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UBB Antibody

Purified Mouse Monoclonal Antibody

     
  • 10 - UBB Antibody AO1667a

    Black line: Control Antigen (100 ng);
    Purple line: Antigen(10ng);
    Blue line: Antigen (50 ng);
    Red line: Antigen (100 ng);

  • 1 - UBB Antibody AO1667a
    Figure 1: Western blot analysis using UBB mAb against human UBB (AA: 1-299) recombinant protein. (Expected MW is 26 kDa)
  • 1 - UBB Antibody AO1667a
    Figure 2: Western blot analysis using UBB mouse mAb against NIH/3T3 (1) and Hela (2) cell lysate.
  • 4 - UBB Antibody AO1667a
    Figure 3: Flow cytometric analysis of Hela cells using UBB mouse mAb (green) and negative control (red).
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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, FC, E
Primary Accession P0CG47
Reactivity Human
Host Mouse
Clonality Monoclonal
Clone Names 3C12
Isotype IgG1
Calculated MW 25762 Da
Description This gene encodes ubiquitin, one of the most conserved proteins known. Ubiquitin is required for ATP-dependent, nonlysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation. Ubiquitin also binds to histone H2A in actively transcribed regions but does not cause histone H2A degradation, suggesting that ubiquitin is also involved in regulation of gene expression. This gene consists of three direct repeats of the ubiquitin coding sequence with no spacer sequence. Consequently, the protein is expressed as a polyubiquitin precursor with a final amino acid after the last repeat. Aberrant form of this protein has been noticed in patients with Alzheimer's and Down syndrome.
Immunogen Purified recombinant fragment of human UBB expressed in E. Coli.
Formulation Purified antibody in PBS with 0.05% sodium azide
Additional Information
Gene ID 7314
Other Names Polyubiquitin-B, Ubiquitin, UBB
Dilution WB~~1/500 - 1/2000
FC~~1/200 - 1/400
E~~1/10000
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsUBB Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name UBB
Function [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Cellular Location [Ubiquitin]: Cytoplasm. Nucleus. Mitochondrion outer membrane; Peripheral membrane protein
Research Areas

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

REFERENCES

1. Science. 2009 Aug 14;325(5942):834-40. 2. Biochem Soc Trans. 2009 Oct;37(Pt 5):937-53.

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