SUMO-1 21C7

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$40.00
SKU: SUMO-1 21C7
View product citations for antibody SUMO-1 21C7 on CiteAb

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DSHB Data Sheet

Catalog Fields

Antigen: SUMO1, aa 57-67
Hybridoma Cells Available: Yes
Antigen Species: Human
Depositor: Matunis, M.
Isotype: MIgG1
Antigen Sequence:
Host Species: mouse
Depositors Institution: Johns Hopkins University School of Medicine
Positive Tested Species Reactivity: Chicken, Human, Mouse, Rat, Xenopus, Zebrafish
Depositors Notes: This antibody recognizes SUMO1 and SUMO1 conjugates in all vertebrate cells tested; does not cross-react with SUMO2 or SUMO3. 21C7 doesn't recognize C. elegans SUMO1.
Antigen Molecular Weight: 11 kDa
Human Protein Atlas:  
Predicted Species Reactivity:  
Gene: SUMO1
Immunogen: Recombinant SUMO-1 (GenBank accession number AAB40390) protein with N-terminal 6xHis tag
Alternate Gene Names: SMT3C, SMT3H3, UBL1, PIC1, DAP1, GMP1, OFC10, SENP2
Alternate Antibody Name: 21C7
Clonality: Monoclonal
Alternate Antigen Name:
Epitope Mapped: Yes
Myeloma Strain: SP2/0-Ag14
Epitope Location or Sequence: aa 57-67 VPMNSLRFLFE
Uniprot ID: P63165 
Immunogen Sequence: Full length protein
Entrez Gene ID: 7341 
Additional Characterization:  
Antibody Registry ID: AB_2198257 
Additional Information: This antibody will recognize both SUMO-1 isoforms.
Recommended Applications: Immunofluorescence, Immunoprecipitation, Western Blot
These hybridomas were created by your colleagues. Please acknowledge the hybridoma contributor and the Developmental Studies Hybridoma Bank (DSHB) in the Materials and Methods of your publications. Please email the citation to us.
For your Materials & Methods section:
SUMO-1 21C7 was deposited to the DSHB by Matunis, M. (DSHB Hybridoma Product SUMO-1 21C7)
Storage and Handling Recommendations
Although many cell products are maintained at 4°C for years without loss of activity, shelf-life at 4°C is highly variable. For immediate use, short term storage at 4°C up to two weeks is recommended. For long term storage, divide the solution into volumes of no less than 20 ul for freezing at -20°C or -80°C. The small volume aliquot should provide sufficient reagent for short term use. Freeze-thaw cycles should be avoided. For concentrate or bioreactor products, an equal volume of glycerol, a cryoprotectant, may be added prior to freezing.
Usage Recommendations
Although the optimal Ig concentration for an application varies for each product and must be optimized for each laboratory, a good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) is 2-5 ug/ml. For western blots, the recommended concentration range is 0.2-0.5 ug/ml.
All cell products contain the antimicrobial ProClin. Click here for additional information.

13 References

  • Initial Publication
  • IF References
  • WB References
  • IHC References
  • IP References
  • FFPE References
  • Epitope Map References
  • All References
  • Initial Publication
    IF References
    WB References

    A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
    Blobel G
    The Journal of cell biology 135.6 Pt 1 (1996 Dec): 1457-70.

    Identification of the SUMO E3 ligase PIAS1 as a potential survival biomarker in breast cancer.
    Bonni S
    PloS one 12.5 (2017): e0177639.

    SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis.
    Matunis MJ
    Molecular cell 29.6 (2008 Mar 28): 729-41.

    SUMO modified proteins localize to the XY body of pachytene spermatocytes.
    Matunis MJ
    Chromosoma 113.5 (2004 Nov): 233-43.

    Detecting endogenous SUMO targets in mammalian cells and tissues.
    Melchior F
    Nature structural & molecular biology 20.4 (2013 Apr): 525-31.

    A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly.
    Pichler A
    Nature structural & molecular biology 22.12 (2015 Dec): 959-67.

    Terminal differentiation of cortical neurons rapidly remodels RanGAP-mediated nuclear transport system.
    Yoshikawa K
    Genes to cells : devoted to molecular & cellular mechanisms 21.11 (2016 Nov): 1176-1194.

    The Sumo protease Senp7 is required for proper neuronal differentiation.
    Garcia-Dominguez M
    Biochimica et biophysica acta 1863.7 Pt A (2016 Jul): 1490-8.

    Identification and analysis of endogenous SUMO1 and SUMO2/3 targets in mammalian cells and tissues using monoclonal antibodies.
    Melchior F
    Nature protocols 9.4 (2014 Apr): 896-909.

    The ROS/SUMO axis contributes to the response of acute myeloid leukemia cells to chemotherapeutic drugs.
    Piechaczyk M
    Cell reports 7.6 (2014 Jun 26): 1815-23.

    Mad1 destabilizes p53 by preventing PML from sequestering MDM2.
    Weaver BA
    Nature communications 10.1 (2019 Apr 4): 1540.

    IHC References

    Mad1 destabilizes p53 by preventing PML from sequestering MDM2.
    Weaver BA
    Nature communications 10.1 (2019 Apr 4): 1540.

    IP References
    FFPE References

    Mad1 destabilizes p53 by preventing PML from sequestering MDM2.
    Weaver BA
    Nature communications 10.1 (2019 Apr 4): 1540.

    Epitope Map References

    Detecting endogenous SUMO targets in mammalian cells and tissues.
    Melchior F
    Nature structural & molecular biology 20.4 (2013 Apr): 525-31.

    All References

    Mad1 destabilizes p53 by preventing PML from sequestering MDM2.
    Weaver BA
    Nature communications 10.1 (2019 Apr 4): 1540.

    A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
    Blobel G
    The Journal of cell biology 135.6 Pt 1 (1996 Dec): 1457-70.

    SUMO-2/3 modification and binding regulate the association of CENP-E with kinetochores and progression through mitosis.
    Matunis MJ
    Molecular cell 29.6 (2008 Mar 28): 729-41.

    SUMO modified proteins localize to the XY body of pachytene spermatocytes.
    Matunis MJ
    Chromosoma 113.5 (2004 Nov): 233-43.

    Identification of the SUMO E3 ligase PIAS1 as a potential survival biomarker in breast cancer.
    Bonni S
    PloS one 12.5 (2017): e0177639.

    Detecting endogenous SUMO targets in mammalian cells and tissues.
    Melchior F
    Nature structural & molecular biology 20.4 (2013 Apr): 525-31.

    A new vertebrate SUMO enzyme family reveals insights into SUMO-chain assembly.
    Pichler A
    Nature structural & molecular biology 22.12 (2015 Dec): 959-67.

    Terminal differentiation of cortical neurons rapidly remodels RanGAP-mediated nuclear transport system.
    Yoshikawa K
    Genes to cells : devoted to molecular & cellular mechanisms 21.11 (2016 Nov): 1176-1194.

    The Sumo protease Senp7 is required for proper neuronal differentiation.
    Garcia-Dominguez M
    Biochimica et biophysica acta 1863.7 Pt A (2016 Jul): 1490-8.

    Identification and analysis of endogenous SUMO1 and SUMO2/3 targets in mammalian cells and tissues using monoclonal antibodies.
    Melchior F
    Nature protocols 9.4 (2014 Apr): 896-909.

    The ROS/SUMO axis contributes to the response of acute myeloid leukemia cells to chemotherapeutic drugs.
    Piechaczyk M
    Cell reports 7.6 (2014 Jun 26): 1815-23.

    Detection of Protein-Protein Interactions and Posttranslational Modifications Using the Proximity Ligation Assay: Application to the Study of the SUMO Pathway.
    Bossis G
    Methods in molecular biology (Clifton, N.J.) 1449. (2016): 279-90.

    Several posttranslational modifications act in concert to regulate gephyrin scaffolding and GABAergic transmission.
    Tyagarajan SK
    Nature communications 7. (2016 Nov 7): 13365.

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