For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 19; NC_000019.9 (2428164..2456958, complement). Location: 19p13.3

Monoclonal

IgG1

LN43

Mouse

LN43 reacts with an epitope loCated in the C-terminal part of lamin B2.

Each vial contains 100 ul 1 mg/ml purified monoclonal antibody in PBS containing 0.09% sodium azide.

Store at 4 degree C, or in small aliquots at -20 degree C.

Small volumes of anti-LMNB2 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Nuclear lamins form a network of intermediate-type filaments at the nucleoplasmic site of the nuclear membrane. Two main subtypes of nuclear lamins can be distinguished, i.e. A-type lamins and B-type lamins. The A-type lamins comprise a set of three proteins arising from the same gene by alternative splicing, i.e. lamin A, lamin C and lamin Adel 10, while the B-type lamins include two proteins arising from two distinct genes, ie lamin B1 and lamin B2.

Nuclear proteins, Cytoskeleton

Flow Cytometry (FC), Immunohistochemistry (IHC) (frozen), Western Blot (WB)

LN43 is suitable for immunohistochemistry on frozen sections, immunoblotting and flow cytometry. Optimal antibody dilution should be determined by titRation; recommended range is 1:100 - 1:200 for flow cytometry, and for immunohistochemistry with avidin-biotinylated Horseradish peroxidase complex (ABC) as detection reagent, and 1:100 - 1:1000 for immunoblotting appliCations.

Figure 1: Immunohistochemistry on frozen sections of human kidney showing nuclear lamina staining in the ductal epithelium

Figure 2: Immunofluorescence staining of a 9 days old zebrafish embryo

67,689 Da[Similar Products]

lamin B2

lamin-B2; OTTHUMP00000198023

Lamin-B2

LMN2??[Similar Products]

LMNB2_HUMAN

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. This gene encodes one of the two B type proteins, B2. This gene is in a head-to-tail orientation with the gene for the translocase of inner mitochondrial membrane 13 homolog gene. [provided by RefSeq]

Lamin B2: nuclear lamins are intermediate filament proteins that constitute the lattice-like matrix at the inner face of the nuclear membrane that underlies the nuclear envelop. The lamins, highly conserved throughout evolution, are encoded by three genes in the human: LMNA, LMNB1, and LMNB2. The A-type lamins (lamin A/C) are developmentally regulated and are generally expressed in differentiated cells. The anchoring of chromatin to the nuclear lamina is involved in the control of gene expression and in DNA replication and repair. During mitosis, the nuclear lamina is reversibly disassembled as the lamin proteins are phosphorylated. B-type lamins are phosphorylated within minutes of engaging the IgM surface receptor of resting splenic B cells. Lamin B2 may be lost during the follicle centre stage of B-cell differentiation in humans. Nuclear lamins are cleaved by caspases during apoptosis.

Protein type: Motility/polarity/chemotaxis; Cytoskeletal

Chromosomal Location of Human Ortholog: 19p13.3

Cellular Component: lamin filament; nuclear inner membrane

Molecular Function: structural molecule activity

Disease: Lipodystrophy, Partial, Acquired, Susceptibility To

Bridger, J. M., Kill, I. R., O'Farrell, M., and Hutchison, C. J. (1993). Internal lamin structures within G1 nuclei of Human dermal fibroblasts, J Cell Sci 104, 297-306. Jenkins, H., H?lman, T., Lyon, C., Lane, B., Stick, R., and Hutchison, C. J. (1993). Nuclei that lack a lamina accumulate karyophilic proteins and assemble a nuclear matrix, J Cell Sci 106, 275-285. Hozak, P., Sasseville, A. M., Raymond, Y., and Cook, P. R. (1995). Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in Human cells, J Cell Sci 108, 635-44. Machiels, B. M., Broers, J. L., Raymond, Y., de Ley, L., Kuijpers, H. J., Caberg, N. E., and Ramaekers, F. C. (1995). Abnormal A-type lamin organization in a Human lung carcinoma cell line, Eur J Cell Biol 67, 328-35. Machiels, B. M., Zorenc, A. H., Endert, J. M., Kuijpers, H. J., van Eys, G. J., Ramaekers, F. C., and Broers, J. L. (1996). An alternative splicing product of the lamin A/C gene lacks exon 10, J Biol Chem 271, 9249-53. Machiels, B. M., Ramaekers, F. C., Kuijpers, H. J., Groenewoud, J. S., Oosterhuis, J. W., and Looijenga, L. H. (1997). Nuclear lamin expression in normal testis and testicular germ cell tumours of adolescents and *****s, J Pathol 182, 197-204. Jansen, M. P., Machiels, B. M., Hopman, A. H., Broers, J. L., Bot, F. J., Arends, J. W., Ramaekers, F. C., and Schouten, H. C. (1997). Comparison of A and B-type lamin expression in reactive lymph nodes and nodular sclerosing Hodgkin's disease, Histopathology 31, 304-12. Broers, J. L., Machiels, B. M., Kuijpers, H. J., Smedts, F., van den Kieboom, R., Raymond, Y., and Ramaekers, F. C. (1997). A- and B-type lamins are differentially expressed in normal Human tissues, Histochem Cell Biol 107, 505-17.

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