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Ubiquilin1 (PLIC1) Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9UMX0 |
|---|---|
| Clone Names | 3081809 |
| Gene ID | 29979 |
|---|---|
| Other Names | Ubiquilin-1, Protein linking IAP with cytoskeleton 1, PLIC-1, hPLIC-1, UBQLN1, DA41, PLIC1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2179c was selected from the Center region of human PLIC1 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | UBQLN1 |
|---|---|
| Synonyms | DA41, PLIC1 |
| Function | Plays an important role in the regulation of different protein degradation mechanisms and pathways including ubiquitin- proteasome system (UPS), autophagy and endoplasmic reticulum-associated protein degradation (ERAD) pathway. Mediates the proteasomal targeting of misfolded or accumulated proteins for degradation by binding (via UBA domain) to their polyubiquitin chains and by interacting (via ubiquitin-like domain) with the subunits of the proteasome (PubMed:15147878). Plays a role in the ERAD pathway via its interaction with ER-localized proteins UBXN4, VCP and HERPUD1 and may form a link between the polyubiquitinated ERAD substrates and the proteasome (PubMed:19822669, PubMed:18307982). Involved in the regulation of macroautophagy and autophagosome formation; required for maturation of autophagy-related protein LC3 from the cytosolic form LC3-I to the membrane-bound form LC3-II and may assist in the maturation of autophagosomes to autolysosomes by mediating autophagosome-lysosome fusion (PubMed:19148225, PubMed:20529957, PubMed:23459205). Negatively regulates the TICAM1/TRIF-dependent toll-like receptor signaling pathway by decreasing the abundance of TICAM1 via the autophagic pathway (PubMed:21695056). Promotes the ubiquitination and lysosomal degradation of ORAI1, consequently down-regulating the ORAI1-mediated Ca2+ mobilization (PubMed:23307288). Suppresses the maturation and proteasomal degradation of amyloid beta A4 protein (A4) by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays the maturation of A4 by sequestering it in the Golgi apparatus and preventing its transport to the cell surface for subsequent processing (By similarity). Ubiquitinates BCL2L10 and thereby stabilizes protein abundance (PubMed:22233804). |
| Cellular Location | Cytoplasm. Nucleus Endoplasmic reticulum. Cytoplasmic vesicle, autophagosome. Cell membrane Note=Detected in neuronal processes and at synapses (By similarity) Recruited to the ER during ER-associated protein degradation (ERAD) (PubMed:19822669). Isoform 1 and isoform 3 colocalize with PSEN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes (PubMed:21143716). Colocalizes with ORAI1 and TICAM1 in the autophagosome (PubMed:23307288, PubMed:21695056). Colocalizes with EPS15 and HGS in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments and with EPS15 also in aggresomes (PubMed:16159959). {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000269|PubMed:16159959, ECO:0000269|PubMed:19822669, ECO:0000269|PubMed:21143716, ECO:0000269|PubMed:21695056, ECO:0000269|PubMed:23307288} |
| Tissue Location | Brain (at protein level) (PubMed:18953672). Ubiquitous. Highly expressed throughout the brain; detected in neurons and in neuropathological lesions, such as neurofibrillary tangles and Lewy bodies. Highly expressed in heart, placenta, pancreas, lung, liver, skeletal muscle and kidney. |
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Provided below are standard protocols that you may find useful for product applications.
Background
PLIC1 is an ubiquitin-like protein (ubiquilin) that shares high degree of similarity with related products in yeast, rat and frog. Ubiquilins contain a N-terminal ubiquitin-like domain and a C-terminal ubiquitin-associated domain. They physically associate with both proteasomes and ubiquitin ligases, and thus are thought to functionally link the ubiquitination machinery to the proteasome to affect in vivo protein degradation. This ubiquilin has also been shown to modulate accumulation of presenilin proteins, and is found in lesions associated with Alzheimer's and Parkinson's disease.
References
Gao, L., et al., J. Virol. 77(7):4149-4159 (2003).Kleijnen, M.F., et al., Mol. Cell 6(2):409-419 (2000).Mah, A.L., et al., J. Cell Biol. 151(4):847-862 (2000).Hanaoka, E., et al., J. Hum. Genet. 45(3):188-191 (2000).
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