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MAB1920 Anti-Laminin γ1 Antibody, clone 2E8

100 µL  
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Key Spec Table

Species ReactivityKey ApplicationsHostFormatAntibody Type
H, RELISA, CULT, IHC, IP, WBMAscitesMonoclonal Antibody
Catalogue NumberMAB1920
Brand Family Chemicon®
Trade Name
  • Chemicon
DescriptionAnti-Laminin γ1 Antibody, clone 2E8
Alternate Names
  • Laminin B2 Chain
Product Information
HS Code3002 15 90
  • Basement membrane, Hippocampal tissue
PresentationLiquid, no preservatives added.
Quality LevelMQ100
ApplicationThis Anti-Laminin γ1 Antibody, clone 2E8 is validated for use in ELISA, CULT, IH, IP, WB for the detection of Laminin γ1.
Key Applications
  • Cell Culture
  • Immunohistochemistry
  • Immunoprecipitation
  • Western Blotting
Application NotesELISA (50% maximal binding to human laminin): (1:300,000.


Affinity chromatography



Optimal working dilutions must be determined by end user.
Biological Information
ImmunogenPurified human laminin
ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
SpecificityReacts with the B2 chain of intact human laminin and does not block the neurite stimulating activity of laminin. Cross reacts with the 200 kDa chain of rat laminin.
Species Reactivity
  • Human
  • Rat
Antibody TypeMonoclonal Antibody
Entrez Gene Number
Entrez Gene SummaryLaminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis.
Gene Symbol
  • LAMC1
  • LAMB2
  • MGC87297
Purification MethodUnpurified
UniProt Number
UniProt SummaryFUNCTION: SwissProt: P11047 # Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
SIZE: 1609 amino acids; 177607 Da
SUBUNIT: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Gamma-1 is a subunit of laminin-1 (EHS laminin), laminin-2 (merosin), laminin-3 (S-laminin), laminin-4 (S-merosin), laminin-6 (K-laminin) and laminin-7 (KS-laminin).
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Found in the basement membranes (major component).
DOMAIN: SwissProt: P11047 The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure. & Domains VI and IV are globular.
SIMILARITY: Contains 11 laminin EGF-like domains. & Contains 1 laminin IV type A domain. & Contains 1 laminin N-terminal domain.
Molecular Weight200 kDa
Physicochemical Information
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
  • 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.
Storage and Shipping Information
Storage ConditionsMaintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Packaging Information
Material Size100 µL
Transport Information
Supplemental Information
Global Trade Item Number
Catalogue Number GTIN
MAB1920 04053252464317


Anti-Laminin γ1 Antibody, clone 2E8 SDS


Safety Data Sheet (SDS) 

Anti-Laminin γ1 Antibody, clone 2E8 Certificates of Analysis

TitleLot Number
MOUSE ANTI-HUMAN LAMININ - 3202257 3202257
MOUSE ANTI-HUMAN LAMININ - 3498508 3498508
MOUSE ANTI-HUMAN LAMININ - 3596786 3596786
MOUSE ANTI-HUMAN LAMININ - 3731657 3731657
MOUSE ANTI-HUMAN LAMININ - 3927586 3927586
MOUSE ANTI-HUMAN LAMININ - 3994098 3994098
MOUSE ANTI-HUMAN LAMININ - 4123411 4123411


Reference overviewPub Med ID
Treadmill exercise induced functional recovery after peripheral nerve repair is associated with increased levels of neurotrophic factors.
Park, JS; Höke, A
PloS one  9  e90245  2014

Show Abstract
24618564 24618564
Mammalian target of rapamycin complex 1 is involved in differentiation of regenerating myofibers in vivo.
Elen H Miyabara,Talita C Conte,Meiricris T Silva,Igor L Baptista,Carlos Bueno,Jarlei Fiamoncini,Rafael H Lambertucci,Carmen S Serra,Patricia C Brum,Tania Pithon-Curi,Rui Curi,Marcelo S Aoki,Antonio C Oliveira,Anselmo S Moriscot
Muscle & nerve  42  2010

Show Abstract
20976781 20976781
Schwartz, E; Wicinski, B; Schmeidler, J; Haroutunian, V; Hof, PR
Translational neuroscience  1  292-299  2010

Show Abstract
21331351 21331351
Mapping gene expression changes in the fetal rat testis following acute dibutyl phthalate exposure defines a complex temporal cascade of responding cell types.
Johnson, KJ; Hensley, JB; Kelso, MD; Wallace, DG; Gaido, KW
Biology of reproduction  77  978-89  2007

Show Abstract
17881770 17881770
Novel extracellular matrix structures in the neural stem cell niche capture the neurogenic factor fibroblast growth factor 2 from the extracellular milieu.
Aurelien Kerever,Jason Schnack,Dirk Vellinga,Naoki Ichikawa,Chris Moon,Eri Arikawa-Hirasawa,Jimmy T Efird,Frederic Mercier
Stem cells (Dayton, Ohio)  25  2007

Show Abstract
17569787 17569787
Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ).
Fukushima, K; Nakamura, A; Ueda, H; Yuasa, K; Yoshida, K; Takeda, S; Ikeda, S
BMC musculoskeletal disorders  8  54  2007

Show Abstract
17598883 17598883
Laminin-311 (Laminin-6) fiber assembly by type I-like alveolar cells.
DeBiase, PJ; Lane, K; Budinger, S; Ridge, K; Wilson, M; Jones, JC
The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society  54  665-72  2006

Show Abstract
16714422 16714422
Laminin-6 assembles into multimolecular fibrillar complexes with perlecan and participates in mechanical-signal transduction via a dystroglycan-dependent, integrin-independent mechanism.
Jones, Jonathan C R, et al.
J. Cell. Sci., 118: 2557-66 (2005)  2005

Show Abstract
15928048 15928048
Cortical GABA interneurons in neurovascular coupling: relays for subcortical vasoactive pathways.
Cauli, Bruno, et al.
J. Neurosci., 24: 8940-9 (2004)  2004

Show Abstract
15483113 15483113
Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10.
Hiroyuki Ido, Kenji Harada, Sugiko Futaki, Yoshitaka Hayashi, Ryoko Nishiuchi, Yuko Natsuka, Shaoliang Li, Yoshinao Wada, Ariana C Combs, James M Ervasti, Kiyotoshi Sekiguchi
The Journal of biological chemistry  279  10946-54  2004

Show Abstract
14701821 14701821

Data Sheet


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Product Families


Life Science Research > Antibodies and Assays > Primary Antibodies