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MAB1922

Sigma-Aldrich

Anti-Laminin α2 Antibody, clone 5H2

ascites fluid, clone 5H2, Chemicon®

Synonym(s):

Laminin M chain, Merosin heavy chain, laminin M, laminin alpha 2 subunit, laminin, alpha 2

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About This Item

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

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

5H2, monoclonal

species reactivity

human, rabbit, monkey

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
cell culture | mammalian: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable

isotype

IgG1

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... LAMA2(3908)
rhesus monkey ... Lama2(715394)

General description

Elements of the extracellular matrix such as laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in organs including the kidney, lung, skin, and nervous system. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. For example, the alpha subfamily of laminin chains is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined. At least 15 distinct laminin trimers, containing various combinations of 5 alpha, 4 beta, and 3 gamma subunits have been found in mammals. Both laminin alpha 5 and alpha 1 are prevalent in kidney. Mice that are homozygous for a null mutation in the alpha 5 laminin gene are dead by embrionic day 14 - 19 with multiple developmental abnormalities. The kidney phenotypes include avascular glomeruli, impaired branching morphogenesis, and renal agenesis.

Specificity

Cross reacts with monkey and rabbit merosin.
Reacts with the 80 kDa fragment of the M-chain of human merosin.

Immunogen

Purified human merosin

Application

Detect Laminin α2 using this Anti-Laminin α2 Antibody, clone 5H2 validated for use in ELISA, CULT, IF, IH, IP & WB.
ELISA:
50% maximal binding to human merosin at 1:50,000 dilution from a previous lot.

Immunohistochemistry:
1:5,000 dilution from a previous lot was used for staining of 8 µm acetone-fixed cryostat muscle sections, prior to detection with a peroxidase-conjugated secondary antibody.

Immunofluorescence:
A previous lot of this antibody was used in immunofluorescent.

Affinity chromatography:
A previous lot of this antibody was used in IAP.

Immunoprecipitation:
A previous lot of this antibody was used in IP.

Optimal working dilutions must be determined by end user.
Research Category
Cell Structure
Research Sub Category
ECM Proteins

Quality

Routinely evaluated by Western Blot on Human Placenta lysate.

Western Blot Analysis:
1:1000 dilution of this lot detected Laminin α2 (merosin) on 10 μg of Human Placenta lysate.

Target description

80 kDa

Physical form

Unpurified
Unpurified ascites in buffer containing no preservatives.

Storage and Stability

Stable for 1 year at -20ºC from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage the IgG1 and affect product performance.

Analysis Note

Control
Vascular breast carcinomas, Cultured embryonic retinal neurons and RGCs

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

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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Burcu Balci-Hayta et al.
BMC neurology, 18(1), 207-207 (2018-12-17)
Alpha-dystroglycan (αDG) is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin globular domains and certain arenaviruses. An important enzyme, known as Like-acetylglucosaminyltransferase (LARGE), has been shown to transfer repeating units of -glucuronic
Kazuma Sugie et al.
International journal of molecular sciences, 19(11) (2018-11-11)
Danon disease, an X-linked dominant cardioskeletal myopathy, is caused by primary deficiency of lysosome-associated membrane protein-2 (LAMP-2). To clarify the clinicopathological features and management, we performed the first nationwide, questionnaire-based survey on Danon disease in Japan. A total of 39
Tobias Willer et al.
Nature genetics, 44(5), 575-580 (2012-04-24)
Walker-Warburg syndrome (WWS) is clinically defined as congenital muscular dystrophy that is accompanied by a variety of brain and eye malformations. It represents the most severe clinical phenotype in a spectrum of diseases associated with abnormal post-translational processing of a-dystroglycan
Holly Colognato et al.
Development (Cambridge, England), 134(9), 1723-1736 (2007-03-31)
Developmental abnormalities of myelination are observed in the brains of laminin-deficient humans and mice. The mechanisms by which these defects occur remain unknown. It has been proposed that, given their central role in mediating extracellular matrix (ECM) interactions, integrin receptors
Isabelle Nelson et al.
Journal of neuromuscular diseases, 2(3), 229-240 (2015-09-02)
Laminin α2 deficient congenital muscular dystrophy, caused by mutations in the LAMA2 gene, is characterized by early muscle weakness associated with abnormal white matter signal on cerebral MRI. To report on 4 patients with LAMA2 gene mutations whose original clinical

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