PHB2 Antibody [P5A22] | Primary Antibodies

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:10000 - 1:50000 IHC1:8000 IF1:50 FCM1:70

Application
WB, IP, IF, FCM

Reactivity
Mouse, Rat, 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
33 kDa 33 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
PHB2 Antibody [P5A22] detects endogenous levels of total PHB2 protein.

Clone
P5A22

Synonym(s)
BAP, REA, PHB2, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity

Background
REA (repressor of estrogen receptor activity, also known as Prohibitin-2/PHB2 in this context) is a broadly expressed nuclear coregulator that associates with estrogen receptor α (ERα) and other nuclear receptors to modulate transcriptional responses to estradiol in a gene‑, tissue‑, and stage‑specific manner, acting predominantly as a brake on estrogen signaling in reproductive tissues and hormone‑responsive epithelia. The protein contains an N‑terminal coiled‑coil/PHB domain that supports oligomerization and interaction with other prohibitin-family members and chromatin regulators, and a C‑terminal region harboring nuclear receptor interaction motifs and sites for post‑translational modification that tune its affinity for ERα and its ability to recruit corepressor or coactivator complexes. REA binds ERα on chromatin and influences the composition of ER transcriptional complexes by constraining the recruitment of p160 coactivators and histone acetyltransferases and by favoring the assembly of complexes that include NCoR/SMRT and histone deacetylases, which diminishes estrogen‑induced histone acetylation and limits the amplitude and duration of ER target gene activation. Uterine studies using conditional and allelic series models show that partial reduction of REA enhances estrogen‑stimulated proliferation, increases expression of ERα target genes, and exaggerates uterine growth responses, whereas complete loss of REA impairs appropriate coordination of proliferation and differentiation and disrupts implantation, demonstrating a dosage‑dependent requirement for REA in setting the physiological window of ER responsiveness. REA also modulates cross‑talk between estrogen-responsive epithelial, stromal, and immune cell populations in the uterus: altered REA levels shift the balance of paracrine signaling factors and inflammatory mediators, changing the local microenvironment and influencing processes such as endometrial receptivity and decidualization. In the mammary gland, REA plays stage-specific roles, where appropriate corepressor activity constrains ductal growth during puberty and pregnancy, while partial loss of REA increases ER target gene expression and accelerates side-branching and alveologenesis, linking its coregulatory function to the architecture and differentiation of mammary epithelium. Dysregulated REA expression or function in breast cancer has been associated with altered ERα signaling output, where reduced REA levels correlate with heightened estrogen-driven transcription and increased proliferation, while maintenance of REA-mediated repression contributes to control of ER target genes implicated in tumor growth and endocrine response.

Background

REA (repressor of estrogen receptor activity, also known as Prohibitin-2/PHB2 in this context) is a broadly expressed nuclear coregulator that associates with estrogen receptor α (ERα) and other nuclear receptors to modulate transcriptional responses to estradiol in a gene‑, tissue‑, and stage‑specific manner, acting predominantly as a brake on estrogen signaling in reproductive tissues and hormone‑responsive epithelia. The protein contains an N‑terminal coiled‑coil/PHB domain that supports oligomerization and interaction with other prohibitin-family members and chromatin regulators, and a C‑terminal region harboring nuclear receptor interaction motifs and sites for post‑translational modification that tune its affinity for ERα and its ability to recruit corepressor or coactivator complexes. REA binds ERα on chromatin and influences the composition of ER transcriptional complexes by constraining the recruitment of p160 coactivators and histone acetyltransferases and by favoring the assembly of complexes that include NCoR/SMRT and histone deacetylases, which diminishes estrogen‑induced histone acetylation and limits the amplitude and duration of ER target gene activation. Uterine studies using conditional and allelic series models show that partial reduction of REA enhances estrogen‑stimulated proliferation, increases expression of ERα target genes, and exaggerates uterine growth responses, whereas complete loss of REA impairs appropriate coordination of proliferation and differentiation and disrupts implantation, demonstrating a dosage‑dependent requirement for REA in setting the physiological window of ER responsiveness. REA also modulates cross‑talk between estrogen-responsive epithelial, stromal, and immune cell populations in the uterus: altered REA levels shift the balance of paracrine signaling factors and inflammatory mediators, changing the local microenvironment and influencing processes such as endometrial receptivity and decidualization. In the mammary gland, REA plays stage-specific roles, where appropriate corepressor activity constrains ductal growth during puberty and pregnancy, while partial loss of REA increases ER target gene expression and accelerates side-branching and alveologenesis, linking its coregulatory function to the architecture and differentiation of mammary epithelium. Dysregulated REA expression or function in breast cancer has been associated with altered ERα signaling output, where reduced REA levels correlate with heightened estrogen-driven transcription and increased proliferation, while maintenance of REA-mediated repression contributes to control of ER target genes implicated in tumor growth and endocrine response.

References
https://pubmed.ncbi.nlm.nih.gov/21862609/ https://pubmed.ncbi.nlm.nih.gov/26653759/

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%