Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Aufreinigung
This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
This USP5 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 59-90 amino acids from the N-terminal region of human USP5.
USP5
Reaktivität: Human
ELISA
Wirt: Kaninchen
Polyclonal
Biotin
Applikationshinweise
WB: 1:1000. IHC-P: 1:50~100
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Haltbarkeit
6 months
Yoshioka, Ye, Okada, Taniguchi, Yoshida, Sugaya, Onose, Koshino, Takahashi, Yajima, Yajima, Abe: "Ubiquitin-specific peptidase 5, a target molecule of vialinin A, is a key molecule of TNF-α production in RBL-2H3 cells." in: PLoS ONE, Vol. 8, Issue 12, pp. e80931, (2013) (PubMed).
Ouyang, Ali, Ravichandran, Dong, Qiu, MacKenzie, Dhe-Paganon, Arrowsmith, Zhai: "Protein aggregates are recruited to aggresome by histone deacetylase 6 via unanchored ubiquitin C termini." in: The Journal of biological chemistry, Vol. 287, Issue 4, pp. 2317-27, (2012) (PubMed).
Falquet, Paquet, Frutiger, Hughes, Hoang-Van, Jaton: "cDNA cloning of a human 100 kDa de-ubiquitinating enzyme: the 100 kDa human de-ubiquitinase belongs to the ubiquitin C-terminal hydrolase family 2 (UCH2)." in: FEBS letters, Vol. 376, Issue 3, pp. 233-7, (1996) (PubMed).
Falquet, Paquet, Frutiger, Hughes, Hoang-Van, Jaton: "A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro." in: FEBS letters, Vol. 359, Issue 1, pp. 73-7, (1995) (PubMed).
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.