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USP8 Antibody (C-term C1072) (Ascites)
Mouse Monoclonal Antibody (Mab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P40818 |
| Other Accession | Q80U87, NP_001122082.1 |
| Reactivity | Human |
| Predicted | Mouse |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Clone/Animal Names | 460CT35.1.6 |
| Calculated MW | 127523 Da |
| Antigen Region | 1-30 aa |
| Gene ID | 9101 |
|---|---|
| Other Names | Ubiquitin carboxyl-terminal hydrolase 8, Deubiquitinating enzyme 8, Ubiquitin isopeptidase Y, hUBPy, Ubiquitin thioesterase 8, Ubiquitin-specific-processing protease 8, USP8, KIAA0055, UBPY |
| Target/Specificity | This USP8 antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the C-terminal region of human USP8. |
| Dilution | WB~~1:500~4000 |
| Format | Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | USP8 Antibody (C-term C1072) (Ascites) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | USP8 (HGNC:12631) |
|---|---|
| Synonyms | KIAA0055, UBPY |
| Function | Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controls tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (PubMed:27302062). |
| Cellular Location | Cytoplasm. Nucleus {ECO:0000250|UniProtKB:Q80U87} Endosome membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein |
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Provided below are standard protocols that you may find useful for product applications.
Background
Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules.
References
Hasdemir, B., et al. J. Biol. Chem. 284(41):28453-28466(2009)
Row, P.E., et al. J. Biol. Chem. 282(42):30929-30937(2007)
Alwan, H.A., et al. J. Biol. Chem. 282(3):1658-1669(2007)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Avvakumov, G.V., et al. J. Biol. Chem. 281(49):38061-38070(2006)
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