The nuclear envelope (NE) is a double-membraned structure that encloses the nucleus in eukaryotic cells. It is made up of two lipid bilayers that are separated by a perinuclear space of 40–50 nm. The outer membrane is contiguous with the endoplasmic reticulum, while the inner membrane is composed of a distinct set of lipids and proteins. The NE plays a crucial role in separating the genetic material in the nucleus from the cytoplasm and ensuring its proper organization. As a result, the NE is involved in a number of fundamental cellular processes, including DNA replication, transcription, and cell division. During cell division, the nuclear envelope breaks down and reforms to ensure proper segregation of genetic material to daughter cells. The NE also acts as a selective permeability barrier, regulating the exchange of materials between the nucleus and cytoplasm. The transport of materials into and out of the nucleus is mediated by nuclear pore complexes, which are large protein channels embedded in the NE. The inner nuclear membrane is lined with a complex meshwork of proteins called the nuclear lamina. It is involved in several fundamental cellular processes, including DNA replication, DNA repair, transcription, chromatin organization, cell cycle regulation, differentiation, apoptosis, and nuclear migration. The main structural components of the nuclear lamina are the lamin family proteins, including lamin A/C, lamin B1, and lamin B2. These intermediate filament proteins form a dense fibrillar network and are crucial for maintaining the mechanical stability of the nucleus. The lamins are phosphorylated during mitosis, which initiates their reversible disassembly and promotes mitotic progression. Mutations in the genes encoding the lamins are implicated in several diseases, collectively called laminopathies. These include premature ageing syndromes, muscular dystrophies, cardiomyopathies, metabolic diseases, and neuropathies. In addition to lamins, the nuclear lamina contains a number of other integral or peripheral membrane proteins, including emerin, Man1, lamina-associated polypeptides 1 and 2 (LAP1 and LAP2), LEM2, barrier-to-autointegration factor (BAF), HP1, and SUN-domain proteins (SUN1 and SUN2). SUN-domain proteins, embedded in the inner nuclear membrane, interact in the perinuclear space with KASH-domain proteins, embedded in the outer nuclear membrane. KASH-domain proteins, including Nesprin1, Nesprin2, and Nesprin3, interact through their cytoplasmic regions with cytoskeletal elements, including actin, microtubules and intermediate filaments. Together, SUN-KASH proteins form LINC complexes, which mediate interactions between the nuclear interior and cytoplasmic cytoskeleton. LINC complexes are required for nuclear migration and play a role in nuclear mechanotransduction, the transmission of mechanical forces to the nuclear interior to modulate signaling pathways and gene expression. We offer a range of nuclear envelope markers including Lamin A + C antibodies and Lamin B1 antibodies, that are validated in multiple applications including western blotting (WB), immunocytochemistry (ICC), and immunohistochemistry (IHC).