For research use only.
| Verified Samples | Verified Samples in WB: U251, Lncap, A549 Verified Samples in IHC: Human breast cancer |
| Dilution | WB 1:1000-1:2000, IHC 1:50-1:100 |
| Isotype | IgG |
| Host | Rabbit |
| Reactivity | Human, Mouse |
| Applications | WB, IHC-P |
| Clonality | Rabbit Monoclonal |
| Immunogen | A synthetic peptide of human Lamin A/C |
| Abbre | Lamin A/C |
| Synonyms | 70 kDa lamin, CDCD1, CDDC, CMD1A, CMT2B1, Cardiomyopathy dilated 1A (autosomal dominant), EMD2, FPL, FPLD, FPLD2, HGPS, IDC, LDP1, LFP, LGMD1B, LMN 1, LMN A, Lamin, Lamin A, Lamin A/C, Lamin A/C like 1, Lamin C, Lamin-A/C, Limb girdle muscular dystrophy 1B (autosomal dominant) |
| Swissprot | |
| Calculated MW | 74 kDa |
| Observed MW | 74 /63 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. Nucleus envelope. 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. |
| Concentration | 300 μg/mL |
| Buffer | 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40% Glycerol, 0.05% stabilizer and 0.05% protective protein. |
| Purification Method | Affinity Purified |
| Research Areas | Cancer, Signal Transduction, Tags and Cell Markers |
| Clone No. | R07-1I5 |
| 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 | The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. 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. Vertebrate lamins consist of two types, A and B. Alternative splicing results in multiple transcript variants. |
Other Clones
1 Results
Other Formats
1 Results
Unconjugated
