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UBE2L3 Antibody (C-term)

Purified Rabbit Polyclonal Antibody (Pab)

     
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  • 1 - UBE2L3 Antibody (C-term) AW5470
    All lanes : Anti-UBE2L3 Antibody (C137) at 1:1000 dilution Lane 1: mouse testis lysates Lane 2: rat testis lysates Lane 3: human testis lysates Lane 4: U87-MG whole cell lysates Lane 5: K562 whole cell lysates Lane 6: PC-12 whole cell lysates Lane 7: NIH/3T3 whole cell lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 18 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 14 - UBE2L3 Antibody (C-term) AW5470
    Formalin-fixed and paraffin-embedded human cancer tissue reacted with the primary antibody, which was peroxidase-conjugated to the secondary antibody, followed by DAB staining. This data demonstrates the use of this antibody for immunohistochemistry; clinical relevance has not been evaluated. BC = breast carcinoma; HC = hepatocarcinoma.
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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
IHC-P, WB
Primary Accession P68036
Other Accession P68037, Q3MHP1, NP_003338
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW H=18,14;M=18 KDa
Isotype Rabbit Ig
Antigen Source HUMAN
Additional Information
Gene ID 7332
Antigen Region 123-153
Other Names Ubiquitin-conjugating enzyme E2 L3, L-UBC, UbcH7, Ubiquitin carrier protein L3, Ubiquitin-conjugating enzyme E2-F1, Ubiquitin-protein ligase L3, UBE2L3, UBCE7, UBCH7
Dilution WB~~1:1000
IHC-P~~1:50~100
Target/Specificity This UBE2L3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 123-153 amino acids from the C-terminal region of human UBE2L3.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
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.
PrecautionsUBE2L3 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name UBE2L3
Synonyms UBCE7, UBCH7
Function Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down- regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis.
Cellular Location Nucleus. Cytoplasm.
Tissue Location Ubiquitous, with highest expression in testis.
Research Areas

BACKGROUND

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2L3 is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is demonstrated to participate in the ubiquitination of p53, c-Fos, and the NF-kB precursor p105 in vitro.

REFERENCES

Moynihan, T.P., et al., Genomics 51(1):124-127 (1998).
Moynihan, T.P., et al., Mamm. Genome 7(7):520-525 (1996).
Nuber, U., et al., J. Biol. Chem. 271(5):2795-2800 (1996).
Robinson, P.A., et al., Mamm. Genome 6(10):725-731 (1995).
Ardley, H.C., et al., Biochim. Biophys. Acta 1491 (1-3), 57-64 (2000).

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