ITN2889
ITN2889
- Catalog: ITN2889
- Gene/Protein: DMBT1 GP340
- Product Description: Immunotag™ DMBT1 Polyclonal Antibody
385.0000
Price in reward points: 385
| Antibody Specification | |
| Datasheet | 
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| Target Protein | DMBT1 |
| Clonality | Polyclonal |
| Storage/Stability | -20°C/1 year |
| Application | IHC-p |
| Recommended Dilution | IHC-p 1:50-300 |
| Concentration | 1 mg/ml |
| Reactive Species | Human,Mouse,Rat |
| Host Species | Rabbit |
| Immunogen | Synthesized peptide derived from part region of human protein |
| Specificity | DMBT1 Polyclonal Antibody detects endogenous levels of protein. |
| Purification | The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen |
| Form | Liquid in PBS containing 50% glycerol, and 0.02% sodium azide. |
| Gene Name | DMBT1 GP340 |
| Accession No. | Q9UGM3 Q60997 Q8CIZ5 |
| Description | deleted in malignant brain tumors 1(DMBT1) Homo sapiens Loss of sequences from human chromosome 10q has been associated with the progression of human cancers. This gene was originally isolated based on its deletion in a medulloblastoma cell line. This gene 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 encoded protein precursor 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 suppressor gene, but rather play a role in the interaction of tumor cells and the immune system. [provided by RefSeq, Mar 2016], |
| Protein Expression | Brain,Lung,Saliva,Small intestine,Trachea, |
| Subcellular Localization | extracellular region,extracellular space,cytoplasm,membrane,extrinsic component of membrane,phagocytic vesicle membrane,zymogen granule membrane,extracellular exosome, |
| Protein Function | More isoforms may exist,developmental stage:Expressed in fetal lung, intestine and skin. Secreted to the extracellular matrix (ECM) in certain fetal epithelia.,disease:A deletion allele of DMBT1 which lacks five of the SRCR domains is associated with an increased risk of Crohn disease.,disease:Defects in DMBT1 are the cause of glioma of the brain [MIM:137800]. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas.,disease:Inactivation of DMBT1 plays an important role in carcinogenesis. A loss or reduction of DMBT1 expression was seen in esophageal, gastric, lung and colorectal carcinomas. Deleted in medulloblastoma and glioblastoma cell lines. Homozygous deletions may be the predominant mechanism of inactivation.,domain:The SRCR domains mediate binding to bacteria. The minimal bacterial-binding site is an 11-residue repeat of GRVEVLYRGSW where VEVL and W are critical residues.,function:May be considered as a candidate tumor suppressor gene for brain, lung, esophageal, gastric, and colorectal cancers. May play roles in mucosal defense system, cellular immune defense and epithelial differentiation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. Required for terminal differentiation of columnar epithelial cells during early embryogenesis. May function as a binding protein in saliva for the regulation of taste sensation. Binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell.,induction:Up-regulated in intestinal epithelial cells in response to proinflammatory stimuli including TNF-alpha and LPS.,polymorphism:The number of SRCR and SRCR-interspersed domains is polymorphic in a variety of tumors and may represent the major site of alterations in cancer.,PTM:Highly N- and O-glycosylated. The O-glycans are heavily sulfated.,similarity:Belongs to the DMBT1 family.,similarity:Contains 1 ZP domain.,similarity:Contains 14 SRCR domains.,similarity:Contains 2 CUB domains.,subcellular location:Some isoforms may be membrane-bound. Localized to the lumenal aspect of crypt cells in the small intestine. In the colon, seen in the lumenal aspect of surface epithelial cells. Formed in the ducts of von Ebner gland, and released into the fluid bathing the taste buds contained in the taste papillae.,subunit:Interacts with LGALS3 (By similarity). Binds SFTPD and SPAR in a calcium-dependent manner. Binds to HIV-1 glycoprotein 120.,tissue specificity:Highly expressed in alveolar and macrophage tissues. In some macrophages, expression is seen on the membrane, and in other macrophages, strongly expressed in the phagosome/phagolysosome compartments. Expressed in lung, trachea, salivary gland, small intestine and stomach. In pancreas, expressed in certain cells of the islets of Langerhans. In digestive tract, confined to tissues with large epithelial surfaces. In intestinal tissue, moderately expressed in epithelial cells of the midcrypts and the crypt base. Expression is significantly elevated in intestinal tissue from patients with inflammatory bowel disease (IBD), particularly in surface epithelial and Paneth cells, but not in IBD patients with mutant NOD2. Present in crypt bases of the duodenum, in crypt tops of the colon, and in collecting ducts of the cortical kidney. Expressed in stratified squamous epithelium of vagina and in outer luminar surface and basilar region of columnar epithelial cells in cervix (at protein level). Isoform 1 is secreted to the lumen of the respiratory tract., |
| Usage | For Research Use Only! Not for diagnostic or therapeutic procedures. |
| Material Safety Data Sheet | |
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