Anti-Human Lamin A/C (Clone 4C11) - Purified No Carrier Protein - 25 µg

IF Microscopy, IP, WB

2 - 8°C Wet Ice

The nucleoplasm is separated from the cytoplasm by a bilayer nuclear envelope that consists ofouter and inner nuclear membranes, nuclear pore complexes, and the nuclear lamina, which is atwo-dimensional matrix composed mainly of type V intermediate filament proteins called lamins1. Lamins are encoded by a family of three genes that collectively produce lamins B1, B2, B3, AΔ10, C2, and A/C. Lamin A/C plays a variety of roles in the nucleus including, but not limitedto: nuclear mechanical stability, structural maintenance, positioning, chromatin organization, epigenetic regulation, transcription, DNA replication, cell cycle progression, differentiation, migration, and polarization. Additionally, lamin A/C is variably expressed in human immunecells during different stages of cell development and activation states. 4C11 was raised against the wild-type Ig-fold domain of lamin A/C (aa 430–545)2. This domainis located in the C-terminal globular domain of the protein’s tripartite structure. A BALB/cmouse was immunized with antigen and splenocytes fused with myeloma cell line X63Ag8.653.4C11 detects both lamins A and C.

≥1.0 mg/ml

Lamin A/C is abundantly expressed in most differentiated cells but notpluripotent stem cells and embryos during development. Lamin A/C is expressed at high levelsin macrophages and dendritic cells but is barely detectable in inactivated T and B cells.Neutrophils lose lamin A/C expression during maturation. T cells exhibit a transient peak inlamin A/C upon antigen recognition. Some B cell lymphomas express lamin A/C.