Lamin fragment

Short Summary : Lys-Ala-Gly-Gln-Val-Val-Thr-Ile-Trp

Category : Bioactive Peptides

Purity : 0.9376

CAS Number :

Formula : C47H76N12O12

Molecular Weight : 1001.18

SMILE : NC(CCCCN)C(NC(C)C(NCC(NC(CCC(N)=O)C(NC(C(C)C)C(NC(C(C)C)C(NC(C(C)O)C(NC(C(C)CC)C(NC(CC1=CNC2=C1C=CC=C2)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O

Solubility : Soluble in DMSO

Storage : Store at -20°C

Description : Lamin fragment has a peptide sequence of Lys-Ala-Gly-Gln-Val-Val-Thr-Ile-Trp.
The lamins are type V intermediate filaments which can be categorized as either A-type (lamin A, C) or B-type (lamin B1, B2) according to homology in sequence, biochemical properties and cellular localization during the cell cycle. Lamin polypeptides have an almost complete α-helical conformation with multiple α-helical domains separated by non-α-helical linkers that are highly conserved in length and amino acid sequence.
Nuclear lamins are intermediate filament-type proteins that are the major building blocks of the nuclear lamina, a fibrous proteinaceous meshwork underlying the inner nuclear membrane. Lamins can also be localized in the nuclear interior, in a diffuse or spotted patter. Lamins also play roles in DNA replication, chromatin organization, spatial arrangement of nuclear pore complexes, nuclear growth, and anchorage of nuclear envelope proteins.
Figure 1: Lamin fragment
Ref:
1. The Cell: A Molecular Approach, Cooper & Hausman. 5th Edition. Pg. 357
2. Ayelet Margalit, Sylvia Vlcek, Yozef Gruenbaum, Roland Foisner (2005). Breaking and Making of the Nuclear Envelope. Journal of Cellular Biochemistry 95, 454-465
3. Bruce Alberts, et al. Molecular Biology of the Cell (4th edition). Garland Science 676-677
4. Geoffrey M. Cooper, Robert E. Hausman. The Cell, A Molecular Approach (4th edition). Sinauer Associates 356-360
5. Goldman et al.(2002). “Nuclear lamins: building blocks of nuclear architecture”. Genes and Development 16,533-547
6. Joanna M. Bridger, Nicole Foeger, Ian R. Kill, Harald Herrmann (2007). The Nuclear Lamina: both a structural framework and a platform for genome organization. FEBS Journal 274, 1354–1361
7. Nico Stuurman, Susanne Heins, Ueli Aebi (1998). Nuclear Lamins: Their Structure, Assembly and Interactions. Journal of Structural Biology 122, 42-46
8. Tripathi K, Muralikrishna B and Parnaik VK (2009) Differential dynamics and stability of lamin A rod domain mutants IJIB, 5(1), 1-8
9. Yozef Gruenbaum, Katherine L. Wilson, Amnon Harel, Michal Goldberg, Merav Cohen (2000). Nuclear Lamins – Structural Proteins with fundamental functions. Journal of Structural Biology129, 313-323

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