|CSC-DC000016||Panoply™ Human AAMP Knockdown Stable Cell Line||Inquriy|
|CSC-SC000016||Panoply™ Human AAMP Over-expressing Stable Cell Line||Inquriy|
|CDCB156055||Rat AAMP ORF clone (NM_001106920.1)||Inquriy|
|CDCB157256||Mouse AAMP ORF clone (NM_146110.2)||Inquriy|
|CDCB163997||Chicken AAMP ORF Clone (NM_001079747)||Inquriy|
|CDCB179551||Danio rerio AAMP ORF Clone (NM_212938)||Inquriy|
|CDCB187795||Rabbit AAMP ORF clone (XM_002712473.2)||Inquriy|
|CDCL182510||Human AAMP ORF clone(NM_001087.3)||Inquriy|
|CDCR022680||Mouse Aamp ORF clone (NM_001190444.1)||Inquriy|
|CDCR268018||Mouse Aamp ORF Clone(NM_146110.3)||Inquriy|
|CDCS407385||Human AAMP ORF Clone (BC014122)||Inquriy|
|CDFG021455||Mouse Aamp cDNA Clone(NM_001190444.1)||Inquriy|
|CDFL000717||Mouse Aamp cDNA Clone(NM_146110.3)||Inquriy|
|MiUTR1H-00010||AAMP miRNA 3'UTR clone||Inquriy|
AAMP (angio-associated migratory cell protein) has six repeating WD40 domains. Its protein structure also has a large acidic amino acid region, a potential transmembrane region, and a potential serine/threonine phosphorylation site. AAMP is structurally homologous to the cell adhesion molecule proteins NCAM, PECAM (CD31), LFA-2, etc. of the immunoglobulin superfamily (AA231-299). This indicates that AAMP plays a more important role in cell adhesion and migration. The AAMP protein also has a positively charged region at the amino terminus with a strong heparin binding potential similar to PECAM (CD31). PECAM-mediated cell aggregation can be inhibited by heparin and chondroitin sulfate. AAMP-derived peptide P189-mediated cell binding and aggregation can also be inhibited by heparin. P189 can be polymerized into granules and used as a heparin-sensitive cell polymerizer to bind and aggregate MCF-7 breast cancer cells and A2058 melanoma cells.
AAMP's biological function
AAMP is expressed in a variety of tissue cells and is highly expressed in vascular endothelial cells, placental trophoblasts, and poorly differentiated colon cancer cells in lymphatic vessels, suggesting that AAMP may have similar functions in migrating cells. In addition, AAMP is expressed in other cells such as vascular smooth muscle cells (VSMCs), epidermal fibroblasts, T lymphocytes, renal tubular epithelial cells, mesangial cells, muscle cells, and various tumor cells such as melanoma cells, breast cancer cells, prostate cancer cells, etc. The AAMP protein in VSMCs is abundantly distributed in the cytoplasm and extracellular matrix, while in epidermal fibroblasts and mesangial cells, AAMP is mainly located on the surface of cytoplasm and cells, and the distribution in extracellular matrix is less.
AAMP shares a common epitope with α-actinin and rapidly contracting skeletal muscle fibrin (fast muscle fibers). AAMP polyclonal antibodies can compete with α-actinin and AAMP, and AAMP polyclonal antibodies can also immunoreact with fast muscle fibers. Α-actinin protein structure but does not exist in the AAMP of similar sequences, secondary structures may be two or higher order structures produced similar conformational epitopes. However, studies in EA.hy926 cells showed that AAMP does not bind to α-actinin, and there is no co-localization in the cells. This proves that α-actinin and AAMP have similar structures, but the two do not interact directly.
Figure 1. AAMP polyclonal antibodies can compete with α-actinin and AAMP. (Yin, et al. 2014)
Co-culture of bovine aortic endothelial cells (BAECs) and human astrocytes in the Transwell system resulted in a 53% increase in AAMP outside the BAECs. Therefore, astrocytes increase the amount of AAMP in endothelial cells and may promote angiogenesis in the nervous system. Due to the high expression of AAMP in vascular endothelial cells, Ge et al. listed AAMP as a functional marker molecule for endothelial cells.
AAMP and disease
AAMP is primarily involved in cell migration, so it may be involved in many pathological processes such as tumor invasion and metastasis that have cell migration events. Interference with AAMP expression in the breast cancer cell line MDA-MB-231 had no significant effect on cell proliferation. Yin et al. found that high levels of AAMP transcriptional profiles are associated with breast cancer progression, metastasis, and patient prognosis. Breast cancer patients with lower AAMP expression levels have longer survival than patients with higher AAMP expression levels. Therefore, the expression level of AAMP has a significant effect on the biological function of breast cancer cells, and the high expression level of AAMP means that the prognosis of breast cancer patients is poor and the risk of tumor metastasis is greater.
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