi.nlm.nih.gov/23933151/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%