USP11 Antibody (N-term R41) Blocking Peptide
€363.00
In stock
SKU
AC-BP2139b
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 11, Deubiquitinating enzyme 11, Ubiquitin thioesterase 11, Ubiquitin-specific-processing protease 11, USP11, UHX1
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP2139b was selected from the N-term region of human USP11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: USP11
Primary Accession: P51784
Other Accession: Q8IUG6
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 11, Deubiquitinating enzyme 11, Ubiquitin thioesterase 11, Ubiquitin-specific-processing protease 11, USP11, UHX1
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP2139b was selected from the N-term region of human USP11 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: USP11
Primary Accession: P51784
Other Accession: Q8IUG6
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
| Is Featured? | No |
|---|
Write Your Own Review