Product: LAMB1 Antibody
Catalog: BF0229
Description: Mouse monoclonal antibody to LAMB1
Application: WB IHC ELISA
Reactivity: Human
Mol.Wt.: 198kDa; 198kD(Calculated).
Uniprot: P07942
RRID: AB_2833675

View similar products>>

   Size Price Inventory
 50ul $250 In stock
 100ul $350 In stock
 200ul $450 In stock

Lead Time: Same day delivery

For pricing and ordering contact:
Local distributors

Product Info

ELISA 1:10000, WB 1:500-1:2000, IHC 1:200-1:1000
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [AFB1651]
LAMB1 antibody detects endogenous levels of total LAMB1.
Cite Format: Affinity Biosciences Cat# BF0229, RRID:AB_2833675.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


CLM; Cutis laxa with marfanoid phenotype; LAM B1; LAMB 1; LAMB1; LAMB1_HUMAN; Laminin B1; Laminin B1 chain; Laminin beta 1 chain; Laminin beta 1 chain precursor; Laminin beta1; Laminin subunit beta 1; Laminin subunit beta-1; Laminin-1 subunit beta; Laminin-10 subunit beta; Laminin-12 subunit beta; Laminin-2 subunit beta; Laminin-6 subunit beta; Laminin-8 subunit beta; LIS5; MGC142015;



Purified recombinant fragment of human LAMB1 expressed in E. Coli.

Laminins, 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 beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.

PTMs - P07942 As Substrate

Site PTM Type Enzyme
S154 Phosphorylation
K184 Ubiquitination
S195 Phosphorylation
K215 Sumoylation
K215 Ubiquitination
Y220 Phosphorylation
S221 Phosphorylation
K229 Ubiquitination
T231 Phosphorylation
K239 Ubiquitination
T242 Phosphorylation
T369 Phosphorylation
T939 Phosphorylation
Y950 Phosphorylation
S953 Phosphorylation
S1222 Phosphorylation
K1231 Ubiquitination
K1244 Ubiquitination
K1255 Ubiquitination
N1279 N-Glycosylation
S1280 Phosphorylation
T1281 Phosphorylation
T1290 Phosphorylation
K1310 Ubiquitination
R1315 Methylation
S1365 Phosphorylation
T1435 O-Glycosylation
K1476 Ubiquitination
S1478 Phosphorylation
S1496 Phosphorylation
S1520 Phosphorylation
K1611 Ubiquitination
S1666 Phosphorylation
Y1671 Phosphorylation
S1682 Phosphorylation
S1735 Phosphorylation
K1741 Ubiquitination
K1757 Ubiquitination
K1773 Ubiquitination

Research Backgrounds


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. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.

Subcellular Location:

Secreted>Extracellular space>Extracellular matrix>Basement membrane.
Note: Major component.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

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. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).


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.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Environmental Information Processing > Signal transduction > PI3K-Akt signaling pathway.   (View pathway)

· Environmental Information Processing > Signaling molecules and interaction > ECM-receptor interaction.   (View pathway)

· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.

· Human Diseases > Infectious diseases: Parasitic > Amoebiasis.

· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.

· Human Diseases > Cancers: Overview > Pathways in cancer.   (View pathway)

· Human Diseases > Cancers: Specific types > Small cell lung cancer.   (View pathway)

Restrictive clause


Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.