MAB1904
Anti-Laminin-1 A&B chains Antibody, cross region, clone AL-2
clone AL-2, Chemicon®, from rat
Synonym(s):
laminin alpha1, laminin beta1
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
rat
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
AL-2, monoclonal
species reactivity
mouse
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1κ
NCBI accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
mouse ... Lama1(16772)
General description
Laminins are secreted glycoproteins incorporated into cell-associated extracellular matrices and an integral part of the structural scaffolding in most animal tissues. The laminin protein is made up of three polypeptide chains; α, β and γ, accounting for its flexibility in connecting various molecules. When originally characterized, laminin-1 clone AL-2 reacted with Engelbreth-Holm-Swarm (EHS) mouse laminin A & B chains on the long arm near the cross region, (Skubitz, 1987). More recently, investigations, (Schèele, 2006) have shown that the clone binds laminin β1 under reducing conditions as well as native ELISAs and that the affinity is increased by the presence of the laminin α1 chain. Thus there is significant laminin β1 reactivity with clone AL-2.
Specificity
Other species have not been tested.
Reacts with EHS mouse laminin A & B chains on the long arm near the cross region.
Immunogen
Epitope: Near cross region
Laminin isolated from EHS mouse sarcoma.
Application
Detect Laminin-1 A&B chains using this Anti-Laminin-1 A&B chains Antibody, cross region, clone AL-2 validated for use in ELISA, IF, IH(P), IP & WB.
Immunofluorescence:
An independent laboratory (Schèele, S., 2006) has verified anti-laminin clone AL-2 to work using immunofluorescence techniques on mouse muscle tissue, including both transgenic and wild-type tissues.
An independent laboratory (Schèele, S., 2006) has verified anti-laminin clone AL-2 to work using immunofluorescence techniques on mouse muscle tissue, including both transgenic and wild-type tissues.
Research Category
Cell Structure
Cell Structure
Research Sub Category
ECM Proteins
ECM Proteins
Quality
Evaluated on a representative lot by Western blot on purified mouse laminin-1.
Target description
~200 kDa
Physical form
Format: Purified
Protein G Purified
Purified in 0.1M Tris-Glycine (pH 7.4) 150mM NaCl with 0.05% NaN3.
Storage and Stability
Maintain at 2-8°C in undiluted aliquots for up to 1 year after date of receipt.
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
12 - Non 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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Laminin isoforms 8 and 10 are primary components of the subendothelial basement membrane promoting interaction with neoplastic lymphocytes.
P Spessotto, Z Yin, G Magro, R Deutzmann, A Chiu, A Colombatti, R Perris
Cancer Research null
Clinical and histopathological analysis of healing process of intraoral reconstruction with ex vivo produced oral mucosa equivalent.
Takeshi Hotta,Satoshi Yokoo,Hiroto Terashi,Takahide Komori
Kobe J. Med. Sci. null
George S Karagiannis et al.
Molecular oncology, 8(2), 178-195 (2013-11-26)
It has been suggested that cancer-associated fibroblasts (CAFs) positioned at the desmoplastic areas of various types of cancer are capable of executing a migratory program, characterized by accelerated motility and collective configuration. Since CAFs are reprogrammed derivatives of normal progenitors
Localization of three distinct heparin-binding domains of laminin by monoclonal antibodies.
Skubitz, A P, et al.
The Journal of Biological Chemistry, 263, 4861-4868 (1988)
Susanne Schéele et al.
Matrix biology : journal of the International Society for Matrix Biology, 25(5), 301-305 (2006-04-25)
We analyzed the reactivity of three different commercially available rat monoclonal antibodies raised against mouse laminin-alpha1beta1gamma1 (laminin-111), AL-1, AL-2, and AL-4. Using ELISA assays, Western blot analysis and immunostainings we present refined epitope maps for these three laminin monoclonals. AL-1
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