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- Table of Contents
13 Citations 6 Q&As
Facts about Laminin subunit alpha-2.
Human | |
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Gene Name: | LAMA2 |
Uniprot: | P24043 |
Entrez: | 3908 |
Belongs to: |
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No superfamily |
LAMA2; Laminin alpha 2; Laminin M chain; laminin subunit alpha-2; laminin, alpha 2; Laminin-12 subunit alpha; Laminin-2 subunit alpha; LAMM; LAMMLaminin-4 subunit alpha; Merosin heavy chain; Merosin
Mass (kDA):
343.905 kDA
Human | |
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Location: | 6q22.33 |
Sequence: | 6; NC_000006.12 (128883138..129516566) |
Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.
Secreted, extracellular space, extracellular matrix, basement membrane. Major component.
BosterBio articles will have you familiar with the LAMA2 Marker. This product allows scientists the ability to analyze the LAMA2 protein in various organisms and receive credits. This product is suitable for both researchers and industry professionals, and it is widely available. It has been used in numerous scientific studies to determine the effects of environmental pollutants upon human health.
LAMA2 (a membrane protein) is found in most of the body's tissues and cells. A monoclonal antibody is required to detect this particular protein. These antibodies can all be purchased at Boster. Each antibody is highly specific against laminin and has the ability to recognize various protein types. They are also highly efficient. These are the top uses for this marker. Let's look at them one by one.
The LAMA2 marker was created to determine if a specific protein is defective. The disease is associated with a variety of problems, including poor ECM structure and function, progressive breathing difficulties, and muscle fragility. The purpose of this study was to identify molecular pathways that lead to the observed pathology for LAMA2 MD. It was discovered that LAMA2 is a component in the laminin-alpha matrix.
The LAMA2 genes have a domain structure that is very similar to human and mouse A chain structures. The short arm domain has the highest homology to mouse and human laminin heavychains, and the long arm helical Domain I and II has the lowest. This gene is thought to be responsible for LAMA2-MD in humans. While there are still many questions, the LAMA2 marker can be a useful tool for researchers.
The therapeutic efficacy of LAMA2 MD is greatly contributed by restoring the interaction between laminins and cell surface receptors. This interaction mediates the signaling between adjacent cells, ECM, and improves membrane integrity. Some groups have been working to restore these interactions using linker proteins such as agrin. Agrin is the most studied linker protein for LAMA2 MD therapies. It is a miniatureized form of agrin.
In the same study, a homozygous private nonsense mutation was identified in the LAMA2 gene. The mutation causes a premature end codon and results a truncated protien. Two adult siblings carried the LAMA2 mutation. This gene is an important contributor to muscular dystrophy. In addition to this mutation, it causes several other conditions. Although the LAMA2 gene plays an essential role in maintaining laminin structure function, mutations in this genes can cause reduced gene expression.
Genomic DNA was isolated from blood. The sequencing of the amplified products revealed that there was a C–T mutation at exon 15. The reverse transcriptase (PCR) results showed that the patients had two normal bands and one in control. The LAMA2 marker
LAMA2-RD types are more susceptible than those with LAMA2-RD. Patients with limb girdle muscle dystrophy may experience walking delay, respiratory insufficiency, or weakness. Patients with this condition may have abnormal brain MRIs in addition to their clinical symptoms. Combining these approaches could improve the results. Further research is needed to find the best treatment for this condition. This condition can lead to severe disability. Therefore, the LAMA2 Marker may be ineffective.
PMID: 8294519 by Vuolteenaho R., et al. Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues.
PMID: 8910357 by Zhang X., et al. Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy.
*More publications can be found for each product on its corresponding product page