| 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 | |
| Host | |
| Immunogen | E.coli-derived human Lamin A/C recombinant protein (Position: Y481-Y646). Human Lamin A/C shares 90% and 92% amino acid (aa) sequence identity with mouse and rat Lamin A/C, respectively. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of LMNA (Prelamin-A/C) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-Lamin A+C/LMNA Antibody Picoband® catalog # PB9280. Tested in Flow Cytometry, IF, IHC, ICC, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: E.coli-derived human Lamin A/C recombinant protein (Position: Y481-Y646). Human Lamin A/C shares 90% and 92% amino acid (aa) sequence identity with mouse and rat Lamin A/C, respectively. (reported region: Y481-Y646).
- Molecular weight context: reported MW: 74 kDa, 63 kDa; calculated MW: 74139 MW
- Reactivity: Human,Mouse,Rat
- Applications: Flow Cytometry, IF, IHC, ICC, WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
Prelamin-A/C; Prelamin-A/C. Lamins are structural protein components of the nuclear lamina, a protein network underlying the inner nuclear membrane that determines nuclear shape and size. There are three types of lamins, A,B and C. The lamin A/C (LMNA) gene contains 12 exons. Alternative splicing within exon 10 gives rise to two different mRNAs that code for pre-lamin A and lamin C. Lamin A/C is mapped to 1q21.2-q21.3 and mutations in this gene cause a variety of human diseases including Emery-Dreifuss muscular dystrophy, dilated cardiomyopathy, and Hutchinson-Gilford progeria syndrome. Lamin A/C deficiency is thus associated with both defective nuclear mechanics and impaired mechanically activated gene transcription. Functional note: 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 localization: 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. Expression/tissue context: 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
- Cytoskeleton: Researchers commonly examine how LMNA (Prelamin-A/C) relates to this theme using model systems and orthogonal readouts.
- Cytoskeleton/ECM: Researchers commonly examine how LMNA (Prelamin-A/C) relates to this theme using model systems and orthogonal readouts.
- Intermediate Filaments: Researchers commonly examine how LMNA (Prelamin-A/C) relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative LMNA (Prelamin-A/C) levels across conditions; band patterns may reflect isoforms and processing.
- IHC/IHC-F: assess spatial distribution of LMNA (Prelamin-A/C) across tissue regions and cell types using matched controls.
- IF/ICC: evaluate subcellular localization and co-localization patterns; signal can depend on fixation/permeabilization and epitope accessibility.
- Flow cytometry: quantify target-positive populations and shifts in expression; gating strategy and background staining controls are essential.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins
- Family / similarity context: Belongs to the intermediate filament family.
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.