PHB

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For Research Use Only. Not For Clinical Use.


Background

A highly conserved protein primarily localized to the inner mitochondrial membrane. It functions as a molecular chaperone to stabilize mitochondrial proteins and maintain cristae structure. It also plays roles in cell cycle regulation, apoptosis, and serves as a putative tumor suppressor.
Protein class

Plasma proteins

Predicted location

Intracellular

Single cell type specificity

Cell type enhanced (Proximal tubular cells)

Immune cell specificity

Low immune cell specificity

Cell line specificity

Cell line enhanced (CACO-2)

Interaction

The mitochondrial prohibitin complex consists of two subunits (PHB1 and PHB2), assembled into a membrane-associated ring-shaped supercomplex of approximately 1 mDa (PubMed:11302691, 20959514, 28017329, 31522117). Interacts with STOML2 (PubMed:21746876). Interacts with MAP1LC3B (membrane-bound form LC3-II); the interaction requires PHB2 and takes place upon Parkin-mediated mitochondrial damage (PubMed:28017329). Interacts with STAT3 (unphosphorylated or phosphorylated at 'Ser-727') (PubMed:31899195). Interacts with CLPB (PubMed:31522117). Interacts with CD86 (via cytoplasmic domain); the interactions increases after priming with CD40 (By similarity). (Microbial infection) Interacts with SARS coronavirus/SARS-CoV nsp2 protein. (Microbial infection) Interacts with chikungunya virus spike glycoprotein E2. (Microbial infection) Interaction with human immunodeficiency virus type 1/HIV-1 envelope glycoprotein GP160. (Microbial infection) Interacts with human enterovirus 71/EV-71 capsid protein VP0, protein 3CD and protease 3C.

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