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Anti-Prohibitin Rabbit Antibody [A14G6]

Catalog No.: F2433

Application: Reactivity: Mouse, Rat, Human

Usage Information

Dilution
WB1:10000 - 1:20000 IP1:40 IHC1:100-1:500 IF1:100 FCM1:120

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse, Rat, Human

Source
Rabbit

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
30 kDa 30 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight.

Positive Control	Rat kidney; Human liver; Mouse kidney; Rat brain; Rat stomach; Rat liver; Mouse liver; Mouse stomach; Human kidney; Human hepatocellular tissue; Breast carcinoma; Placenta; NIH/3T3; MCF7; A431; HEK-293; HEK-293 T; Ramos; HepG2; HeLa
Negative Control

Datasheet & SDS

Biological Description

Specificity
Prohibitin Rabbit mAb detects endogenous levels of total Prohibitin protein.

Clone
A14G6

Synonym(s)
PHB, PHB1, Prohibitin 1

Background
Mitochondria are central regulators of both cell survival and cell death, maintaining the balance between pro- and anti-apoptotic signals while producing ATP through the oxidative phosphorylation (OXPHOS) pathway. Within mitochondria, prohibitin (PHB) proteins serve multiple essential functions. The first member, PHB1, was initially identified as an anti-proliferative protein in mammalian cells, whereas PHB2 was later discovered through its interaction with the IgM antigen receptor in complex with PHB1. PHB1 and PHB2 have molecular weights of approximately 32 kDa and 34 kDa, respectively. Both contain an N-terminal transmembrane domain, which belongs to an evolutionarily conserved prohibitin domain also present in other scaffold proteins such as stomatin, stomatin-like proteins (SLP1–3), flotillin, and HflK/C. Their C-terminal regions harbor coiled-coil domains that facilitate protein–protein interactions, including heterodimerization between PHB1 and PHB2 and binding to various transcriptional regulators. Dysregulation of PHBs has been linked to a wide spectrum of conditions, including aging, metabolic disorders, proliferative diseases, and degenerative pathologies. At the cellular level, depletion of PHB complexes impairs proliferation and heightens susceptibility to apoptosis. Subcellular localization studies reveal that PHB1 and PHB2 are distributed in the nucleus, mitochondria, and cytosol, and can also associate with certain membrane receptors. In the nucleus, PHBs function as transcriptional co-regulators by interacting with transcription factors, chromatin-modifying enzymes, cell-cycle proteins, and RNA-binding proteins. Within the cytoplasm, they engage with cytoskeletal transport proteins, signaling molecules, and membrane-associated receptors. PHBs are particularly abundant in cells with high energy requirements, which are especially vulnerable to mitochondrial dysfunction. Functionally, PHB proteins contribute to mitochondrial respiratory chain subunit turnover, OXPHOS complex assembly and activity, mitochondrial biogenesis, maintenance of mitochondrial networks, regulation of apoptosis, and mitophagy.

Background

Mitochondria are central regulators of both cell survival and cell death, maintaining the balance between pro- and anti-apoptotic signals while producing ATP through the oxidative phosphorylation (OXPHOS) pathway. Within mitochondria, prohibitin (PHB) proteins serve multiple essential functions. The first member, PHB1, was initially identified as an anti-proliferative protein in mammalian cells, whereas PHB2 was later discovered through its interaction with the IgM antigen receptor in complex with PHB1. PHB1 and PHB2 have molecular weights of approximately 32 kDa and 34 kDa, respectively. Both contain an N-terminal transmembrane domain, which belongs to an evolutionarily conserved prohibitin domain also present in other scaffold proteins such as stomatin, stomatin-like proteins (SLP1–3), flotillin, and HflK/C. Their C-terminal regions harbor coiled-coil domains that facilitate protein–protein interactions, including heterodimerization between PHB1 and PHB2 and binding to various transcriptional regulators. Dysregulation of PHBs has been linked to a wide spectrum of conditions, including aging, metabolic disorders, proliferative diseases, and degenerative pathologies. At the cellular level, depletion of PHB complexes impairs proliferation and heightens susceptibility to apoptosis. Subcellular localization studies reveal that PHB1 and PHB2 are distributed in the nucleus, mitochondria, and cytosol, and can also associate with certain membrane receptors. In the nucleus, PHBs function as transcriptional co-regulators by interacting with transcription factors, chromatin-modifying enzymes, cell-cycle proteins, and RNA-binding proteins. Within the cytoplasm, they engage with cytoskeletal transport proteins, signaling molecules, and membrane-associated receptors. PHBs are particularly abundant in cells with high energy requirements, which are especially vulnerable to mitochondrial dysfunction. Functionally, PHB proteins contribute to mitochondrial respiratory chain subunit turnover, OXPHOS complex assembly and activity, mitochondrial biogenesis, maintenance of mitochondrial networks, regulation of apoptosis, and mitophagy.

References
https://pubmed.ncbi.nlm.nih.gov/30669391/

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

Tech Support

Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

Handling Instructions

Tel: +1-832-582-8158 Ext:3
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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%