| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | E3 SUMO protein ligase TRIM28 antibody; E3 SUMO-protein ligase TRIM28 antibody; FLJ29029 antibody; KAP 1 antibody; KAP-1 antibody; KRAB associated protein 1 antibody; KRAB interacting protein 1 antibody; KRAB-associated protein 1 antibody; KRAB-interacting protein 1 antibody; KRIP 1 antibody; KRIP-1 antibody; KRIP1 antibody; Nuclear corepressor KAP 1 antibody; Nuclear corepressor KAP-1 antibody; RING finger protein 96 antibody; RNF96 antibody; TF1B antibody; TIF1 beta antibody; TIF1-beta antibody; TIF1B antibody; TIF1B_HUMAN antibody; Transcription intermediary factor 1 beta antibody; Transcription intermediary factor 1-beta antibody; Trim28 antibody; Tripartite motif containing 28 antibody; tripartite motif containing protein 28 antibody; Tripartite motif-containing protein 28 antibody |
| 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
Anti-Lamin A+C/LMNA Antibody Picoband® (monoclonal, 5F3C12) is an antibody reagent for detection of LMNA (tripartite motif containing 28). Researchers commonly use anti-LMNA antibodies to measure relative expression and localization across biological samples, with assay selection guided by the listed applications (WB, IHC, Flow, ELISA).
Boster Bio Anti-Lamin A+C/LMNA Antibody Picoband® (monoclonal, 5F3C12) catalog # M00438-6. Tested in IHC, 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
- Target: LMNA — Membrane cofactor protein (tripartite motif containing 28). Alternative names: E3 SUMO protein ligase TRIM28 antibody; E3 SUMO-protein ligase TRIM28 antibody; FLJ29029 antibody; KAP 1 antibody; KAP-1 antibody; KRAB associated protein 1 antibody; KRAB interacting protein 1 antibody; KRAB-associated protein 1 antibody; KRAB-interacting protein 1 antibody; KRIP 1 antibody; KRIP-1 antibody; KRIP1 antibody; Nuclear corepressor KAP 1 antibody; Nuclear corepressor KAP-1 antibody; RING finger protein 96 antibody; RNF96 antibody; TF1B antibody; TIF1 beta antibody; TIF1-beta antibody; TIF1B antibody; TIF1B_HUMAN antibody; Transcription intermediary factor 1 beta antibody; Transcription intermediary factor 1-beta antibody; Trim28 antibody; Tripartite motif containing 28 antibody; tripartite motif containing protein 28 antibody; Tripartite motif-containing protein 28 antibody
- Antibody format: Monoclonal; clone 5F3C12; IgG2b
- Species context: Host: Mouse, Reactivity: Human,Mouse,Rat
- Purification: Immunogen affinity purified.
- 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.
- Molecular weight context: observed 74 kDa (reported)
- Provided application(s): WB, IHC, Flow, ELISA
These attributes help contextualize how the antibody is commonly selected (host/clonality/isotype/label) and how signals are interpreted across sample types and assay formats.
Biological background
Function: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21 (CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway. Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions. Acts as a corepressor for ZFP568. (Microbial infection) Plays a critical role in the shutdown of lytic gene expression during the early stage of herpes virus 8 primary infection. This inhibition is mediated through interaction with herpes virus 8 protein LANA1.
Cellular localization: Nucleus.
Tissue details: Expressed in all tissues tested including spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.
Background: 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.
Cross reactivity: No cross-reactivity with other proteins.
Research relevance and current trends
- Quantitative and spatial profiling: expression patterns are increasingly studied across cell states using multiplex imaging and omics-informed validation.
- Isoforms and post-translational modifications: researchers often evaluate how isoform composition and PTMs can shift apparent molecular weight or localization.
- Context-aware interpretation: comparative studies commonly include perturbations (stimulation, inhibition, genetic models) to relate target changes to pathway behavior.
Common research applications
- Western blot (WB): compare relative target abundance and apparent size shifts (e.g., isoforms/PTMs) across conditions.
- Immunohistochemistry (IHC): assess distribution across tissue compartments and compare staining patterns between groups.
- Flow cytometry: quantify target-positive populations and compare shifts after stimulation or differentiation.
Across these uses, researchers typically interpret changes in signal as relative differences between matched sample groups, considering sample preparation and biological context.
Notes for experimental interpretation
- Apparent molecular weight can vary due to isoforms, proteolysis, glycosylation, phosphorylation, and sample preparation differences.
- Species reactivity and epitope conservation can influence observed signal patterns, especially in cross-species studies.
- Control concepts: include appropriate negative controls (e.g., isotype controls where relevant) and, when feasible, genetic or orthogonal controls (KO/KD, peptide competition, or independent assays) to support interpretation.
For antibody reagents, monoclonal antibodies are often chosen for epitope consistency across lots, while polyclonals may recognize multiple epitopes and can show different background characteristics depending on context.
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.