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MFAP5 encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. Zusätzlich bieten wir Ihnen MFAP5 Proteine (14) und MFAP5 Kits (12) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 46 products:
Human Polyclonal MFAP5 Primary Antibody für ELISA, WB - ABIN563536
Luistro, He, Smith, Packman, Vilenchik, Carvajal, Roberts, Cai, Berkofsky-Fessler, Hilton, Linn, Flohr, Jakob-Røtne, Jacobsen, Glenn, Heimbrook, Boylan: Preclinical profile of a potent gamma-secretase inhibitor targeting notch signaling with in vivo efficacy and pharmacodynamic properties. in Cancer research 2009
Human Polyclonal MFAP5 Primary Antibody für IHC, IHC (p) - ABIN4332461
Leung, Yeung, Yip, Pradeep, Balasubramanian, Liu, Wong, Mangala, Armaiz-Pena, Lopez-Berestein, Sood, Birrer, Mok: Calcium-dependent FAK/CREB/TNNC1 signalling mediates the effect of stromal MFAP5 on ovarian cancer metastatic potential. in Nature communications 2014
Likely pathogenic variants included a TGFB2 (zeige TGFB2 Antikörper) variant in one patient and a SMAD3 (zeige SMAD3 Antikörper) variant in another. These variants have been reported previously in individuals with similar phenotypes. Variants of uncertain significance of particular interest included novel variants in MYLK (zeige MYLK Antikörper) and MFAP5, which were identified in a third patient
The results answer the question of how MAGP2 controls cell type dependent Notch (zeige NOTCH1 Antikörper) signaling, but more importantly uncover a new mechanism to understand how extracellular matrices and cellular environments impact Notch (zeige NOTCH1 Antikörper) signaling.
Our results demonstrate that factors involving low-grade inflammation modulate MFAP5 expression and that the modified expression of MFAP5 may further regulate adipose tissue inflammation.
FAK (zeige PTK2 Antikörper)/CREB (zeige CREB1 Antikörper)/TNNC1 (zeige TNNC1 Antikörper) has a role in mediating the effect of stromal MFAP5 on ovarian cancer metastatic potential
Alteration of MAGP-2, a component of microfibrils and elastic fibers, appears as an initiating mechanism of inherited Thoracic aortic aneurysm and dissection (TAAD).
EPS led to the discovery of two novel immunomodulatory proteins, MFAP5 and PENK (zeige PENK Antikörper) that when administered to mice subjected to endotoxemic shock, reversed the cytokine storm and provided a significant survival benefit
Decreased MFAP5 gene expression in the endometrium of patients with implantation failure after in vitro ertilization treatment
The MAGP2-based assay provided superior performance for the purpose of cell culture identification compared to assays using standard reference genes.
microfibrillar proteins MAGP-1 (zeige MFAP2 Antikörper) and MAGP-2 can function outside of their role in elastic fibers to activate a cellular signaling pathway
MAGP-2 promotes angiogenic cell spouting in vitro by antagonizing Notch (zeige NOTCH1 Antikörper) signaling pathways in endothelial cells.
Binding of MAGP2 to microfibrils is regulated by proprotein convertase cleavage.
Loss of MAGP2 expression in vivo has pleiotropic effects.
interaction with fibrillin-1 (zeige FBN1 Antikörper) and fibrillin-2 (zeige FBN2 Antikörper) suggesting role in elastic fiber assembly
Tight skin fibrillin 1 (zeige FBN1 Antikörper) altered extracellular matrix organization and caused fibrosis by affecting deposition of MAGP-2 or other fibrillin-1 (zeige FBN1 Antikörper)-associated proteins.
microfibril-associated MAGP-2 may stimulate elastic fiber macroassembly by targeting the release of elastin (zeige ELN Antikörper) globules from the cell membrane onto developing elastic fibers
MAGP-2 is identified as a novel regulator of angiogenesis.
results show MAGP-2 is covalently and periodically located along the fibrillin-containing microfibrils of the developing nuchal ligament, suggesting that it is an integral component of most if not all of the microfibrils in this elastic fiber-rich tissue
This gene encodes a 25-kD microfibril-associated glycoprotein which is rich in serine and threonine residues. It lacks a hydrophobic carboxyl terminus and proline-, glutamine-, and tyrosine-rich regions, which are characteristics of a related 31-kDa microfibril-associated glycoprotein (MFAP2). The close similarity between these two proteins is confined to a central region of 60 aa where precise alignment of 7 cysteine residues occurs. The structural differences suggest that this encoded protein has some functions that are distinct from those of MFAP2.
microfibrillar associated protein 5
, microfibril-associated glycoprotein 2
, microfibril-associated glycoprotein-2
, microfibrillar-associated protein 5