mAb 3F2.3

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SKU: mAb 3F2.3

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DSHB Data Sheet

Catalog Fields

Clone ID/Product Name: mAb 3F2.3
Available to For-Profits: Yes
Alternate Antibody Name:
Gene Symbol: CAPZB
Ab Isotype: MIgG2a, kappa light chain
Gene Name:
Antibody Registry ID: AB_531768 
Uniprot ID: P14315 
RRID:  
Entrez Gene ID: 832 
Clonality: Monoclonal
Immunogen: Purified capping protein beta-2
Clone:
Immunogen Sequence: Full length
Myeloma Strain: P3x63 Ag8.653
Epitope Mapped: No
Antigen Name: F-actin capping protein beta-2 subunit
Epitope Location or Sequence:
Alternate Antigen Name:
Deposit Date: 2/13/1996
Antigen Molecular Weight: 30.6 kDa
Depositor: Cooper, J.A.
Antigen Sequence:
Depositor Institution: Washington University Med. School, St. Louis
Antigen Species: Chicken
Depositor Notes: For immunofluorescence staining, fixation with a glyoxal-based solution has been successful (PMID: 24319057/ 28899994) while paraformaldehyde has generally not succeeded. Glyoxal solutions can be prepared and used as described (PMID: 29146773) and are commercially available under the name GlyoFixx.
Host Species: mouse
Hybridoma Cells Available (Non-Profit): Yes
Confirmed Species Reactivity: Chicken, Human, Mouse, Rat
Additional Information: 3F2 does not cross-react with the CapZ Beta-1 subunit.
Predicted Species Reactivity:  
Human Protein Atlas:  
Additional Characterization:  
Recommended Applications: Function Blocking, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blot
All cell products contain the antimicrobial ProClin. Click here for additional information.
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:
mAb 3F2.3 was deposited to the DSHB by Cooper, J.A. (DSHB Hybridoma Product mAb 3F2.3)
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
The optimal Ig concentration for an application varies by species and antibody affinity. For each product, the antibody titer must be optimized for every application by the end user laboratory. A good starting concentration for immunohistochemistry (IHC), immunofluorescence (IF), and immunocytochemistry (ICC) when using mouse Ig is 2-5 ug/ml. For western blots, the recommended concentration range of mouse Ig 0.2-0.5 ug/ml. In general, rabbit antibodies demonstrate greater affinity and are used at a magnitude lower Ig concentration for initial testing. The recommended concentrations for rabbit Ig are 0.2-0.5 ug/ml (IF, IHC and ICC) and 20-50 ng/ml (WB).

11 References

  • Initial Publication
  • IF References
  • WB References
  • IHC References
  • IP References
  • FB References
  • All References
  • Initial Publication

    Identification and characterization of an actin-binding site of CapZ.
    Cooper JA
    The Journal of cell biology 116.4 (1992 Feb): 923-31.

    IF References

    Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates.
    Cooper JA
    The Journal of cell biology 127.2 (1994 Oct): 453-65.

    Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.
    Cooper JA
    Cell motility and the cytoskeleton 38.2 (1997): 120-32.

    Actin capping protein is required for dendritic spine development and synapse formation.
    Zheng JQ
    The Journal of neuroscience : the official journal of the Society for Neuroscience 31.28 (2011 Jul 13): 10228-33.

    Correlation of actin crosslinker and capper expression levels with stereocilia growth phases.
    Barr-Gillespie PG
    Molecular & cellular proteomics : MCP 13.2 (2014 Feb): 606-20.

    WB References

    Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.
    Cooper JA
    The Journal of cell biology 135.1 (1996 Oct): 169-79.

    Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates.
    Cooper JA
    The Journal of cell biology 127.2 (1994 Oct): 453-65.

    The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein.
    Litchfield DW
    The Journal of biological chemistry 281.47 (2006 Nov 24): 36347-59.

    Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1.
    Gundersen GG
    Molecular biology of the cell 23.20 (2012 Oct): 4032-40.

    Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc.
    Gregorio CC
    Molecular biology of the cell 19.5 (2008 May): 1837-47.

    Rapid and efficient purification of actin from nonmuscle sources.
    Cooper JA
    Cell motility and the cytoskeleton 39.2 (1998): 166-71.

    Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.
    Cooper JA
    Cell motility and the cytoskeleton 38.2 (1997): 120-32.

    Actin capping protein is required for dendritic spine development and synapse formation.
    Zheng JQ
    The Journal of neuroscience : the official journal of the Society for Neuroscience 31.28 (2011 Jul 13): 10228-33.

    Correlation of actin crosslinker and capper expression levels with stereocilia growth phases.
    Barr-Gillespie PG
    Molecular & cellular proteomics : MCP 13.2 (2014 Feb): 606-20.

    IHC References

    Heterodimeric capping protein is required for stereocilia length and width regulation.
    Barr-Gillespie PG
    The Journal of cell biology 216.11 (2017 Nov 6): 3861-3881.

    IP References

    The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein.
    Litchfield DW
    The Journal of biological chemistry 281.47 (2006 Nov 24): 36347-59.

    Heterodimeric capping protein is required for stereocilia length and width regulation.
    Barr-Gillespie PG
    The Journal of cell biology 216.11 (2017 Nov 6): 3861-3881.

    FB References
    All References

    Heterodimeric capping protein is required for stereocilia length and width regulation.
    Barr-Gillespie PG
    The Journal of cell biology 216.11 (2017 Nov 6): 3861-3881.

    Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates.
    Cooper JA
    The Journal of cell biology 127.2 (1994 Oct): 453-65.

    Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.
    Cooper JA
    Cell motility and the cytoskeleton 38.2 (1997): 120-32.

    Actin capping protein is required for dendritic spine development and synapse formation.
    Zheng JQ
    The Journal of neuroscience : the official journal of the Society for Neuroscience 31.28 (2011 Jul 13): 10228-33.

    Correlation of actin crosslinker and capper expression levels with stereocilia growth phases.
    Barr-Gillespie PG
    Molecular & cellular proteomics : MCP 13.2 (2014 Feb): 606-20.

    Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.
    Cooper JA
    The Journal of cell biology 135.1 (1996 Oct): 169-79.

    The role of CKIP-1 in cell morphology depends on its interaction with actin-capping protein.
    Litchfield DW
    The Journal of biological chemistry 281.47 (2006 Nov 24): 36347-59.

    Actin-capping protein promotes microtubule stability by antagonizing the actin activity of mDia1.
    Gundersen GG
    Molecular biology of the cell 23.20 (2012 Oct): 4032-40.

    Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc.
    Gregorio CC
    Molecular biology of the cell 19.5 (2008 May): 1837-47.

    Rapid and efficient purification of actin from nonmuscle sources.
    Cooper JA
    Cell motility and the cytoskeleton 39.2 (1998): 166-71.

    Identification and characterization of an actin-binding site of CapZ.
    Cooper JA
    The Journal of cell biology 116.4 (1992 Feb): 923-31.

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