Anti-Prelamin-A Antibody, clone 7G11

Lamin-A is a key component of the nuclear lamina, a protein network underlying the inner membrane that determines nuclear shape and size. The same gene (Lmna, Dhe, or Lamn1 in murine species; Gene ID 16905) that encodes lamin-A also codes for the alternatively spliced prelamin-C isoforms (UniProt P48678-2 and P48678-3). Murine lamin-A (UniProt P48678-1) is initially produced as a 665-amino acid prelamin A that terminals in a CAAX motif. It is further processed post-translationally by four enzymatic steps to yield the mature Lamin-A. Farnesylation of Cys662, endoproteolytic cleavage of the last three amino acids (a.a. 663-665), carboxylmethylation of Cys662, and the final endoproteolytic removal of the remaining propeptide sequence (a.a. 648-662), including the farnesylated Cys662, is catalyzed by the ER membrane zinc metalloproteinase ZMPSTE24.

Clone 7G11 detects prelamin-A regardless of its farnesylation state, but not mature Lamin-A (a.a. 1-647) lacking the C-terminal propeptide sequence. Clone 7G11 does not detect the pre- or mature forms of the spliced isoforms C1 & C2 (Lamin-C; P48678-2 & P48678-3).

Epitope: C-terminal propeptide sequence

Linear peptide corresponding to the C-terminal propeptide sequence of mouse Prelamin-A.

Research Category
Cell Structure

Research Sub Category
Adhesion (CAMs)

This Anti-Prelamin-A Antibody, clone 7G11 is validated for use in Western Blotting and Immunofluorescence for the detection of Prelamin-A.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected 2-day FTI (5 µM; Cat. No. 344550) treatment-induced prelamin-A accumulation in C2C12 cell lysate.
Immunofluorescence Analysis: A representative lot detected upregulated prelamin-A immunoreactivity in keratinocytes, but not in dermal fibroblasts by fluorescent immunohistochemistry using paraformaldehyde-fixed and paraffin-embedded skin sections from keratinocyte-specific Fntb knockout mice, while prelamin-A upregulation was seen in both keratinocytes and dermal fibroblasts from mice with non-tissue/cell type-specific Zmpste24 knockout (Lee, R., et al. (2010). Hum. Mol. Genet.19(8):1603-1617).
Immunofluorescence Analysis: A representative lot stained the nuclear rim of hepatocytes by fluorescent immunohistochemistry using methanol-fixed and Tween-permeabilized frozen liver sections from a transgenic mouse strain that produces the C662S non-farnesylated prelamin-A only (nPLAO/nPLAO) and no lamin-C, while cellular prelamin-A level was undetectable in liver sections from wild-type mice or a mouse strain that produces wild-type prelamin-A only (PLAO/PLAO) and no lamin-C (Davies, B.S., et al. (2010). Hum. Mol. Genet. 19(13):2682-2694).
Western Blotting Analysis: A representative lot detected cellular prelamin-A accumulation upon farnesyltransferase inhibitor (FTI) treatment in murine fibroblasts. Clone 7G11 selectively detects prelamin-A, but not mature lamin-A or lamin-C (Lee, R., et al. (2010). Hum. Mol. Genet.19(8):1603-1617).
Note: Under normal condition, cellular prelamin-A level is below detection. Any newly produced prelamin-A is quickly processed further to yield mature lamin-A. Cellular farnesyltransferase and/or ZMPSTE24 activity must be inhibited (by gene knockout or inhibitor treatment) to allow antibody-based detection of cellular prelamin-A.

Evaluated by Western Blotting in RAW264.7 cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected 2-day FTI-276 (5 µM; Cat. No. 344550) treatment-induced prelamin-A accumulation in murine RAW 264.7 macrophages.

~74 kDa observed. This antibody detects A form prelamin but does not detect isoform C.

Format: Purified

Protein G Purified

Purified rat monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.

Concentration: Please refer to lot specific datasheet.

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