MAB1905
Anti-Laminin α1/β 1 Antibody, clone AL-4
clone AL-4, Chemicon®, from rat
Sign Into View Organizational & Contract Pricing
All Photos(1)
Laminin A Chain
Recommended Products
biological source
rat
antibody form
affinity purified immunoglobulin
antibody product type
primary antibodies
clone
AL-4, monoclonal
species reactivity
mouse
manufacturer/tradename
Chemicon®
technique(s)
ELISA: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG
NCBI accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
mouse ... Lama1(16772)
Specificity
As original characterized, clone AL-4 reacts with EHS mouse laminin, A chain (laminin α1). The epitope is mapped to the carboxy terminal globular domain on the A chain. Recent work by Scheele et al (2006) has further demonstrated that clone AL-4, under reducing conditions, recognized both the 200 kDa β1/γ1 band and the 400 kDa α1 band of mouse EHS laminin. However the affinity for the 400 kDa band was very low. AL-4 also demonstrated strong binding the Laminin β1. By ELISA the epitope for the AL-4 seemed to be located on the Laminin β1 chain, however the clone also recognizes the laminin α1 chain in immunoblots, thus AL-4 seems to show mixed cross reactivity to laminins α1 and β1, with the β1 reactivity being more prominent.
Immunogen
Laminin isolated from mouse EHS tumor.
Application
ELISA/RIA
Western blot
Immunoprecipitation
Immunohistochemistry. Reactive on tissue frozen in OCT at -70°C. Sections may be treated with hyaluronidase. Shows reactivity to paraffin embedded EHS tumor.
Optimal working dilutions must be determined by the end user.
Western blot
Immunoprecipitation
Immunohistochemistry. Reactive on tissue frozen in OCT at -70°C. Sections may be treated with hyaluronidase. Shows reactivity to paraffin embedded EHS tumor.
Optimal working dilutions must be determined by the end user.
Research Category
Cell Structure
Cell Structure
Research Sub Category
ECM Proteins
ECM Proteins
This Anti-Laminin α1/β 1 Antibody, clone AL-4 is validated for use in ELISA, IP, WB, IH(P) for the detection of Laminin α1/β 1.
Physical form
Format: Purified
Purified from ascites by Protein G affinity chromatography. Purified immunoglobulin in 0.02M PB, 0.25M NaCl, pH=7.6, 0.1% sodium azide
Storage and Stability
Maintain between 2 and 8°C.
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.
WGK
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Developmental biology, 239(1), 161-175 (2002-01-11)
For implantation and placentation to occur, mouse embryo trophoblast cells must penetrate the uterine stroma to make contact with maternal blood vessels. A major component of the uterine epithelial basement membrane and underlying stromal matrix with which they interact is
Molecular therapy. Methods & clinical development, 2, 15010-15010 (2015-06-02)
Preclinical gene therapy strategies using recombinant adeno-associated virus (AAV) vectors in animal models of Duchenne muscular dystrophy have shown dramatic phenotype improvements, but long-lasting efficacy remains questionable. It is believed that in dystrophic muscles, transgene persistence is hampered, notably by
Interaction between fibronectin and ?1 integrin is essential for tooth development.
Testing null
The extracellular matrix protein laminin ?2 regulates the maturation and function of the blood-brain barrier.
The Journal of Neuroscience null
Development (Cambridge, England), 136(20), 3495-3504 (2009-09-29)
Basement membranes have essential structural and signalling roles in tissue morphogenesis during embryonic development, but the mechanisms that control their formation are still poorly understood. Laminins are key components of basement membranes and are thought to be essential for initiation
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service