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
Sign Into View Organizational & Contract Pricing
All Photos(2)
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.
Not finding the right product?
Try our Product Selector Tool.
Storage Class
12 - Non Combustible Liquids
wgk_germany
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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
Ghaidaa Kashgari et al.
Developmental cell, 52(6), 764-778 (2020-02-29)
The fusion of digits or toes, syndactyly, can be part of complex syndromes, including van der Woude syndrome. A subset of van der Woude cases is caused by dominant-negative mutations in the epithelial transcription factor Grainyhead like-3 (GRHL3), and Grhl3-/-mice
H Kurata et al.
The Journal of allergy and clinical immunology, 103(5 Pt 2), S471-S484 (1999-05-18)
Adenoviruses have several specific features useful for gene therapy. They infect various lineages of cells irrespective of cell cycle status. However, the exact mechanism of their infection and in vivo kinetics as a gene expression vector have not been elucidated.
Raven Diacou et al.
Cell reports, 25(9), 2510-2523 (2018-11-30)
Gene regulation of multipotent neuroretinal progenitors is partially understood. Through characterizing Six3 and Six6 double knockout retinas (DKOs), we demonstrate Six3 and Six6 are jointly required for the maintenance of multipotent neuroretinal progenitors. Phenotypes in DKOs were not found in
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