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STUB1 Antibody (C-term)

Purified Mouse Monoclonal Antibody (Mab)

     
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  • 1 - STUB1 Antibody (C-term) AM8629b
    All lanes : Anti-STUB1 Antibody (C-term) at 1:4000 dilution Lane 1: 293 whole cell lysate Lane 2: Hela whole cell lysate Lane 3: HepG2 whole cell lysate Lane 4: L929 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-mouse IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 35 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product info
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 Q9UNE7
Reactivity Human, Mouse
Host Mouse
Clonality monoclonal
Isotype IgG1,k
Clone Names 1008CT12.4.1
Calculated MW 34856 Da
Additional info
Gene ID 10273
Other Names E3 ubiquitin-protein ligase CHIP, 6.3.2.-, Antigen NY-CO-7, CLL-associated antigen KW-8, Carboxy terminus of Hsp70-interacting protein, STIP1 homology and U box-containing protein 1 {ECO:0000312|HGNC:HGNC:11427}, STUB1 (HGNC:11427)
Target/Specificity This STUB1 antibody is generated from a mouse immunized with a recombinant protein of human STUB1.
Dilution WB~~1:4000
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.
PrecautionsSTUB1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name STUB1 (HGNC:11427)
Function E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF- BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.
Cellular Location Cytoplasm.
Tissue Location Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung
Research Areas

BACKGROUND

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF- BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.

REFERENCES

Scanlan M.J.,et al.Int. J. Cancer 76:652-658(1998).
Ballinger C.A.,et al.Mol. Cell. Biol. 19:4535-4545(1999).
Krackhardt A.M.,et al.Blood 100:2123-2131(2002).
Daniels R.J.,et al.Hum. Mol. Genet. 10:339-352(2001).
Wan D.,et al.Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).

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