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Lamin A/C antibody

LMNA Reactivity: Human, Mouse, Rat, Cow, Dog WB, IHC, ICC, FACS, IHC (fro) Host: Mouse Monoclonal 133A2 unconjugated
Catalog No. ABIN335389
  • Target See all Lamin A/C (LMNA) Antibodies
    Lamin A/C (LMNA)
    Reactivity
    • 131
    • 72
    • 70
    • 26
    • 15
    • 12
    • 8
    • 7
    • 6
    • 6
    • 6
    • 4
    • 4
    • 3
    • 3
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human, Mouse, Rat, Cow, Dog
    Host
    • 97
    • 44
    • 2
    • 1
    Mouse
    Clonality
    • 96
    • 48
    Monoclonal
    Conjugate
    • 113
    • 9
    • 8
    • 6
    • 2
    • 2
    • 2
    • 2
    This Lamin A/C antibody is un-conjugated
    Application
    • 119
    • 54
    • 54
    • 48
    • 32
    • 31
    • 29
    • 19
    • 14
    • 7
    • 3
    • 2
    • 2
    • 1
    Western Blotting (WB), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunohistochemistry (Frozen Sections) (IHC (fro))
    Specificity
    Human, rat, mouse, bovine, dog.
    Purification
    Purified
    Immunogen
    133A2 is a mouse monoclonal IgG3/kappa antibody obtained from fusion of P3/X63.Ag8.653 mouse myeloma cells with spleen cells from a BALB/c mouse immunized with partially purified recombinant human lamin A.
    Clone
    133A2
    Isotype
    IgG3
    Top Product
    Discover our top product LMNA Primary Antibody
  • Application Notes
    133A2 recognizes an epitope located between residues 598-611 of lamin A and therefore 133A2 reacts exclusively with lamin A. 133A2 is suitable for immunocytochemistry, immunohistochemistry on frozen sections, immunoblotting and flow cytometry. Optimal antibody dilution should be determined by titration, recommended range is 1:100 - 1:200 for flow cytometry, and for immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagent, and 1:100 - 1:1000 for immunoblotting applications.
    Restrictions
    For Research Use only
  • Storage
    4 °C
  • Broers, Bronnenberg, Kuijpers, Schutte, Hutchison, Ramaekers: "Partial cleavage of A-type lamins concurs with their total disintegration from the nuclear lamina during apoptosis." in: European journal of cell biology, Vol. 81, Issue 12, pp. 677-91, (2003) (PubMed).

    Broers, Machiels, van Eys, Kuijpers, Manders, van Driel, Ramaekers: "Dynamics of the nuclear lamina as monitored by GFP-tagged A-type lamins." in: Journal of cell science, Vol. 112 ( Pt 20), pp. 3463-75, (2000) (PubMed).

    Neri, Raymond, Giordano, Borgatti, Marchisio, Capitani, Martelli: "Spatial distribution of lamin A and B1 in the K562 cell nuclear matrix stabilized with metal ions." in: Journal of cellular biochemistry, Vol. 75, Issue 1, pp. 36-45, (1999) (PubMed).

    Neri, Raymond, Giordano, Capitani, Martelli: "Lamin A is part of the internal nucleoskeleton of human erythroleukemia cells." in: Journal of cellular physiology, Vol. 178, Issue 3, pp. 284-95, (1999) (PubMed).

    Pugh, Coates, Lane, Raymond, Quinlan: "Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3T3 cells." in: Journal of cell science, Vol. 110 ( Pt 19), pp. 2483-93, (1997) (PubMed).

    Broers, Machiels, Kuijpers, Smedts, van den Kieboom, Raymond, Ramaekers: "A- and B-type lamins are differentially expressed in normal human tissues." in: Histochemistry and cell biology, Vol. 107, Issue 6, pp. 505-17, (1997) (PubMed).

    Jansen, Machiels, Hopman, Broers, Bot, Arends, Ramaekers, Schouten: "Comparison of A and B-type lamin expression in reactive lymph nodes and nodular sclerosing Hodgkin's disease." in: Histopathology, Vol. 31, Issue 4, pp. 304-12, (1997) (PubMed).

    Machiels, Ramaekers, Kuijpers, Groenewoud, Oosterhuis, Looijenga: "Nuclear lamin expression in normal testis and testicular germ cell tumours of adolescents and adults." in: The Journal of pathology, Vol. 182, Issue 2, pp. 197-204, (1997) (PubMed).

    Machiels, Broers, Raymond, de Ley, Kuijpers, Caberg, Ramaekers: "Abnormal A-type lamin organization in a human lung carcinoma cell line." in: European journal of cell biology, Vol. 67, Issue 4, pp. 328-35, (1996) (PubMed).

    Hozák, Sasseville, Raymond, Cook: "Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells." in: Journal of cell science, Vol. 108 ( Pt 2), pp. 635-44, (1995) (PubMed).

  • Target
    Lamin A/C (LMNA)
    Alternative Name
    Lamin A (LMNA Products)
    Background
    Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane. Two main subtypes of nuclear lamins can be distinguished, i.e. A-type lamins and B-type lamins. The A-type lamins comprise a set of three proteins arising from the same gene by alternative splicing, i.e. lamin A, lamin C and lamin Adel 10, while the B-type lamins include two proteins arising from two distinct genes, i.e. lamin B1 and lamin B2. Recent evidence has revealed that mutations in A-type lamins give rise to a range of rare but dominant genetic disorders, including Emery-Dreifuss muscular dystrophy, dilated cardiomyopathy with conduction-system disease and Dunnigan-type familial partial lipodystrophy. In addition, the expression of A-type lamins coincides with cell differentiation and as A-type lamins specifically interact with chromatin, a role in the regulation of differential gene expression has been suggested for A-type lamins.
    Pathways
    Apoptosis, Caspase Cascade in Apoptosis, ER-Nucleus Signaling, Protein targeting to Nucleus
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