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anti-Human DMBT1 Antibodies:
anti-Mouse (Murine) DMBT1 Antibodies:
anti-Rat (Rattus) DMBT1 Antibodies:
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Exosomal DMBT1 from human urine-derived stem cells facilitates diabetic wound repair by promoting angiogenesis.
Present study indicated that DMBT1 is upregulated in stools of colorectal cancer (CRC) patients, while exhibiting variable expression in CRC tissues. Loss of DMBT1 protein in CRC tissues is significantly associated with adverse clinicopathological features (advanced stage, lymph node or distant metastasis and high histological grade).
We investigated whether PRH1 and PRH2 polymorphisms in saliva acidic proline-rich protein (PRP) receptors for indigenous bacteria match and predict individual differences in the development of caries..They instead developed 3.9-fold more caries than P1 children from plaque accumulation in general when treated with orthodontic multibrackets; and had basic PRP polymorphisms and low DMBT1-mediated S. mutans adhesion
We found that in 3 different populations, mucosal DMBT1 expression was significantly increased (2.5 fold) in individuals with dysplasia compared to multifocal atrophic gastritis without intestinal metaplasia; the increase was also observed in individuals with advanced gastritis and positive H. pylori infection.
DMBT1 is expressed differently in cholangiocarcinogenesis and poorer patients' survival rates are associated with absent DMBT1 expression in non-neoplastic biliary tissue, suggesting a tumour-suppressive role of DMBT1 in early cholangiocarcinogenesis
we conclude that DMBT1 by binding with CRNDE and c-IAP1 associated with PI3K-AKT pathway is crucial for GBC carcinogenesis, and targeting this pathway may be pivotal in the treatment of GBC.
Studies indicate that salivary scavenger and agglutinin (SALSA) binds to many microbes and endogenous complement components.
The data suggest that DMBT1 inhibition of twitching motility contributes to the mechanisms by which mucosal fluids protect against P. aeruginosa infection.
this study shows that SAG inhibits the Interaction of DC-SIGN and Langerin with oral microorganisms
These results support the hypothesis that genetic variation in DMBT1 may influence microbial defense.
DMBT1 DNA copy number variation does not affect susceptibility to Crohn's disease in Northern Europeans.
this study shows that salivary agglutinin modulates the lectin pathway of the complement system
DMBT1 can potentially serve as a biomarker for early Acute respiratory distress syndrome diagnosis and disease severity assessment.
The copy number variation at DMBT1 does not affect risk of developing age-related macular degeneration and can therefore be ruled out from future studies investigating the association of structural variation at 10q26 with age-related macular degeneration.
The basal and meconium-induced NO production in lung epithelial cells is positively regulated by DMBT1.
SALSA, together with fibronectin and C1q, may be involved in the containment of injured placental structures into fibrinoids.
The DMBT1 may play a role in epithelial differentiation and local innate immunity during neonatal inflammatory bowel processes.
Data indicate that DMBT1 promotes VEGF and suppresses IL-6 production in alveolar tissues, which could point to DMBT1 having a possible role in the transition from inflammation to regeneration.
Gp340 expression patterns at these sites were also distinct.
multiallelic copy number variation (CNV) within DMBT1 is extensive across all populations.
a novel role for interleukin-27 (IL-27) as mediator of intestinal epithelial barrier protection mediated via DMBT1 and IDO1
DMBT1 functions as an important endothelium-derived ECM protein that is able to bind angiogenic factors and promote adhesion, migration, proliferation, and angiogenesis as well as vascular repair.
Data show that deletion of hensin from intercalated cells results in the absence of typical alpha-intercalated cells and the consequent development of complete distal renal tubular acidosis (dRTA).
Carboxyl-terminal Asp(D) -3, Thr(T) -2, Lys(K) -1 and Leu(L) 0 are involved in numerous interactions with PDZ1 domains of NHERF/EBP50 and PDZK1/CAP70.
binds gram-positive and gram-negative bacteria and interacts with lung surfactant protein D
Muclin is a Golgi cargo receptor that binds to regulated secretory proteins under the mildly acidic pH conditions that exist in the trans-Golgi network
Mouse embryonic stem cells seeded on hensin formed hemispheric epithelial structures whose outermost layer terminally differentiated to an epithelium that resembled the visceral endoderm.
The results identify a novel mammary tumor susceptibility locus in mice and support a role for DMBT1 in suppression of mammary tumors in both mice and women.
Dmbt1(-/-) mice display enhanced susceptibility to dextran sulfate sodium-induced colitis and elevated Tnf, Il6, and Nod2 expression levels during inflammation.
Muclin deficiency impairs trafficking of regulated proteins to a stimulus-releasable pool in the exocrine pancreas
Expression of pro-Muclin (Dmbt1) in rat pancreatic AR42J cells induces functional regulated secretory granules.
CRP-ductin (also known as Muclin) is upregulated in the pancreas and gastrointestinal tract of CFTR knockout mice. This sulfated glycoprotein may be a protective molecule upregulated by inflammation.
Demonstrate that galectin-3 plays a critical role in hensin ECM assembly by oligomerizing secreted monomeric hensin.
Data suggest that DMBT1 is secreted by oviduct epithelium and plays role in sperm-ovum interactions during in vitro fertilization.
Sperm binding to porcine oviductal cells is mediated by SRCR domains contained in DMBT1
Involvement of AKAP4 in the formation of the fibrous sheath on boar precursor sperm cells and the phosphorylation of pro-AKAP4 as an early step in the signal transduction pathway gated by DMBT1 that leads to sperm selection through acrosome alteration.
Loss of sequences from human chromosome 10q has been associated with the progression of human cancers. The gene DMBT1 was originally isolated based on its deletion in a medulloblastoma cell line. DMBT1 is expressed with transcripts of 6.0, 7.5, and 8.0 kb in fetal lung and with one transcript of 8.0 kb in adult lung, although the 7.5 kb transcript has not been characterized. The DMBT1 protein is a glycoprotein containing multiple scavenger receptor cysteine-rich (SRCR) domains separated by SRCR-interspersed domains (SID). Transcript variant 2 (8.0 kb) has been shown to bind surfactant protein D independently of carbohydrate recognition. This indicates that DMBT1 may not be a classical tumor supressor gene, but rather play a role in the interaction of tumor cells and the immune system.
, deleted in malignant brain tumors 1 protein
, glycoprotein 340
, salivary agglutinin
, surfactant pulmonary-associated D-binding protein
, deleted in malignant brain tumors 1 pseudogene
, glycoprotein 300
, mucin-like glycoprotein
, deleted in malignant brain tumors 1
, hypothetical protein