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SUMO1 Antibody (C-term D86)

Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - SUMO1 Antibody (C-term D86) AP1222e
    All lanes : Anti-SUMO1 at 1:1000 dilution Lane 1: K562 whole cell lysate Lane 2: Hela whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 12 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 P63165
Other Accession Q5I0H3, A7WLH8, P63166, Q7SZR5, Q8QGH2, Q5E9D1, Q5EAX4, O57686
Reactivity Human
Predicted Xenopus, Bovine, Chicken, Zebrafish, Mouse, Pig, Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit Ig
Calculated MW 11557 Da
Additional info
Gene ID 7341
Other Names Small ubiquitin-related modifier 1, SUMO-1, GAP-modifying protein 1, GMP1, SMT3 homolog 3, Sentrin, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein SMT3C, Smt3C, Ubiquitin-like protein UBL1, SUMO1, SMT3C, SMT3H3, UBL1
Target/Specificity This SUMO1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human SUMO1 sequence.
Dilution WB~~1:1000
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein G column, eluted with high and low pH buffers and neutralized immediately, 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.
PrecautionsSUMO1 Antibody (C-term D86) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name SUMO1
Synonyms SMT3C, SMT3H3, UBL1
Function Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
Cellular Location Nucleus membrane. Nucleus speckle. Cytoplasm. Nucleus, PML body. Note=Recruited by BCL11A into the nuclear body.
Research Areas

BACKGROUND

Covalent modification of target lysines by SUMO (small ubiquitin-like modifier) modulates processes such as protein localization, transcription, nuclear transport, mitosis, DNA replication and repair, signal transduction, and viral reproduction. SUMO does not seem to be involved in protein degradation and may in fact function as an antagonist of ubiquitin in the degradation process. The SUMO family consists of SUMO1 and closely related homologs SUMO2, SUMO3, and SUMO4. Sumoylation has been shown to regulate a wide range of proteins, including MDM2, PIAS, PML, RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, PARK2, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, CaMK, DNMT3B, TDG, HIF1A, CHD3, EXOSC9, RAD51, and viral targets such as CMV-IE1/2, EBV-BZLF1, and HPV/BPV-E1.

REFERENCES

Yang, S.H., et al., Mol. Cell 13(4):611-617 (2004).
Bailey, D., et al., J. Biol. Chem. 279(1):692-703 (2004).
Ling, Y., et al., Nucleic Acids Res. 32(2):598-610 (2004).
Pountney, D.L., et al., Exp. Neurol. 184(1):436-446 (2003).
Ohshima, T., et al., J. Biol. Chem. 278(51):50833-50842 (2003).

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