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MATN2 encodes a member of the von Willebrand factor A domain containing protein family. Additionally we are shipping Matrilin 2 Kits (5) and Matrilin 2 Proteins (5) and many more products for this protein.
Showing 10 out of 44 products:
Human Polyclonal MATN2 Primary Antibody for WB - ABIN1881529
Deák, Piecha, Bachrati, Paulsson, Kiss: Primary structure and expression of matrilin-2, the closest relative of cartilage matrix protein within the von Willebrand factor type A-like module superfamily. in The Journal of biological chemistry 1997
Show all 5 Pubmed References
Human Polyclonal MATN2 Primary Antibody for ELISA, WB - ABIN4332839
Zhang, Zhang, Huang, Zhou, Du, Yi, Luo: High glucose-induced Matrilin-2 expression in mouse mesangial cells was mediated by transforming growth factor beta 1 (TGF-β1). in Biochemical and biophysical research communications 2016
Cow (Bovine) Polyclonal MATN2 Primary Antibody for WB - ABIN2787330
Ichikawa, Suenaga, Koda, Ozaki, Nakagawara: DeltaNp63/BMP-7-dependent expression of matrilin-2 is involved in keratinocyte migration in response to wounding. in Biochemical and biophysical research communications 2008
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findings showed that YopK binds to the cell surface-exposed endogenous MATN2 and that purified YopK protein strongly inhibits the bacterial adherence to HeLa cells
Data show that the mRNA and protein levels of matrilin-2 were increased after irradiation treatment in both mouse lung tissue and human pulmonary alveolar epithelial cells (HPAEpiC).
Taken together, our results showed that high-glucose-induced Matrilin-2 expression that was mediated by the TGF-beta1 (show TGFB1 Antibodies)/Smad3 (show SMAD3 Antibodies) signaling pathway might play a role in Diabetic nephropathy (DN) pathogenesis and our finding provided a potential diagnostic and/or therapeutic target for DN.
Matrilin-2 induces post-burn inflammatory responses as an endogenous danger signal, partly through a TLR4 (show TLR4 Antibodies)-mediated mechanism
matrilin-2, a filament-forming protein widely distributed in extracellular matrices.
matrilin-2 is expressed in normal skin by keratinocytes and fibroblasts and may thus contribute to cutaneous homeostasis.
study of interactions by which matrilin-2 can be integrated into extracellular filamentous networks
These results suggest that matrilin-2 may be a specific and clinically useful biomarker for discriminating between indolent and clinically aggressive pilocytic astrocytoma.
DeltaNp63/BMP-7 (show BMP7 Antibodies) signaling pathway modulates wound healing process through the regulation of matrilin-2.
data indicate matrilin-2 is a novel basement membrane component in the liver, synthesized during sinusoidal "capillarization" in cirrhosis & in hepatocellular carcinoma
Matn2 functions as a tumor suppressor in hepatocarcinogenesis, and in this process activation of EGFR (show EGFR Antibodies) together with that of Erk1/2 (show MAPK1/3 Antibodies), as well as inactivation of GSK-3beta (show GSK3b Antibodies), play strategic roles.
The absence of matrilin-2 has no effect on hepatic stellate cell activation and regression kinetics, synthetic activity, proliferative capacity, motility, or HSC (show FUT1 Antibodies) apoptosis.
MATN2 is a deleterious endogenous neuroaxonal injury response signal that activates innate immune cells.
Matrilin-2 may play an important role in the communication of matrix to matrix and matrix to cells and will be used as a potential biomarker in the early stage of osteoarthritis of articular cartilage.
Expression of matrilin-2 during maturation of mouse skeletal tissues
Matrilin-2 null mice show no gross abnormalities during embryonic or adult development, are fertile, and have a normal lifespan.
matrilin 2 is a permissive substrate for axonal growth and cell migration, and that it is required for successful nerve regeneration.
This gene encodes a member of the von Willebrand factor A domain containing protein family. This family of proteins is thought to be involved in the formation of filamentous networks in the extracellular matrices of various tissues. This protein contains five von Willebrand factor A domains. The specific function of this gene has not yet been determined. Two transcript variants encoding different isoforms have been found for this gene.