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Mouse Anti-DMBT1 Recombinant Antibody (G-4) (CBMAB-D1168-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
G-4
Antibody Isotype
IgG
Application
WB, IP, IF, ELISA

Basic Information

Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Deleted In Malignant Brain Tumors 1
Introduction
DMBT1 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. DMBT1 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.
Entrez Gene ID
Human1755
Mouse12945
Rat170568
UniProt ID
HumanQ9UGM3
MouseQ60997
RatQ8CIZ5
Alternative Names
Deleted In Malignant Brain Tumors 1; Salivary Agglutinin; Surfactant Pulmonary-Associated D-Binding Protein; Salivary Scavenger And Agglutinin; Glycoprotein 340; Gp-340; Hensin;
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.
Biological Process
Antimicrobial humoral immune response mediated by antimicrobial peptide Source: UniProtKB
Defense response Source: GO_Central
Defense response to Gram-negative bacterium Source: UniProtKB
Defense response to Gram-positive bacterium Source: UniProtKB
Defense response to virus Source: UniProtKB-KW
Detection of bacterial lipoprotein Source: GO_Central
Epithelial cell differentiation Source: UniProtKB
Induction of bacterial agglutination Source: UniProtKB
Innate immune response Source: UniProtKB
Protein transport Source: UniProtKB-KW
Receptor-mediated endocytosis Source: UniProtKB
Cellular Location
Secreted. 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 (By similarity).
Involvement in disease
Glioma (GLM):
The gene represented in this entry is involved in disease pathogenesis. Homozygous deletions may be the predominant mechanism of DMBT1 inactivation playing a role in carcinogenesis. DMBT1 is deleted in medulloblastoma and glioblastoma cell lines; point mutations have also been reported in patients with glioma. A loss or reduction of DMBT1 expression has been seen in esophageal, gastric, lung and colorectal carcinomas as well. Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
PTM
Highly N- and O-glycosylated. The O-glycans are heavily sulfated (By similarity).
More Infomation

Nexoe, A. B., Pedersen, A. A., von Huth, S., Sorensen, G. L., Holmskov, U., Jiang, P. P., ... & Rathe, M. (2021). No effect of deleted in malignant brain tumors 1 deficiency on chemotherapy induced murine intestinal mucositis. Scientific Reports, 11(1), 1-11.

Hains, D. S., Polley, S., Liang, D., Saxena, V., Arregui, S., Ketz, J., ... & Schwaderer, A. L. (2021). Deleted in malignant brain tumor 1 genetic variation confers urinary tract infection risk in children and mice. Clinical and Translational Medicine, 11(7).

Wang, L., Tuo, H., Song, Z., Li, W., & Peng, Y. (2021). Reg3A (regenerating family member 3 alpha) acts as a tumor suppressor by targeting DMBT1 (deleted in malignant brain tumors 1) in gastric cancer. Bioengineered, 12(1), 7644-7655.

Bathum Nexoe, A., Pedersen, A. A., von Huth, S., Detlefsen, S., Hansen, P. L., & Holmskov, U. (2020). Immunohistochemical localization of deleted in malignant brain tumors 1 in normal human tissues. Journal of Histochemistry & Cytochemistry, 68(6), 377-387.

Qu, N., Shi, R. L., Liao, T., Huang, S. L., Wen, D., Hu, J. Q., ... & Ji, Q. H. (2020). Germline missense mutation of Deleted in malignant brain tumor 1 (DMBT1) in familial mediastinal neuroendocrine cancer and in vitro effects in thyroid cancer cells. Neuroendocrinology, 110(7-8), 714-720.

Müller, H., Schmiedl, A., Weiss, C., Ai, M., Jung, S., & Renner, M. (2020). DMBT1 is upregulated in lung epithelial cells after hypoxia and changes surfactant ultrastructure. Pediatric Pulmonology, 55(11), 2964-2969.

Zhang, C. X. (2019). The protective role of DMBT1 in cervical squamous cell carcinoma. The Kaohsiung journal of medical sciences, 35(12), 739-749.

Park, H. S., Kim, B. C., Yeo, H. Y., Kim, K. H., Yoo, B. C., Park, J. W., & Chang, H. J. (2018). Deleted in malignant brain tumor 1 is a novel prognostic marker in colorectal cancer. Oncology reports, 39(5), 2279-2287.

Valero, A., Roldán, M. L., Ruiz, M. F., Teijeiro, J. M., Marquez, S. B., & Marini, P. E. (2018). Deleted in Malignant Brain Tumor 1 (DMBT1) expression pattern in normal cervix and at different stages of squamous intraepithelial lesions. The Open Biomarkers Journal, 8(1).

Garay, J., Piazuelo, M. B., Lopez-Carrillo, L., Leal, Y. A., Majumdar, S., Li, L., ... & Zabaleta, J. (2017). Increased expression of deleted in malignant brain tumors (DMBT1) gene in precancerous gastric lesions: Findings from human and animal studies. Oncotarget, 8(29), 47076.

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For research use only. Not intended for any clinical use.

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