The LAMC3 Polyclonal Antibody (PAC013504) is a valuable tool for researchers studying LAMC3, a key component of laminin-332, an extracellular matrix protein involved in cell adhesion and migration. This antibody, generated in rabbits, is highly specific for human samples and has been validated for use in Western blot applications. By targeting the LAMC3 protein, this antibody allows for the detection and analysis of LAMC3 in various cell types, making it ideal for studies in cell biology, cancer research, and tissue development.LAMC3 is known for its crucial role in maintaining the structural integrity of tissues and organs, and its dysregulation has been implicated in diseases such as cancer and genetic disorders affecting skin and mucous membranes.
Research on LAMC3 is essential for understanding its function in normal physiological processes and its potential as a therapeutic target for diseases characterized by aberrant cell adhesion and migration. The LAMC3 Polyclonal Antibody is a valuable tool for investigating the role of LAMC3 in health and disease, paving the way for new insights and potential treatment strategies.
LAMC3: 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. Defects in LAMC3 are the cause of cortical malformations occipital (OCCM). OCCM is a disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes.Protein type: Extracellular matrix; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptideChromosomal Location of Human Ortholog: 9q34.12Cellular Component: basement membrane; extracellular region; membrane; proteinaceous extracellular matrixMolecular Function: structural molecule activityBiological Process: astrocyte development; cell adhesion; cellular morphogenesis during differentiation; extracellular matrix organization and biogenesis; retina development in camera-type eye; visual perceptionDisease: Cortical Malformations, Occipital
UniProt Protein Details:
NCBI Summary:
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 gamma chain isoform laminin, gamma 3. The gamma 3 chain is most similar to the gamma 1 chain, and contains all the 6 domains expected of the gamma chain. It is a component of laminin 12. The gamma 3 chain is broadly expressed in skin, heart, lung, and the reproductive tracts. In skin, it is seen within the basement membrane of the dermal-epidermal junction at points of nerve penetration. Gamma 3 is also a prominent element of the apical surface of ciliated epithelial cells of lung, oviduct, epididymis, ductus deferens, and seminiferous tubules. The distribution of gamma 3-containing laminins along ciliated epithelial surfaces suggests that the apical laminins are important in the morphogenesis and structural stability of the ciliated processes of these cells. [provided by RefSeq, Aug 2011]