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>   首页   >   产品   >   一抗   >   细胞生物学   >   UBE3C Antibody (Center)   

UBE3C Antibody (Center)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - UBE3C Antibody (Center) AP20457c
    All lanes: Anti-UBE3CAntibody(Center) at 1:1000 dilution + 293T whole cell lysate Lysates/proteins at 20 µg per lane. Secondary: Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated (ASP1615) at 1/15000 dilution. Observed band size: 124 KDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q15386
Reactivity Human
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 123923 Da
Antigen Region 549-578 aa
Additional Information
Gene ID 9690
Other Names Ubiquitin-protein ligase E3C, 632-, HectH2, UBE3C, KIAA0010, KIAA10
Target/Specificity This UBE3C antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 549-578 amino acids from the Central region of human UBE3C.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.05% (V/V) Proclin 300. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain 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.
PrecautionsUBE3C Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name UBE3C {ECO:0000303|PubMed:17323924, ECO:0000312|HGNC:HGNC:16803}
Function E3 ubiquitin-protein ligase that specifically catalyzes 'Lys- 29'- and 'Lys-48'-linked polyubiquitin chains (PubMed:11278995, PubMed:12692129, PubMed:16341092, PubMed:16601690, PubMed:24158444, PubMed:24811749, PubMed:25752573, PubMed:25752577, PubMed:32039437, PubMed:33637724, PubMed:34239127). Accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:32039437, PubMed:9575161). Associates with the proteasome and promotes elongation of ubiquitin chains on substrates bound to the 26S proteasome (PubMed:24158444, PubMed:28396413, PubMed:31375563). Also catalyzes 'Lys-29'- and 'Lys-48'-linked ubiquitination of 26S proteasome subunit ADRM1/RPN13 in response to proteotoxic stress, impairing the ability of the proteasome to bind and degrade ubiquitin- conjugated proteins (PubMed:24811749, PubMed:31375563). Acts as a negative regulator of autophagy by mediating 'Lys-29'- and 'Lys-48'- linked ubiquitination of PIK3C3/VPS34, promoting its degradation (PubMed:33637724). Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'- or 'Lys-48'-linked polyubiquitin chains; with some preference for 'Lys-48' linkages (PubMed:11278995, PubMed:16601690, PubMed:25752577). Acts as a negative regulator of type I interferon by mediating 'Lys-48'-linked ubiquitination of IRF3 and IRF7, leading to their degradation by the proteasome (PubMed:21167755). Catalyzes ubiquitination and degradation of CAND2 (PubMed:12692129).
Tissue Location Highly expressed in skeletal muscle. Detected at much lower levels in kidney and pancreas.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

E3 ubiquitin-protein ligase that accepts ubiquitin from the E2 ubiquitin-conjugating enzyme UBE2D1 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Can assemble unanchored poly-ubiquitin chains in either 'Lys-29'-or 'Lys-48'-linked polyubiquitin chains. Has preference for 'Lys-48' linkages. It can target itself for ubiquitination in vitro and may promote its own degradation in vivo.

REFERENCES

Nomura N., et al. DNA Res. 1:27-35(1994).
Hillier L.W., et al. Nature 424:157-164(2003).
Scherer S.W., et al. Science 300:767-772(2003).
Mural R.J., et al. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
You J., et al. J. Biol. Chem. 276:19871-19878(2001).

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