| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Prelamin-A/C;Lamin-A/C;70 kDa lamin;Renal carcinoma antigen NY-REN-32;LMNA;LMN1; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Form | Liquid |
| Host | |
| Immunogen | A synthesized peptide derived from human Lamin A/C |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Storage | |
| Target | |
| UniProt # |
Overview
This product is an anti-LMNA antibody for target detection and characterization. Key identifiers include host species: Rabbit; Monoclonal; clone 22L53; isotype IgG; reactivity: Human,Mouse,Rat. Reported application contexts include WB, IHC, ICC, IF, Flow (as provided in the source record). Boster Bio Anti-Lamin A/C Rabbit Monoclonal Antibody catalog # M00438-5. Tested in WB, IHC, ICC/IF, Flow Cytometry applications. This antibody reacts with Human, Mouse, Rat.
Key elements and design rationale
- Target: LMNA (Prelamin-A/C).
- Antibody format: Monoclonal; clone 22L53; isotype IgG.
- Host: Rabbit.
- Species reactivity: Human,Mouse,Rat (confirm in your model system with appropriate controls).
This description is intended to help interpret the antibody design and the biological context of the target using the fields provided in the catalog record, alongside general experimental considerations.
Biological background
LMNA (protein: T-cell surface glycoprotein CD4) is a commonly studied target in molecular and cellular biology. Functional context (as provided): Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone. Reported cellular localization context: Nucleus. Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin- A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C. Tissue expression notes (as provided): In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress. .
Research relevance and current trends
- Research context keywords from the source record include: Cytoskeleton,Cytoskeleton/ECM,Intermediate Filaments,Nucleus,Signal Transduction,Subcellular Markers,Tags & Cell Markers.
- Current studies often focus on connecting target abundance/localization to pathway perturbations across models, tissues, and cell states.
- Quantitative and multiplexed assays (e.g., imaging + immunoblot panels) are commonly used to compare phenotypes across conditions and time-courses.
Common research applications
- Western blotting (WB): assess relative target abundance across samples, treatments, or time-points.
- Immunohistochemistry (IHC): evaluate spatial distribution of target-positive staining in tissue architecture.
- Immunofluorescence/ICC (IF/ICC): visualize subcellular localization patterns and cell-to-cell heterogeneity.
- Flow cytometry: quantify target-positive populations and compare shifts in marker distributions.
Workflow ideas (metafield): Validate LMNA antibody specificity using KO/KD control samples (WB/IF/IHC as appropriate), Detect LMNA expression by Western blot in cell or tissue lysates, Detect LMNA in FFPE tissue sections by immunohistochemistry, Localize LMNA by immunofluorescence/immunocytochemistry in cultured cells, Quantify LMNA-positive cells by flow cytometry in single-cell suspensions
Notes for experimental interpretation
- Consider isoforms and post-translational modifications (PTMs) that may shift apparent molecular weight or epitope accessibility.
- Apparent molecular weight may vary by sample type and processing (observed MW: 70-74 kDa; calculated MW: 74139 MW).
- Control concepts: include appropriate negative controls (e.g., isotype, KO/KD samples) and orthogonal validation when feasible.
Additional product details (from the source record)
- Molecular weight (observed): 70-74 kDa
- Cellular localization (provided): Nucleus. Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin- A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C.
- Tissue details (provided): In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress. .
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