Description

Background:

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. Alternative splicing results in multiple transcript variants. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. [provided by RefSeq, Apr 2012]

Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone.

Product datasheet:

Overview

Product Description   Phospho-Lamin A/C (S22) Polyclonal Antibody, 100µg, (ATB-P0485)
Image
Species ReactivitiesHuman,Mouse,Rat
ImmunogenSynthesized peptide derived from human Lamin A/C around the phosphorylation site of S22.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. [Nuclear lamins regulate osteogenic differentiation of mesenchymal stem cells]. Bogdanova MA, et al. Tsitologiia, 2014. PMID 25509159
  2. Characterization of unfolding mechanism of human lamin A Ig fold by single-molecule force spectroscopy-implications in EDMD. Bera M, et al. Biochemistry, 2014 Nov 25. PMID 25343322
  3. Antisense oligonucleotide induction of progerin in human myogenic cells. Luo YB, et al. PLoS One, 2014. PMID 24892300 Free PMC Article
  4. Interphase phosphorylation of lamin A. Kochin V, et al. J Cell Sci, 2014 Jun 15. PMID 24741066
  5. Phenotypic intermediate forms overlapping to Emery-Dreifuss and limb girdle muscular dystrophies caused by lamin A/C gene mutations. Albuquerque MA, et al. Pediatr Neurol, 2014 May. PMID 24656463
  6. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins.
    McKeon F.D., Kirschner M.W., Caput D.
    Nature 319:463-468(1986) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
  7. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins.
    Fisher D.Z., Chaudhary N., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 83:6450-6454(1986) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C), PROTEIN SEQUENCE OF 583-644.
  8. In vivo and in vitro examination of the functional significances of novel lamin gene mutations in heart failure patients.
    Sylvius N., Bilinska Z.T., Veinot J.P., Fidzianska A., Bolongo P.M., Poon S., McKeown P., Davies R.A., Chan K.-L., Tang A.S.L., Dyack S., Grzybowski J., Ruzyllo W., McBride H., Tesson F.
    J. Med. Genet. 42:639-647(2005) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION (ISOFORM C), VARIANTS CMD1A TRP-190; GLY-192 AND SER-541, CHARACTERIZATION OF VARIANTS CMD1A GLY-192 AND SER-541.
  9. The progerin allele of lamin A disrupts chromatin organization.
    Csoka A.B.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
  10. Complete sequencing and characterization of 21,243 full-length human cDNAs.
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Corpus callosum.

external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

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