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- Table of Contents
Facts about Basal cell adhesion molecule.
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Human | |
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Gene Name: | BCAM |
Uniprot: | P50895 |
Entrez: | 4059 |
Belongs to: |
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No superfamily |
antigen identified by monoclonal F8; Auberger B antigen; basal cell adhesion molecule (Lu and Au blood groups); basal cell adhesion molecule (Lutheran blood group); basal cell adhesion molecule; B-CAM cell surface glycoprotein; BCAM; B-cell adhesion molecule; CD239 antigen; CD239; F8/G253 antigen; glycoprotein 95kDa; LUAU; Lutheran antigen; Lutheran blood group (Auberger b antigen included); Lutheran blood group glycoprotein; MSK19
Mass (kDA):
67.405 kDA
Human | |
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Location: | 19q13.32 |
Sequence: | 19; NC_000019.10 (44809059..44821421) |
Wide tissue distribution (highest in the pancreas and very low in brain). Closely associated with the basal layer of cells in epithelia and the endothelium of blood vessel walls.
Membrane; Single-pass type I membrane protein.
The BCAM Marker is a useful marker in clinical research. Scientists around the world can use it to study the genome of different species and applications. It can also be used for analyses of gene ontology that reveal molecular functions and proteins which have been elevated in HGSC plasma. To find out more about this marker, read the following article. Here are some of the best uses. Boster Bio is a great source for scientists!
Boster Bio BCAM protein quantification by sandwich ELISA Kits utilize standard sandwich ELISA technology for detection of mouse BCAM. Each well is precoated with a monoclonal anti-BCAM antibody. The wells are then filled with standard or biotinylated detect polyclonal antibody goat. The conjugates that are not bound are washed away by TBS or PBS buffer. After this, the 96-well plate is incubated with an acidic stop solution and the resultant sample is examined.
Boster Bio's BCAM protein quantification with strip plate ELISA kits employs the microwell and strip-plate designs, as well as HRP detection using colorimetric methods for precise and accurate results. This ELISA kit can detect native BCAM in biological samples. The appropriate samples include undiluted body fluids tissues homogenates, fluids, secretions, and other biological samples. The kit also includes quality control assays that measure reproducibility.
The ELISA protocol was validated using the Boster Bio Human VEGF PicoKine ELISA Kit. The protein was expressed using pET15b vector in HESCand IPTG-inducible cell lines. It was expressed as a 16-kDa band on the gel electrophoresis chromatogram. The gel-eluted protein was then dialyzed using dialysis buffer that contained 8 M to 0M Urea.
The BCAM gene is a protein-coding gene that has numerous clinical applications. It is associated with diseases such as Sickle Cell Disease and Lutheran Null among other conditions. Gene Ontology (GO) annotations include transmembrane-sensing receptor activity and laminin binding. Interestingly, a paralog of the BCAM gene, dubbed MCAM is also a crucial paralog.
Lu/BCAM overexpression caused colony formation, cell adhesion, and cell adhesion. The gene was overexpressed to increase the number of colonies and to decrease migration. It also increased Erk phosphorylation and RhoA activity. The gene is regulated by the H-ras V12 protein. It could be utilized as a target for anti-adhesion strategies to fight cancer. It needs more research.
Presently, BCAM is a universal prognostic test, meaning that it can be used for all subtypes of breast cancer. The BCAM marker is a blend of several molecular characteristics. It includes the breast cancer-specific FGD3 SUSD3 metagene, in addition to four metagenes that attract attention that are common to multiple types of cancer. It also includes the tumor size and number of positive lymph nodes.
In the present study Lu/BCAM expression was positively correlated with the risk of developing human bladder cancer. These results suggest that Lu/BCAM is an effective therapeutic target. Lu/BCAM is positively linked in the development of tumors in mice and makes it a potential therapeutic target to treat bladder cancer. If this gene is confirmed and confirmed, it could be a valuable tool for cancer research. Lu/BCAM therefore is an attractive biomarker for cancer research.
Many types of cancer, including those of the ovarian or bladder, possess the BCAM gene. Researchers investigated BCAM by generating monoclonal antigens to it. The antibodies were found to increase the expression of the BCAM antigen in vivo, and upregulated in certain types of cells following malignant transformation. This study could provide clues for prognostication and diagnostics. It could also shed light on the mechanism behind BCAM gene expression.
BCAM is more than an indicator of prognosis, but it also helps in assessing the risk of developing bronchopulmonary disease (BPD) early. However, research is still in the beginning stages in this area. Currently, there are several biomarkers that are available to diagnose cancer. A few of these include the BCAM gene and the DEK gene. This study is focused on the BCAM gene, SIGLEC-14 and the ANGPTL-3.
To understand the molecular function of the proteins that are upregulated in HGSC plasma, we performed an analysis of gene ontology. These analyses revealed that plasma proteins have many membrane receptor-driven pathways that communicate with the extracellular matrix as well as growth factors. Analyses of plasma proteins also revealed that some are associated with platelet-derived growth factor and tumour necrosis factors. We also identified extracellular proteases which are inhibitors of growth factors.
We identified a number of genes that were highly enriched in both RR or OS RNA-Seq results that were derived from 31 LAC and normal tissue. We identified the most commonly used DEGs, validated them using Venn diagram software, and carried out analysis of gene ontology. Gene ontology and KEGG pathways were analyzed using the WEB-based GEne SET AnaLysis Toolkit (GeSA). To visualize the protein-protein interaction network, we also determined the mapping of DEGs to proteins. We also identified the genes that are central using Molecular Complex Detection and Gene Expression Profiling Interactive Analysis.
Comparing the three proteomic assays showed that the SOMAscan protein was differentially regulated in OC and N-plasma. The two platforms also had an unidirectional correlation. The resulting p-values have been adjusted by Benjamini-Hochberg correction. Figure 2 summarizes the resulting list of proteins increased in N-plasma (OC-plasma)
The proteins that were enriched were classified into OS and RR by their OS enrichment scores. The proteins that were enriched were analyzed using a functional gene ontology database. Venn diagrams were used to define the proteins identified to have a high concentration of both OS and RR. These were the categories used for eighty percent of the proteins found to be enriched in OS/RR.
The secretome of OC-plasma proteins points to tumor cells’ immune responses and metastasis-promoting factors. These proteins include vesicle-encapsulated and bone-fide secreted polypeptides. This study provides new insights into the HGSC microenvironment and provides innovative tools to stratify. These analyses will be useful for future studies utilizing affinity proteomics.
This study assessed the expression levels of a small subset of tumor-related genes for adenocarcinoma. We identified genes that had differing expression profiles and demonstrated prognostic value. The genes that were highly expressed were identified based on their relevance to human retinal diseases. We also analyzed the possibility for these genes to be connected to other cancers.
PMID: 7777537 by Parsons S.F., et al. The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver.
PMID: 7954395 by Campbell I.G., et al. Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily.