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L1293

Sigma-Aldrich

Anti-Lamin A (C-terminal) antibody produced in rabbit

enhanced validation

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-LAMA, Anti-LMN1, Anti-LMNA, Anti-Lamin A/C

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~70 kDa

Espèces réactives

rat, human, mouse

Validation améliorée

independent
Learn more about Antibody Enhanced Validation

Concentration

~1 mg/mL

Technique(s)

indirect immunofluorescence: 1-2 μg/mL using human HeLa, rat NRK, and mouse 3T3 cells
western blot: 0.1-0.2 μg/mL using human HeLa nuclear extract

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... LMNA(4000)
mouse ... Lmna(16905)
rat ... Lmna(60374)

Description générale

Lamin is a structural protein of the nuclear lamina. Lamin A is a type A lamin encoded by the LMNA gene. Lamin A contains 664 amino acids and is expressed in most somatic cells. It contains α-helical rod domain to enable assembly into filaments, a nuclear localization sequence, and a carboxy-terminal CAAX box isoprenylation sequence for nuclear membrane targeting.

Immunogène

synthetic peptide corresponding to amino acids 598-611 of human lamin A with a C-terminal added cysteine, conjugated to KLH. The corresponding sequence differs by one amino acid in rat, three amino acids in mouse, and by a gap of one amino acid in both rat and mouse lamin A.

Application

Anti-Lamin A (C-terminal) antibody is suitable for use in western blot (0.1-0.2 μg/mL) using HeLa nuclear extract. This antibody can also be used in indirect immunofluorescence (1-2 μg/mL) using HeLa cells, rat NRK and mouse 3T3 cells. Additionally, anti-Lamin A (C-terminal) antibodies are suitable for use in immunoblotting (approx. 70 kDa). Cleaved fragments of lamin A may form additional bands at 45-50 kDa.
Anti-Lamin A (C-terminal) antibody produced in rabbit has been used in:
  • western blotting
  • immunofluorescence microscopy
  • immunohistochemistry

Actions biochimiques/physiologiques

Lamin A cut into a 47kDa fragment that facilitates chromatin condensation and nuclear degradation during cell death
Mutations in lamin A and C have been linked to a variety of rare human diseases including muscular dystrophy, lipodystrophy, cardiomyopathy, neuropathy, and progeroid syndromes (collectively termed laminopathies) and to premature aging (Hutchinson-Gilford progeria syndrome).

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Homozygous missense mutation in the lamin A/C gene causes autosomal recessive Hutchinson-Gilford progeria syndrome
Plasilova M, et al.
Journal of medical Genetics, 41, 609-614 (2004)
Nuclear Structure and Dynamics
Cell Biology (2017)
Lamins at a glance
Ho CY and Lammerding J
Journal of Cell Science, 125(9), 2087-2093 (2012)
U Aebi et al.
Nature, 323(6088), 560-564 (1986-10-09)
The nuclear lamina, a protein meshwork lining the nucleoplasmic surface of the inner nuclear membrane, is thought to provide a framework for organizing nuclear envelope structure and an anchoring site at the nuclear periphery for interphase chromatin. In several higher
Tao Hong et al.
American journal of physiology. Endocrinology and metabolism, 300(3), E500-E507 (2010-12-16)
It has previously been known that transcription of the PGC-1α gene can be either inhibited or stimulated by p38 MAP kinase (p38 MAPK). To determine whether p38 MAPK plays an inhibitory or stimulatory role in PGC-1α gene transcription, we further

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