Recombinant Human DMBT1 His-tag Protein, CF Summary
Product Specifications
Thr20-Arg1662 (T31A, T42P, L54S, S1629L), with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
11032-DB
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
When Recombinant Human Siglec-8 Fc Chimera Protein (9045-SL) is immobilized at 5.0 μg/mL (100 μL/well), the concentration of Recombinant Human DMBT1 His-tag (Catalog # 11032-DB) that produces 50% of the optimal binding response is 0.500-5.00 μg/mL
2 μg/lane of Recombinant Human DMBT1 His-tag Protein (Catalog # 11032-DB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 225-285 kDa.
Reconstitution Calculator
Background: DMBT1
DMBT1 (Deleted in Malignant Brain Tumor 1) also known as Glycoprotein 340 and salivary agglutinin is a secreted glycoprotein with mass of 340 kDa. It belongs to group B of the SRCR (scavenger cysteine-rich) superfamily with each SRCR domain containing 8 cysteines (1). Primary sequence of DMBT1 is composed of 8-13 SRCR domains (due to alternative splicing), a CUB domain, another SRCR domain, a second CUB domain and ended with a ZP (zona pellucida) domain (2-3). DMBT1 is heavily glycosylated where N-linked and O-linked glycosylation account for almost 25% of the mass (3-4). It is mainly expressed in epithelial cells and mucosal tissues of respiratory and gastrointestinal tracts and urogenital organs. It is also found in human body fluids (saliva, tear, broncho-alveolar lavage, and pancreatic juice) (5-6). Extent of glycosylation varies among different tissues or individuals (7-8). Orthologues of DMBT1 have been found in monkey, mouse, rat, rabbit, bovine, and porcine. Human DMBT1 shares 49% and 35% amino acid homology with mouse and rat homolog. DMBT1 plays an important role in innate immune response. It is an agglutinating agent for several bacteria strains through a specific region in the SRCR domain in a calcium dependent way (9-10). It can also bind to viruses such as influenza A virus and human immunodeficiency virus type I and inhibit their activity. Binding to viruses is mediated by the sialic acid glycan of DMBT-1, independent of calcium. In addition to binding pathogens, DMBT-1 also binds a broad spectrum of host proteins including SP-d, SP-A, secretory IgA, refoil factors (TFFs), MUC5B, complement factor C1q, lactoferrin and DNA (11). Recent studies identify DMBT1 as a high affinity ligand of Siglec-8 in human airways (12). Inactivation of DMBT1 affects stem cell differentiation and results in tumor formation (13).
- Resnick, D. et al. (1994) Trends Biochem Sci. 19:5.
- Holmskov, U. et al. (1999) Proc Natl Acad Sci USA. 96:10794.
- Mollenhauer, J. et al. (1997) Nat Genet. 17:32.
- Prakobphol, A. et al. (2000) J Biol Chem. 275:39860.
- Mollenhauer, J. et al. (2000) Cancer Res. 60:1704.
- Stoddard, E. et al. (2007) J Immunol. 179:3126.
- Schulz, B. L. et al. (2002) Biochem J. 366:511.
- Eriksson, C. et al. (2007) Glycoconj J. 24:131.
- Bikker, F.J. et al. (2004) J Biol Chem. 279:47699.
- Madsen, J. et al. (2003) Eur J Immunol. 33:2327.
- Madsen, J. et al. (2010) Innate Immun. 16:160.
- Gonzalez-Gil, A. et al. (2021) J Allergy Clin Immunol. 147:1442.
- Ligtenberg, A. J. et al. (2007) Biol Chem. 388:1275.
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