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USP16 Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | Q9Y5T5 |
| Other Accession | NP_006438 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 93570 Da |
| Antigen Region | 386-416 aa |
| Gene ID | 10600 |
|---|---|
| Other Names | Ubiquitin carboxyl-terminal hydrolase 16 {ECO:0000255|HAMAP-Rule:MF_03062}, 341912 {ECO:0000255|HAMAP-Rule:MF_03062}, Deubiquitinating enzyme 16 {ECO:0000255|HAMAP-Rule:MF_03062}, Ubiquitin thioesterase 16 {ECO:0000255|HAMAP-Rule:MF_03062}, Ubiquitin-processing protease UBP-M, Ubiquitin-specific-processing protease 16 {ECO:0000255|HAMAP-Rule:MF_03062}, USP16 {ECO:0000255|HAMAP-Rule:MF_03062} |
| Target/Specificity | This USP16 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 386-416 amino acids from the Central region of human USP16. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| 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 | USP16 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | USP16 {ECO:0000255|HAMAP-Rule:MF_03062} |
|---|---|
| Function | Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator (PubMed:17914355). Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser- 11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis (PubMed:17914355). In resting B- and T- lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination (PubMed:17914355). Prefers nucleosomal substrates (PubMed:17914355). Does not deubiquitinate histone H2B (PubMed:17914355). Also deubiquitinates non- histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit (PubMed:32129764). Also mediates deubiquitination of tektin proteins (TEKT1, TEKT2, TEK3, TEKT4 and TEKT5), promoting their stability. |
| Cellular Location | Nucleus. Cytoplasm |
| Tissue Location | Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas |
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Provided below are standard protocols that you may find useful for product applications.
Background
Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.
References
Puente, X.S., et al., Nat. Rev. Genet. 4(7):544-558 (2003).
Cai, S.Y., et al., Proc. Natl. Acad. Sci. U.S.A. 96(6):2828-2833 (1999).
D'Andrea, A., et al., Crit. Rev. Biochem. Mol. Biol. 33(5):337-352 (1998).
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