Lamin A/C antibody | JOL2
Mouse anti Human lamin A/C, clone JOL2, recognizes both recombinant and native forms of human lamin A and C, nuclear intermediate filament proteins encoded by the same LMNA gene via alternative splicing. In addition to providing structural support to the nuclear envelope, these proteins contribute to chromatin organisation and the regulation of gene expression.
Mutations in the LMNA gene are responsible for a broad spectrum of disorders, termed laminopathies, including Emery-Dreifuss muscular dystrophy and dilated cardiomyopathy.
The JOL2 clone has been shown to bind to an epitope between amino acids 464-572.
Mutations in the LMNA gene are responsible for a broad spectrum of disorders, termed laminopathies, including Emery-Dreifuss muscular dystrophy and dilated cardiomyopathy.
The JOL2 clone has been shown to bind to an epitope between amino acids 464-572.
Product Details
- Target Species
- Human
- Species Cross-Reactivity
-
Target Species Cross Reactivity Xenopus - N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Preparation
- Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
0.09% Sodium Azide - Immunogen
- Recombinant human lamin A
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised Balb/c mice were fused with cells of the mouse SP2-0/Ag4 myeloma cell line
Storage Information
- Storage
- Store at +4oC or at -20oC if preferred.
This product should be stored undiluted.
Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use. - Guarantee
- 18 months from date of despatch.
More Information
- UniProt
- P02545
- Entrez Gene
- LMNA
- GO Terms
- GO:0005515 protein binding
- GO:0005198 structural molecule activity
- GO:0005635 nuclear envelope
- GO:0005638 lamin filament
- GO:0005737 cytoplasm
- GO:0006921 cellular component disassembly involved in apoptosis
- GO:0007517 muscle organ development
- GO:0048471 perinuclear region of cytoplasm
- GO:0090343 positive regulation of cell aging
- Regulatory
- For research purposes only
Applications of Lamin A/C antibody
| Application Name | Verified | Min Dilution | Max Dilution |
|---|---|---|---|
| Flow Cytometry | |||
| Immunofluorescence | |||
| Immunohistology - Frozen | |||
| Immunohistology - Paraffin 1 | 0.4 ug/ml | ||
| Immunoprecipitation | |||
| Western Blotting |
- 1Mouse anti lamin A/C requires antigen retrieval using heat treatment prior to staining of paraffin sections. Citrate buffer pH 6.2 is recommended for this purpose.
Where this product has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own system using appropriate negative/positive controls.
- Histology Positive Control Tissue
- Human colon
Copyright © 2020 Bio-Rad Antibodies (formerly AbD Serotec)
Secondary Antibodies Available
Negative Isotype Controls Available
| Description | Product Code | Applications | Pack Size | List Price | Quantity |
|---|---|---|---|---|---|
| Mouse IgG1 Negative Control | MCA928 | F | 100 Tests |
|
Product Specific References
References for Lamin A/C antibody
-
Tilgner, K. et al. (2009) Dynamic complexes of A-type lamins and emerin influence adipogenic capacity of the cell via nucleocytoplasmic distribution of beta-catenin.
J Cell Sci. 122: 401-13. -
Ivorra, C. et al. (2006) A mechanism of AP-1 suppression through interaction of c-Fos with lamin A/C.
Genes Dev. 20: 307-20. -
Navarro, C.L. et al. (2004) Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy.
Hum Mol Genet. 13: 2493-503. -
Cummings, M. et al. (2006) XPA versus ERCC1 as chemosensitising agents to cisplatin and mitomycin C in prostate cancer cells: role of ERCC1 in homologous recombination repair.
Biochem Pharmacol. 72: 166-75. -
Markiewicz, E. et al. (2006) The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus.
EMBO J. 25: 3275-85. -
Zhang, Q. et al. (2007) Nesprin-1 and -2 are involved in the pathogenesis of Emery Dreifuss muscular dystrophy and are critical for nuclear envelope integrity.
Hum Mol Genet. 16: 2816-33. -
Jean, D. et al. (2008) Cathepsin L expression is up-regulated by hypoxia in human melanoma cells: role of its 5'-untranslated region.
Biochem J. 413: 125-34. -
Ndong, Jde. L. et al. (2009) Down-regulation of the expression of RB18A/MED1, a cofactor of transcription, triggers strong tumorigenic phenotype of human melanoma cells.
Int J Cancer. 124: 2597-606.
