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Key Documents

05-714

Sigma-Aldrich

Anti-Lamin A/C Antibody, clone 14

clone 14, Upstate®, from mouse

Synonym(s):

Anti-CDCD1, Anti-CDDC, Anti-CMD1A, Anti-CMT2B1, Anti-EMD2, Anti-FPL, Anti-FPLD, Anti-FPLD2, Anti-HGPS, Anti-IDC, Anti-LDP1, Anti-LFP, Anti-LGMD1B, Anti-LMN1, Anti-LMNC, Anti-LMNL1, Anti-MADA, Anti-PRO1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

14, monoclonal

species reactivity

canine, chicken, human, rat, mouse

manufacturer/tradename

Upstate®

technique(s)

immunocytochemistry: suitable
western blot: suitable

isotype

IgG

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... LMNA(4000)

General description

Nuclear lamins are composed of the type V intermediate filament proteins. Often referred to as nucleoskeletal proteins they play a key role in nuclear integrity, positioning of nuclear pores, and overall nuclear size and shape. They also play several key functional roles in the maintenance and propagation of the genome--replication, transcription-- as well as the disassembly and reassembly of the nucleus during cell division. In vitro studies have shown that dimers are the basic building blocks of higher order lamin structures and in low concentrations lamins are distributed throughout the nucleoplasm. In humans, there are two types of lamins: A-type lamins (lamins A and C), found primarily in differentiated cells, and B-type lamins (lamins B1 and B2), found in all nucleated cells. Nuclear lamins are involved in a number of essential nuclear functions, including nuclear envelope assembly and disassembly during cell division, DNA synthesis, transcription, and apoptosis. Nuclear lamins have been found to co-localize with DNA synthesis sites.

Specificity

Recognizes Lamin A, MW ~74 kDa and Lamin C, MW ~65 kDa.

Immunogen

Peptide from human lamin A/C corresponding to amino acids 398 to 490.

Application

Anti-Lamin A/C Antibody, clone 14 detects level of Lamin A/C & has been published & validated for use in IC & WB.
Immunocytochemistry:
This antibody has been reported by an independent laboratory to detect Lamin A/C in human endothelial cells.
Research Category
Cell Structure
Research Sub Category
Cytoskeletal Signaling

Quality

Evaluated by western blot on RIPA lysates from A431 cells.

Western Blot Analysis:
0.5-2 μg/mL of this antibody detected Lamin A/C in 20 μg of RIPA lysates from A431 cells.

Target description

~74/65 kDa

Linkage

Replaces: MABE481

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1 in buffer containing 50% storage buffer (20 mM sodium phosphate, pH 7.5, 0.15 M NaCl, 1 mg/mL BSA, 0.09% sodium azide) and 50% glycerol. Store at -20°C.

Storage and Stability

Stable for 1 year at -20ºC from date of receipt.

Analysis Note

Control
Positive Antigen Control: Catalog #12-301, non-stimulated A431 cell lysate. Add 2.5µL of 2-mercaptoethanol/100µL of lysate and boil for 5 minutes to reduce the preparation. Load 20µg of reduced lysate per lane for minigels.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Jose D Debes et al.
Cancer research, 65(3), 708-712 (2005-02-12)
Alterations in nuclear structure distinguish cancer cells from noncancer cells. These nuclear alterations can be translated into quantifiable features by digital image analysis in a process known as quantitative nuclear morphometry. Recently, quantitative nuclear morphometry has been shown to predict
Sribalasubashini Muralimanoharan et al.
Endocrinology, 159(5), 2022-2033 (2018-03-17)
Dysregulation of human trophoblast invasion and differentiation with placental hypoxia can result in preeclampsia, a hypertensive disorder of pregnancy. Herein, we characterized the role and regulation of miR-1246, which is markedly induced during human syncytiotrophoblast differentiation. miR-1246 targets GSK3β and
Ubiquitin-dependent recruitment of the Bloom syndrome helicase upon replication stress is required to suppress homologous recombination.
Tikoo, S; Madhavan, V; Hussain, M; Miller, ES; Arora, P; Zlatanou, A; Modi, P; Townsend et al.
The Embo Journal null
Angelika Oehmig et al.
BMC genomics, 9, 441-441 (2008-09-26)
The identification of novel drug targets by assessing gene functions is most conveniently achieved by high-throughput loss-of-function RNA interference screening. There is a growing need to employ primary cells in such screenings, since they reflect the physiological situation more closely
Laura D Brown et al.
Endocrinology, 157(6), 2447-2460 (2016-04-07)
Insulin is an important fetal growth factor. However, chronic experimental hyperinsulinemia in the fetus fails to accelerate linear and lean mass growth beyond normal rates. Mechanisms preventing accelerated lean mass accretion during hyperinsulinemia are unknown. To address potential mechanisms, late-gestation

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