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FIGURE: 1 / 1
USP13 Antibody (PA5-23318) in WB
Western blot analysis of USP13 in human spleen lysate in the 1) absence and 2) presence of immunizing peptide. Samples were incubated in USP13 polyclonal antibody (Product # PA5-23318) using a dilution of 0.25 µg/mL followed by a goat anti-rabbit Ig HRP secondary antibody. PicoTect ECL substrate solution was used for this test.
Product Details
PA5-23318
Applications
Tested Dilution
Publications
Product Specifications
Species Reactivity
Bovine,
Dog,
Horse,
Human,
Mouse,
Non-human primate
Host/Isotype
Rabbit
/ IgG
Class
Polyclonal
Type
Antibody
Immunogen
A portion of amino acids 500-550 of human USP13
Conjugate
Form
Liquid
Concentration
0.5 mg/mL
Purification
Antigen affinity chromatography
Storage buffer
PBS with 0.05% BSA
Contains
0.05% sodium azide
Storage conditions
-20° C, Avoid Freeze/Thaw Cycles
Shipping conditions
Ambient (domestic); Wet ice (international)
RRID
AB_2540842
Target Information
Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data. [UniProt]
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: Deubiquitinating enzyme 13; Isopeptidase T-3; ISOT-3; Ubiquitin carboxyl-terminal hydrolase 13; ubiquitin specific peptidase 13 (isopeptidase T-3); ubiquitin specific protease 13 (isopeptidase T-3); Ubiquitin thioesterase 13; ubiquitin thiolesterase 13; Ubiquitin-specific-processing protease 13
Gene Aliases: 2700071E21Rik; AI848077; IsoT-3; ISOT3; USP13
UniProt ID: (Bovine) E1BMF7, (Human) Q92995, (Mouse) Q5BKP2
Entrez Gene ID: (Bovine) 100141289, (Horse) 100065844, (Human) 8975, (Dog) 478640, (Mouse) 72607
cysteine-type endopeptidase activity
thiol-dependent ubiquitin-specific protease activity
zinc ion binding
ubiquitin protein ligase binding
ubiquitin binding
chaperone binding
proteasome binding
BAT3 complex binding
Lys48-specific deubiquitinase activity
protein binding
ubiquitin-like protein ligase binding
ubiquitin-specific protease activity involved in positive regulation of ERAD pathway
peptidase activity
cysteine-type peptidase activity
omega peptidase activity
hydrolase activity
thiol-dependent ubiquitinyl hydrolase activity
metal ion binding
cysteine protease
regulation of transcription, DNA-templated
ubiquitin-dependent protein catabolic process
autophagy
cell proliferation
regulation of autophagy
protein K29-linked deubiquitination
protein K6-linked deubiquitination
protein stabilization
protein K63-linked deubiquitination
protein K48-linked deubiquitination
positive regulation of ERAD pathway
maintenance of unfolded protein involved in ERAD pathway
melanocyte differentiation
proteolysis
protein deubiquitination
proteasome-mediated ubiquitin-dependent protein catabolic process
regulation of proteasomal protein catabolic process
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