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member of a family of non-histone chromosomal proteins [RGD, Feb 2006].. Additionally we are shipping HMGN2 Antibodies (72) and HMGN2 Kits (20) and many more products for this protein.
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Data show that high mobility group nucleosomal binding domain 2 (HMGN2) knockdown induced the increased expression of alpha5beta1 integrin on cell membranes, which resulted in a significant increase in Klebsiella pneumoniae internalization.
Data show that chronic lymphocytic leukemia (CLL) cells present high-mobility group (show SSRP1 Proteins) nucleosome-binding protein 2 (HMGN2) at membrane.
enhanced expression of HMGN2 in osteosarcoma cells by HMGN2 lentivirus, exerts inhibitory effects on growth and migration of osteosarcoma cells.
HMGN2 is an anti-tumor effector molecule of CD8 (show CD8A Proteins) T cells.
A polypeptide, HMGN2, was isolated and may be an antimicrobial effector molecule of mononuclear leukocytes.
HMGN2 is modified by covalent attachment of small ubiquitin-related modifier 1 (SUMO1 (show SUMO1 Proteins)) by pro-inflammatory signal and identified the major SUMOylated lysine residues that localize to the HMGN2 nucleosome-binding domain at Lys (show LYZ Proteins)-17 and Lys (show LYZ Proteins)-35.
HMGN2 is a bona fide Aurora B (show AURKB Proteins) substrate in vivo and show that its dynamic association to chromatin is controlled by Aurora B (show AURKB Proteins).
HMGN2 acts as a positive modulator of nuclear factor kappaB signalling to promote lipopolysaccharide-induced beta-defensin-2 (show DEFB4 Proteins) expression.
HMGN2 protein has antimicrobial activity and is probably involved in innate immunity in vivo.
The association of the PRLr (show PRLR Proteins) with HMGN2 enables Stat5a (show STAT5A Proteins)-responsive promoter binding, thus facilitating transcriptional activation and promoting anchorage-independent growth.
study demonstrates a role of HMGN2 in modulating specific gene expression and identifies beta-defensin-1 (show DEFB1 Proteins), beta-defensin-3 (show DEFB103A Proteins), and beta-defensin-4 (show DEFB4 Proteins) as HMGN2 targets during the development of ICR mice treated with LPS (show TLR4 Proteins)
The ectopic expression of Hmgn2 antagonizes mouse erythroid differentiation in vitro, which may be due to enhancement of DNA replication and/or blocking entry of mitosis at S-phase.
Rate of positive nuclei in early-cleaved embryos from small-versus large-follicles is similar for HMGN2 after parthenogenesis.
member of a family of non-histone chromosomal proteins
high mobility group nucleosome-binding domain-containing protein 2
, high mobility group protein N2
, high-mobility group (nonhistone chromosomal) protein 17
, high-mobility group nucleosomal binding domain 2
, non-histone chromosomal protein HMG-17
, nonhistone chromosomal protein HMG-17
, high mobility group protein 17
, high-mobility group nucleosome-binding domain-containing protein 2
, high mobility group nucleosomal binding domain 4
, high mobility group nucleosomal binding domain 2