Anti-Lamin A+C/LMNA Antibody Picoband® (monoclonal, 5F3C12), HRP Conjugate

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.

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

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.

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.

1. Lammerding, J.; Schulze, P. C.; Takahashi, T.; Kozlov, S.; Sullivan, T.; Kamm, R. D.; Stewart, C. L.; Lee, R. T. : Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction. J. Clin. Invest. 113: 370-378, 2004. 2. Lin, F.; Worman, H. J. : Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem. 268: 16321-16326, 1993. 3. Wydner, K. L.; McNeil, J. A.; Lin, F.; Worman, H. J.; Lawrence, J. B. : Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization. Genomics 32: 474-478, 1996.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.