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- Table of Contents
Facts about Disintegrin and metalloproteinase domain-containing protein 8.
Human | |
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Gene Name: | ADAM8 |
Uniprot: | P78325 |
Entrez: | 101 |
Belongs to: |
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No superfamily |
a disintegrin and metalloproteinase domain 8; ADAM 8; ADAM metallopeptidase domain 8; ADAM8; CD156a antigen; CD156a; CD156human leukocyte differentiation antigen; Cell surface antigen MS2; EC 3.4.24; EC 3.4.24.-; MGC134985; MS2; MS2disintegrin and metalloproteinase domain-containing protein 8
Mass (kDA):
88.771 kDA
Human | |
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Location: | 10q26.3 |
Sequence: | 10; NC_000010.11 (133262422..133276891, complement) |
Membrane; Single-pass type I membrane protein.
You'll need to know how to use the Anti-ADAM8 marker, whether you're a scientist, a biomedical engineer or researcher. Detecting antibodies with Western blot is the most common method for determining ADAM8 levels in samples. Autoradiography films are also a viable option. Here are three possible ways to use this mark. Continue reading to learn how you can use this marker.
The ADAM8 protein contains various domains, processed forms, and transmembrane segments. The ADAM8 proteins were expressed in whole cells from TNBC-derived human non-tumoral MCF-10A or TNBC cell line lines. Western blotting was used for the determination of ADAM8 protein levels. B-actin was used to load the control. Figure 1 shows an example blot (n=3); all lanes were taken with the same gel. The vertical line is re-alignment. MDA-231 is the marker for ADAM8, while MDA-468 is the marker for MW.
Boster Bio's Anti-ADAM8 Antibody reacts with human DNA. It has been subject to extensive testing in ELISA, WB. It can be stored at room temperature for up to one-year and is available in liquid in PBS with 50% glucose and 0.02% sodium azide. The Antibody has been tested in ELISA and WB and is suitable for use in immunological research.
In a mouse study, the ADAM8-specific antibody was shown to be a TNBC therapeutic targets. Mab1031, an Adam8-specific antibody that was administered intraperitoneally to mice, was given twice per week for a period of five weeks. The control group received IgG2B isotype-matched IgG2B. The tumor burden and tumor weight were significantly reduced by the ADAM8 antibody treatment. Additionally, brain metastasis rates were lower.
The ADAM8 Protein is essential for the growth breast cancer cells in an orthotopic-xenograft model. ADAM8 expression is consistently detected in at least half of breast cancer patients' distant metastases. It may be used to detect the disease early enough to treat it. It has an unmatched therapeutic potential. ADAM8 was tested in mice models. It is a sensitive biomarker that can be used to help patients with breast cancer.
ADAM8 plays a significant role in regulating vascular formation. The primary goal of cancer treatment is to reduce angiogenesis in humans. Vascular growth can also be inhibited by blocking ADAM8 within cancer cells. The anti-ADAM8 marker blocks VEGF A-mediated Angiogenesis and decreases expression 5 angiogenesis mediators. ADAM8 is a key regulator of cancer growth.
Hypoxia, which is an environmental factor that causes cancer cell growth in low-oxygen environments, can cause ADAM8 expression. In breast cancer, hypoxia can lead to cell death by necrosis. Hypoxia can also be overcome by inducing ADAM8 activation in tumor cells. This prevents tumor cells from growing and reduces the likelihood of metastases.
ADAM8 is expressed under several pathological conditions. TNBC, basal-like breast carcinomas, and TNBC have high levels ADAM8 DNA. They are associated for poorer prognosis. ADAM8 protein expression was also detected in breast cancer-derived metastases and adjacent normal marrow tissue. ADAM8 is a strong marker for breast carcinoma. It can detect both benign and malignant breast cancer cells.
The process of detecting antibodies in Western blotting involves moving target proteins to the membrane. These are the antibodies that will bind to the protein of curiosity. The process is based in protein migration, which can detect tiny proteins. The protein of curiosity can be either cells or tissue homogenates. In Western blotting, the size of a band corresponds with the amount of protein in a sample.
A WB procedure consists of two main steps, sample preparation and extraction. Because they determine the quality of the final blot, sample preparation and protein extract methods are critical. The western-blot protocol includes a detailed guide for both new and experienced researchers. To help identify problems, there is a comprehensive troubleshooting section. The positive control checks whether the antibody is effective by confirming that the target has been bound.
The second step involves the blocking of membrane unreacted sites. The second step involves blocking membrane unreacted sites. Finally, blockers should not cross-react with the detection reagents. BSA, gelatin, nonfat dry and milk are all common blockers. TBS is a common buffer.
Normally, proteins can be separated on a gel based on type and molecularweight. The separated proteins are then transferred on a gel by type and molecular weight. They are then probed with antibodies. The western-blot results can then be detected using chemiluminescence. In the quantitative western blot method, the proper selection of primary antibodies and the use of protein loading controls are key to maximizing signal.
A radio immunoprecipitation buffer is used to create protein lysates. Boster Biological Technology Co. Ltd. makes a BCA protein assay kits that can measure the protein concentration. The protein samples then are loaded onto a PVDF Membrane and electrophoresis takes place. After the protein lysates have separated, the samples are exposed to the Coomassie Brilliant Blue R-250 dye.
You can categorize Western blot antibody detection techniques as monoclonal (or polyclonal) using either monoclonal or multiclonal methods. Polyclonal antibodies are made up of multiple immunoglobulin molecules. They bind to many epitopes in a single antigen. These antibodies are usually produced from sheep, donkeys, and rabbits. Monoclonal antibodies, on the other hand, are homogenous, cloned immunoglobulin molecules that recognize a specific epitope of the target protein. Monoclonal antibodies are purified from the tissue culture supernat.
Boster Bio Anti ADAM8 antibody is available for identification. The antibody reacts with Human and has been tested in ELISA/WB. It can be stored at -20°C for one year. It is also available in liquid form in PBS. The liquid contains 50 % glucoserol and 0.02% of sodium azide.
The ADAM8 member of the ADAM family is a transmembrane gene. It mediates cell adhesion, migration, and proteolysis of extracellular matrix. It is synthesized via a signal sequencing. The ADAM8 Protein consists five domains plus a transmembrane. The cytoplasmic Tail is catalytically active and the four-dimensional MP Domain sheds cytokines.
ADAM8 secretes miR-710. It is remarkable that ADAM8 soluble can be absorbed into blood. TNBC cells expressing miR720 restored their migration capabilities and invasiveness. Patients with TNBC and healthy controls had serum samples that showed significantly higher levels ADAM8-positive tumors.
ADAM8 regulates eleven miRNAs. To screen ADAM8's expression, RNA preparations had to be used. All 11 miRNAs were reduced when ADAM8-2 was knocked out. The siADAM8-1 knockdown decreased eight miRNAs, while siADAM8-1 reduced three. ADAM8 knockdown also inducible several other miRNAs.
PMID: 9126482 by Yoshiyama K., et al. CD156 (human ADAM8): expression, primary amino acid sequence, and gene location.
PMID: 15574124 by Bartholin L., et al. FLRG, a new ADAM12-associated protein, modulates osteoclast differentiation.