Lamin B2 (HRP)

Référence L1220-35-HRP-100ul

Conditionnement : 100ul

Marque : US Biological

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L1220-35-HRP Lamin B2 (HRP)

Clone Type
Polyclonal
Host
mouse
Swiss Prot
Q03252
Isotype
IgG1
Grade
Purified
Applications
IC WB
Crossreactivity
Hm Hu Mo Xe
Accession #
NM_032737.2
Shipping Temp
Blue Ice
Storage Temp
-20°C

Nuclear lamins form a network of filaments at the nucleoplasmic site of the nuclear membrane. Two main subtypes of nuclear lamins can be distinguished: 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, i.e. lamin B1 and lamin B2. Type A lamins comprise a set of three proteins arising from the same gene by alternative splicing: lamins A, C, and Adel 10. B-type lamins include two proteins arising from two distinct genes, i.e. lamin B1 and lamin B2. Mutations in A-lamins give rise to a range of genetic disorders, including autosomal dominant Emery-Dreifuss muscular dystrophy (AD-EDMD), dilated cardiomyopathy and Dunnigan-type familial partial lipodystrophy. Aberrant expression patterns of nuclear lamins have been described in various types of cancer depending on the subtype of cancer, its aggressiveness, proliferative capacity and degree of differentiation. In general, the expression of A-type lamins (lamins A and C) has been correlated with a non-proliferating, differentiated state of cells and tissues. Lamins A and C, the products of the LMNA gene, are nuclear intermediate filament proteins and are the major structural components of the lamina network that underlies and supports the nuclear envelope. Expression of A-lamin coincides with cell differentiation and may be related protein’s abnormal expression and organization in neoplastic tissues and cells.||Applications: |Suitable for use in Western Blot and Immunocytochemistry. Other applications not tested. ||Recommended Dilution: |Immunocytochemistry: Methanol/acetone fixation |Optimal dilution determined by the researcher. ||Storage and Stability:|Store product at 4°C if to be used immediately within two weeks. For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C. Aliquots are stable at -20°C for 12 months after receipt. Dilute required amount only prior to immediate use. Further dilutions can be made in assay buffer. Note: Sodium azide is a potent inhibitor of peroxidase and should not be added to HRP conjugates. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.||Note: Applications are based on unconjugated antibody.

Applications
Product Type: Mab|Isotype: IgG1|Clone No: 2Q1130 (LN43)|Host: mouse|Concentration: As Reported|Form: Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).|Purity: Purified from culture supernatant|Immunogen: Detergent insoluble fraction of potoroo cell line PtK1.|Specificity: Recognizes an epitope located in the C-terminal part of Lamin B2. Species Crossreactivity: human, mouse, hamster and Xenopus.||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Detergent insoluble fraction of potoroo cell line PtK1.
Form
Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with horseradish peroxidase (HRP).
Purity
Purified from culture supernatant
Specificity
Recognizes an epitope located in the C-terminal part of Lamin B2. Species Crossreactivity: human, mouse, hamster and Xenopus.
References
1. 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. 2. 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. 3. 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. 4. 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. 5. 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