Abcam, ab248435, Anti-Cleaved Lamin A + C (Asp230) antibody [EPR4520-11] - BSA and Azide free

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal Lamin-A/C antibody. Carrier free. Suitable for WB and reacts with Mouse, Human samples. Cited in 1 publication.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR4520-11,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Mouse, Human,
Applications:WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
ab248435 is the carrier-free version of
ab133269
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Cleaved Lamin A + C (Asp230) also known as Progerin refers to a post-translationally modified form of A-type lamins that results from caspase-mediated cleavage at Asp230. The mass of Lamin A is approximately 74 kDa while Lamin C is around 65 kDa. These proteins mainly localize to the nuclear lamina a structural layer beneath the inner nuclear membrane. They express in a variety of tissues but are particularly abundant in cells with a high demand for nuclear structural integrity such as skin heart and muscle tissues.
Biological function summary
These cleaved lamins play a pivotal role in maintaining nuclear shape and stability. They serve as integral components of the nuclear lamina which is part of a complex scaffold that provides mechanical support to the nucleus. Cleaved Lamin A + C also aids in chromatin organization influencing gene expression. Their function impacts key cellular processes like DNA replication and repair as well as regulation of the cell cycle.
Pathways
The involvement of Cleaved Lamin A + C is important within apoptosis and cellular senescence pathways. They interact with proteins such as Caspase-6 and Caspase-7 in these processes. Lamin cleavage leads to nuclear disassembly during programmed cell death while in cellular senescence it signals alterations in nuclear integrity that influence aging-related pathways.
Cleaved Lamin A + C associates with accelerated aging disorders such as Hutchinson-Gilford Progeria Syndrome (HGPS). In this condition the accumulation of mutated lamin proteins results in defective nuclear architecture. Disorders like muscular dystrophy present a link as well where abnormal proteins like Emerin and Nesprin could interact with lamins affecting muscle cell viability and function.