Lamin A/C Monoclonal Antibody (AN005340L)
For research use only.
| Verified Samples |
Verified Samples in WB: SH-SY5Y, HL-60, U-87 MG, Hep G2 Verified Samples in IF: HeLa, U-2 OS |
| Dilution | WB 1:2000-1:4000, IF 1:500-1:1000 |
| Isotype | IgG1 |
| Host | Mouse |
| Reactivity | Human |
| Applications | WB, IF |
| Clonality | Monoclonal |
| Immunogen | Recombinant human Lamin A/C protein expressed by E.coli |
| Abbre | Lamin A/C |
| Synonyms | Prelamin-A/C, LMNA, LMN1, Lamin A/C |
| Swissprot | |
| Calculated MW | 65 kDa |
| Observed MW |
70,80 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Nucleus lamina, Nucleus envelope, Nucleus |
| Tissue Specificity | 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. |
| Concentration | 1 mg/mL |
| Buffer | PBS with 0.05% proclin 300, 1% protective protein and 50% glycerol,pH7.4 |
| Purification Method | Protein A/G Purification |
| Research Areas | Signal Transduction, Tags and Cell Markers, Cancer, Cell Biology, Developmental Biology, Epigenetics and Nuclear Signaling, Biochemicals |
| Clone No. | 4F1 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | The product is shipped with ice pack, upon receipt, store it immediately at the temperature recommended. |
| background | Lamin A/C is also named as LMNA,or LMN1. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis,the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability,chromatin structure and gene expression. The lack of lamin A/C can be as a novel marker for undifferentiated embryonic stem cells and lamin A/C expression is as an early indicator of differentiation (PMID: 16179429). Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy,familial partial lipodystrophy,limb girdle muscular dystrophy,dilated cardiomyopathy,Charcot-Marie-Tooth disease,and Hutchinson-Gilford progeria syndrome. This protein has 4 isoforms produced by alternative splicing with the molecular weight of 74 kDa,65 kDa,70 kDa and 64 kDa. This antibody can recognize 4 isoforms of Lamin A/C. |
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