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>   首页   >   产品   >   一抗   >   细胞生物学   >   USP14 Antibody (N-term)   

USP14 Antibody (N-term)

Mouse Monoclonal Antibody (Mab)

     
  • 1 - USP14 Antibody (N-term) AM2220b
    All lanes: Anti-USP14 Antibody (N-term) at 1:1000 dilution Lane 1: A2058 whole cell lysate Lane 2: Mouse brain lysate Lane 3: Rat brain whole cell lysate Lane 4: Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary: Goat Anti-Mouse IgG, (H+L), Peroxidase conjugated (ASP1613) at 1/8000 dilution. Observed band size: 60 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 P54578
Reactivity Human, Mouse, Rat
Host Mouse
Clonality Monoclonal
Isotype IgG1
Clone Names 889CT6.2.1
Calculated MW 56069 Da
Additional Information
Gene ID 9097
Other Names Ubiquitin carboxyl-terminal hydrolase 14, Deubiquitinating enzyme 14, Ubiquitin thioesterase 14, Ubiquitin-specific-processing protease 14, USP14, TGT
Target/Specificity Purified His-tagged USP14 protein was used to produced this monoclonal antibody.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified monoclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, 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.
PrecautionsUSP14 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name USP14
Synonyms TGT
Function Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029).
Cellular Location Cytoplasm. Cell membrane; Peripheral membrane protein
Research Areas

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

BACKGROUND

Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell. Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis. Serves also as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1. Indispensable for synaptic development and function at neuromuscular junctions (NMJs).

REFERENCES

Deshpande K.L., et al. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
Kalnine N., et al. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Reuter T.Y., et al. Exp. Cell Res. 289:211-221(2003).
Carrascal M., et al. J. Proteome Res. 7:5167-5176(2008).
Koulich E., et al. Mol. Biol. Cell 19:1072-1082(2008).

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