Laminin Markers
The Laminin Markers are PrecisA Monoclonals™, mouse monoclonal antibodies targeting different laminin subunits. The PrecisA Monoclonals laminin antibodies are the perfect tools to identify specific laminin subunits present in a tissue of interest to further understand the roles and expression patterns of different laminins.
Laminin proteins are the major components of the basement membrane. They are crucial for a wide variety of biological processes, such as cell adhesion, migration, embryonic development, differentiation, and phenotypic stability. Laminins are a family of conserved multidomain, trimeric proteins that are part of the extracellular matrix structure. They are composed of three different subunits; an α-chain, a β-chain, and a γ-chain, that can be found in five (α1-5), three (β1-3), and three (γ1-3) genetic variants respectively.
About BioLamina
BioLamina develops, manufactures and distributes full length, human, recombinant laminins intended for biologically relevant cell culture.
For more information about human recombinant laminin proteins, please visit BioLamina's science room.
The Laminin Marker Panel
The Laminin Markers were developed in collaboration with the Swedish biotech company BioLamina AB. With the use of BioLamina’s human recombinant laminin isoforms, PrecisA Monoclonals selectively recognize the specific subunits of the laminins.
In order to select for specificity and rule out any cross-reactivity, the validation was carried out in different applications such as ELISA, Western blot, and immunohistochemistry.
By choosing the proper PrEST Antigens our laminin antibodies are specific for each subunit without any cross-reactivity. The PrecisA Monoclonal antibodies are developed using stringent conditions. We guarantee secured continuity and stable supply.
Explore Laminin Markers
The complete laminin marker antibody panel is presented in our product catalog.
Combine different laminin antibodies
Combine the different laminin antibodies to target specific laminins. For example, laminin-421 consists of alpha 4, beta 2, and gamma 1 and will be detected by the Anti-LAMA4, Anti-LAMB2, and Anti-LAMC1 antibodies from the marker panel.
LAMC1: an example of the development of specific laminin antibodies.
The laminin antibodies are carefully selected to recognize only one specific laminin subunit. The antibody selection process starts already during the antigen selection phase and continued throughout the development and QC processes.
ELISA based functional characterization screen
Here we show how a monoclonal antibody targeting laminin gamma 1 (Anti-LAMC1) has been developed and selected through our process and can be used to detect Laminin gamma 1 expression in tissue.
All our laminin antibodies have gone through an ELISA-based functional characterization screening to confirm that they are specific for the corresponding laminin subunit without cross-reactivity with other subunits. This has been done using ELISA plates coated with different human recombinant laminin isoforms.
Subunit specificity confirmed by Western Blot
For further characterization, we have confirmed subunit specificity in WB using the same human recombinant laminins as for ELISA. The data below shows that the antibody only detects its specific subunit and does not display any cross-reactivity.
Immunohistochemistry to confirm protein expression in relevant tissues
Finally, the antibodies were tested by IHC (see below) to confirm protein expression in relevant tissues and the absence of non-specific staining.
Taken together data confirms that the Anti-LAMC1 antibody is highly specific and selective for its target subunit in various applications.
Laminin-521: an example of how laminin antibodies can be used for the detection and recognition of specific laminin subunits.
Laminin-521 is a protein naturally expressed by human pluripotent stem cells and is a critical factor in the pluripotent stem cell niche (Rodin et al, 2014; Laperle, 2015). Laminin-521 is also crucially important for the development and function of several tissues, including heart muscle (Roediger, 2010) and retinal epithelium (Aisenbrey et al., 2006). In the adult kidney, laminin-521 is a key component of the glomerular basement membrane (Miner 2012).
The data below demonstrates how our PrecisA Monoclonal antibodies against the laminin alpha 5, the beta 2, and the gamma 1 subunits can be used to detect the presence of laminin-521 in the kidney. The monoclonal antibodies used for this staining belong to different IgG isotypes, including IgG1, IgG2a, and IgG2b, which makes it possible to use them for multiplex IHC on the same tissue section.
Discover PrecisA Monoclonals targeting Laminin subunits
PrecisA Monoclonals Laminin Marker Panel
Anti-LAMA1 (AMAb91091, AMAb91117)
Anti-LAMA2 (AMAb91166)
Anti-LAMA3 (AMAb91123)
Anti-LAMA4 (AMAb91133, AMAb91134)
Anti-LAMA5 (AMAb91124)
Anti-LAMB1 (AMAb91092)
Anti-LAMB2 (AMAb91096, AMAb91097)
Anti-LAMB3 (AMAb91160, AMAb91161)
Anti-LAMC1 (AMAb91136, AMAb91137, AMAb91138, AMAb91140)
Anti-LAMC2 (AMAb91098)
References
Aisenbrey S, et al. Retinal pigment epithelial cells synthesize laminins, including laminin 5, and adhere to them through alpha3- and alpha6-containing integrins. Invest Ophthalmol Vis Sci. 2006 Dec;47(12):5537-44.
Ascierto ML, et al. Transcriptional mechanisms of resistance to anti-PD-1 therapy. Clin Cancer Res , 2017 Feb 13; 23(12):3168-3180.
Laperle A, et al. α-5 Laminin Synthesized by Human Pluripotent Stem Cells Promotes Self-Renewal. Stem Cell Reports. 2015 Aug 11;5(2):195-206.
Long NP, et al. An integrative data mining and omics-based translational model for the identification and validation of oncogenic biomarkers of pancreatic cancer. Cancers (Basel), 2019 Jan 29; 11(2):155.
Miner JH. et al. The glomerular basement membrane. Exp Cell Res. 2012 May 15;318(9):973-8.
Rodin S et al. Long-term self-renewal of human pluripotent stem cells on human recombinant laminin-511. Nat Biotechnol. 2010 Jun;28(6):611-5.
Rodin S et al. Clonal culturing of human embryonic stem cells on laminin-521/E-cadherin matrix in defined and xeno-free environment. Nat Commun. 2014;5:3195.
Roediger M et al. Tissue distribution of the laminin beta1 and beta2 chain during embryonic and fetal human development. J Mol Histol. 2010 Apr;41(2-3):177-84.
Tahoun M, et al. Mutations in LAMB2 are associated with albuminuria and optic nerve hypoplasia with hypopituitarism. J Clin Endocrinol Metab, 2019 Nov 26; 105(3):595-599
Troughton LD, et al. Laminin N-terminus α31 protein distribution in adult human tissues. PLoS One, 2020 Dec 2; 15(12):e0239889.