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- Table of Contents
Designing a Western blot for VCP? The guide has the expected band size, antibodies backed by real blot images, the controls to run alongside, and protocols taken from published papers.
Open the VCP Western Blot GuideDesigning an IHC experiment for VCP? The guide has the expected staining pattern, antigen retrieval and fixation, antibodies backed by real IHC images, the tissue controls to run alongside, and protocols taken from published papers.
Open the VCP IHC Guide
1 Citations
Facts about Transitional endoplasmic reticulum ATPase.
Vesicle budding from the tER is an ATP-dependent procedure. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is essential for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome.
| Human | |
|---|---|
| Gene Name: | VCP |
| Uniprot: | P55072 |
| Entrez: | 7415 |

| Belongs to: |
|---|
| AAA ATPase family |

15S Mg(2+)-ATPase p97 subunit; IBMPFD; IBMPFDMGC8560; MGC131997; p97; TER ATPase; TERA; transitional endoplasmic reticulum ATPase; valosin containing protein; Valosin-containing proteinMGC148092; VCP; yeast Cdc48p homolog
Mass (kDA):
89.322 kDA

| Human | |
|---|---|
| Location: | 9p13.3 |
| Sequence: | 9; NC_000009.12 (35056064..35072668, complement) |
Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus. Cytoplasm, Stress granule. Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients (PubMed:15456787). Present in the Lewy bodies specifically found in neurons from Parkinson disease patients (PubMed:15456787). Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78 (PubMed:16168377). Following DNA double-strand breaks, recruited to the sites of damage (PubMed:22120668). Recruited to stalled replication forks via interaction with S






PMID: 8413590 by Pleasure I.T., et al. Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein.
PMID: 23349634 by Cloutier P., et al. A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.