ADL67.10

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SKU: ADL67.10

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DSHB Data Sheet

Catalog Fields

Product Name/ID: ADL67.10
Available to For-Profits: Yes
Alternate Antibody Name: ADL67; alphaL528-622
Gene Name: Lam
Ab Isotype: MIgG1
Gene Symbol:
Antibody Registry ID: AB_528336 
Uniprot ID: P08928 
RRID:  
Entrez Gene ID: 33782 
Clonality: Monoclonal
Immunogen: Recombinant total protein
Clone:
Immunogen Sequence: Total protein
Myeloma Strain: NS0
Epitope Mapped: Yes
Antigen Name: lamin Dm0
Epitope Location or Sequence: aa 548-620 [Depositor Notes] or aa 528-622 [PMID 8776884].
Alternate Antigen Name:
Deposit Date: 3/11/2003
Antigen Molecular Weight: Predicted: 71 kDa; Apparent: 74 and 76 kDa
Depositor: Fisher, P. A.
Antigen Sequence:
Depositor Institution: SUNY at Stony Brook, Pharmacological Sciences
Antigen Species: Drosophila
Depositor Notes: Reacts with Sf9 lamin. Reacts with all Dm isoforms; does not react with lamin C. Epitope between aa 548-620 (tail region). Recognizes Lamin B (PMID: 7593280).
Host Species: mouse
Hybridoma Cells Available (Non-Profit): Yes
Confirmed Species Reactivity: Drosophila, Mosquito, Spodoptera frugiperda
Additional Information:
Predicted Species Reactivity:  
Human Protein Atlas:  
Additional Characterization:  
Recommended Applications: 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:
ADL67.10 was deposited to the DSHB by Fisher, P. A. (DSHB Hybridoma Product ADL67.10)
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).

20 References

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

    Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins.
    Weber K
    Journal of cell science 108 ( Pt 10). (1995 Oct): 3189-98.

    Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae.
    Schmitt B
    The Journal of cell biology 137.5 (1997 Jun 2): 1001-16.

    Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation.
    Furukawa K
    Developmental biology 284.1 (2005 Aug 1): 219-32.

    Characterization of the Drosophila melanogaster genome at the nuclear lamina.
    van Steensel B
    Nature genetics 38.9 (2006 Sep): 1005-14.

    Cloning and Characterization of Sf9 Cell Lamin and the Lamin Conformational Changes during Autographa californica multiple nucleopolyhedrovirus Infection.
    Ji S
    Viruses 8.5 (2016 May 7): .

    The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
    Rzepecki R
    PloS one 7.2 (2012): e32649.

    Molecular genetic analysis of the nested Drosophila melanogaster lamin C gene.
    Wallrath LL
    Genetics 171.1 (2005 Sep): 185-96.

    Confocal Analysis of Nuclear Lamina Behavior during Male Meiosis and Spermatogenesis in Drosophila melanogaster.
    Prantera G
    PloS one 11.3 (2016): e0151231.

    Cytoskeletal control of nuclear morphology and chromatin organization.
    Shivashankar GV
    Journal of molecular biology 427.3 (2015 Feb 13): 695-706.

    Genome mapping and characterization of the Anopheles gambiae heterochromatin.
    Sharakhov IV
    BMC genomics 11. (2010 Aug 4): 459.

    Bypassing the Greatwall-Endosulfine pathway: plasticity of a pivotal cell-cycle regulatory module in Drosophila melanogaster and Caenorhabditis elegans.
    Goldberg ML
    Genetics 191.4 (2012 Aug): 1181-97.

    SCF-Fbxo42 promotes synaptonemal complex assembly by downregulating PP2A-B56.
    Ohkura H
    The Journal of cell biology 220.2 (2021 Feb 1): .

    PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is essential for both mRNA nuclear export and its subsequent cytoplasmic trafficking.
    Kopytova DV
    RNA biology 18.11 (2021 Nov): 1969-1980.

    Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing in Drosophila.
    Hannon GJ
    eLife 10. (2021 Feb 4): .

    WB References

    Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins.
    Weber K
    Journal of cell science 108 ( Pt 10). (1995 Oct): 3189-98.

    Interphase phosphorylation of the Drosophila nuclear lamin: site-mapping using a monoclonal antibody.
    Fisher PA
    Journal of cell science 108 ( Pt 9). (1995 Sep): 3137-44.

    A crucial role for Ras suppressor-1 (RSU-1) revealed when PINCH and ILK binding is disrupted.
    Kadrmas JL
    Journal of cell science 125.Pt 13 (2012 Jul 1): 3185-94.

    Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae.
    Schmitt B
    The Journal of cell biology 137.5 (1997 Jun 2): 1001-16.

    Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation.
    Furukawa K
    Developmental biology 284.1 (2005 Aug 1): 219-32.

    Characterization of the Drosophila melanogaster genome at the nuclear lamina.
    van Steensel B
    Nature genetics 38.9 (2006 Sep): 1005-14.

    Cloning and Characterization of Sf9 Cell Lamin and the Lamin Conformational Changes during Autographa californica multiple nucleopolyhedrovirus Infection.
    Ji S
    Viruses 8.5 (2016 May 7): .

    The Drosophila mus 308 gene product, implicated in tolerance of DNA interstrand crosslinks, is a nuclear protein found in both ovaries and embryos.
    Fisher PA
    DNA repair 4.9 (2005 Aug 15): 971-82.

    PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is essential for both mRNA nuclear export and its subsequent cytoplasmic trafficking.
    Kopytova DV
    RNA biology 18.11 (2021 Nov): 1969-1980.

    Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing in Drosophila.
    Hannon GJ
    eLife 10. (2021 Feb 4): .

    IHC References
    IP References
    Epitope Map References
    All References

    Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins.
    Weber K
    Journal of cell science 108 ( Pt 10). (1995 Oct): 3189-98.

    Stall in Canonical Autophagy-Lysosome Pathways Prompts Nucleophagy-Based Nuclear Breakdown in Neurodegeneration.
    Fanto M
    Current biology : CB 27.23 (2017 Dec 4): 3626-3642.e6.

    Boundaries potentiate polycomb response element-mediated silencing.
    Chetverina D
    BMC biology 19.1 (2021 Jun 2): 113.

    Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae.
    Schmitt B
    The Journal of cell biology 137.5 (1997 Jun 2): 1001-16.

    Null mutants of Drosophila B-type lamin Dm(0) show aberrant tissue differentiation rather than obvious nuclear shape distortion or specific defects during cell proliferation.
    Furukawa K
    Developmental biology 284.1 (2005 Aug 1): 219-32.

    Characterization of the Drosophila melanogaster genome at the nuclear lamina.
    van Steensel B
    Nature genetics 38.9 (2006 Sep): 1005-14.

    Cloning and Characterization of Sf9 Cell Lamin and the Lamin Conformational Changes during Autographa californica multiple nucleopolyhedrovirus Infection.
    Ji S
    Viruses 8.5 (2016 May 7): .

    The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.
    Rzepecki R
    PloS one 7.2 (2012): e32649.

    Molecular genetic analysis of the nested Drosophila melanogaster lamin C gene.
    Wallrath LL
    Genetics 171.1 (2005 Sep): 185-96.

    Confocal Analysis of Nuclear Lamina Behavior during Male Meiosis and Spermatogenesis in Drosophila melanogaster.
    Prantera G
    PloS one 11.3 (2016): e0151231.

    Cytoskeletal control of nuclear morphology and chromatin organization.
    Shivashankar GV
    Journal of molecular biology 427.3 (2015 Feb 13): 695-706.

    Genome mapping and characterization of the Anopheles gambiae heterochromatin.
    Sharakhov IV
    BMC genomics 11. (2010 Aug 4): 459.

    Bypassing the Greatwall-Endosulfine pathway: plasticity of a pivotal cell-cycle regulatory module in Drosophila melanogaster and Caenorhabditis elegans.
    Goldberg ML
    Genetics 191.4 (2012 Aug): 1181-97.

    SCF-Fbxo42 promotes synaptonemal complex assembly by downregulating PP2A-B56.
    Ohkura H
    The Journal of cell biology 220.2 (2021 Feb 1): .

    PCID2, a subunit of the Drosophila TREX-2 nuclear export complex, is essential for both mRNA nuclear export and its subsequent cytoplasmic trafficking.
    Kopytova DV
    RNA biology 18.11 (2021 Nov): 1969-1980.

    Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing in Drosophila.
    Hannon GJ
    eLife 10. (2021 Feb 4): .

    Interphase phosphorylation of the Drosophila nuclear lamin: site-mapping using a monoclonal antibody.
    Fisher PA
    Journal of cell science 108 ( Pt 9). (1995 Sep): 3137-44.

    A crucial role for Ras suppressor-1 (RSU-1) revealed when PINCH and ILK binding is disrupted.
    Kadrmas JL
    Journal of cell science 125.Pt 13 (2012 Jul 1): 3185-94.

    The Drosophila mus 308 gene product, implicated in tolerance of DNA interstrand crosslinks, is a nuclear protein found in both ovaries and embryos.
    Fisher PA
    DNA repair 4.9 (2005 Aug 15): 971-82.

    Intermediate filament protein polymerization: molecular analysis of Drosophila nuclear lamin head-to-tail binding.
    Fisher PA
    Journal of structural biology 117.1 (1996 Jul-Aug): 1-15.

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