USP3 Antibody (N-term) Blocking Peptide
€363.00
In stock
SKU
AC-BP2132a
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.
Other Names:
Ubiquitin carboxyl-terminal hydrolase 3, Deubiquitinating enzyme 3, Ubiquitin thioesterase 3, Ubiquitin-specific-processing protease 3, USP3
Target/Specificity:
The synthetic peptide sequence is selected from aa 129~143 of human USP3.
Gene Name: USP3
Gene ID: 9960
Primary Accession: Q9Y6I4
Other Accession: UBP3_HUMAN
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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.
Other Names:
Ubiquitin carboxyl-terminal hydrolase 3, Deubiquitinating enzyme 3, Ubiquitin thioesterase 3, Ubiquitin-specific-processing protease 3, USP3
Target/Specificity:
The synthetic peptide sequence is selected from aa 129~143 of human USP3.
Gene Name: USP3
Gene ID: 9960
Primary Accession: Q9Y6I4
Other Accession: UBP3_HUMAN
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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