MAB3540
Anti-Lamin A Antibody, CT, a.a. 598-611, clone 133A2
clone 133A2, Chemicon®, from mouse
Synonym(s):
70 kDa Lamin
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
culture supernatant
antibody product type
primary antibodies
clone
133A2, monoclonal
species reactivity
rat, mouse, canine, bovine, human
manufacturer/tradename
Chemicon®
technique(s)
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
western blot: suitable
isotype
IgG3
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... LMNA(4000)
General description
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.
Specificity
Monoclonal 133A2 reacts against human lamin A but not lamin C. The epitope lies with the 98 amino acids of the C terminus that is unique to lamin A. Specifically deletion analysis has shown that amino acids 598-611 were essential for reactivity {Hozak, P et.al. (1995), J. Cell Sci 635-644}.
Immunogen
Epitope: C-terminus, a.a. 598-611
Synthetic peptide from the C-terminus of human lamin A. This sequence is not present in the the lamin C isoform.
Application
Immunoblotting: Lamin A detected as a 70kDa protein under reduced conditions.
Immunocytochemistry on fixed cells (methanol/acetone fixation)
Immunohistochemistry on frozen tissue sections.
Optimal working dilutions must be determined by the end user.
Immunocytochemistry on fixed cells (methanol/acetone fixation)
Immunohistochemistry on frozen tissue sections.
Optimal working dilutions must be determined by the end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Cytoskeleton
Cytoskeleton
This Anti-Lamin A Antibody, C-terminus, a.a. 598-611, clone 133A2 is validated for use in FC, WB, IC, IH for the detection of Lamin A.
Physical form
Format: Purified
Liquid in buffer containing 0.1% sodium azide.
Storage and Stability
Maintain -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
CHEMICON 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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Description
Pricing
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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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Micah J Drummond et al.
Journal of applied physiology (Bethesda, Md. : 1985), 111(1), 135-142 (2011-04-30)
Amino acid transporters and mammalian target of rapamycin complex 1 (mTORC1) signaling are important contributors to muscle protein anabolism. Aging is associated with reduced mTORC1 signaling following resistance exercise, but the role of amino acid transporters is unknown. Young (n
Raju Padiya et al.
PloS one, 9(5), e94228-e94228 (2014-05-07)
Cardiovascular complication due to diabetes has remained a major cause of death. There is an urgent need to intervene the cardiac complications in diabetes by nutritional or pharmacological agents. Thus the present study was designed to find out the effectiveness
Petra Sehnalová et al.
Biology of the cell, 106(5), 151-165 (2014-03-13)
The optimal repair of DNA lesions is fundamental for physiological processes. We asked whether the recruitment of HP1β, 53BP1 and BMI1 proteins to ultraviolet (UVA)-induced DNA lesions requires functional A-type lamins. We found that UVA irradiation of nuclear lamina abolished
Jason P Chua et al.
Human molecular genetics, 23(5), 1376-1386 (2013-10-24)
Spinobulbar muscular atrophy (SBMA) is an inherited neuromuscular disorder caused by the expansion of a CAG repeat encoding a polyglutamine tract in exon 1 of the androgen receptor (AR) gene. SBMA demonstrates androgen-dependent toxicity due to unfolding and aggregation of
Hea-Jin Jung et al.
Molecular and cellular biology, 34(24), 4534-4544 (2014-10-15)
B-type lamins (lamins B1 and B2) have been considered to be essential for many crucial functions in the cell nucleus (e.g., DNA replication and mitotic spindle formation). However, this view has been challenged by the observation that an absence of
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