Recombinant Human Fibulin 2 Protein, CF Summary
Ala28-Leu1184 (Thr854Ala), with an N-terminal HA tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant Human Fibulin 2 (Catalog # 9559-FB) supports HFL1 human fetal lung fibroblast cell adhesion. The ED50 for this effect is 0.15-0.9 μg/mL
Background: Fibulin 2
Fibulin 2 is the second largest member of the seven-member fibulin family of extracellular membrane (ECM) glycoproteins. Fibulin-2 consists of 1184 amino acids (aa) with a predicted molecular weight of ~125 kDa. The overall structure is common to fibulins: 3 Anaphylatoxin (AT)-like domains, 11 Epidermal Growth Factor (EGF)‑like domains, and a Fibulin-type carboxy-terminal (FC) domain (1-4). Fibulin 2 is considered a Class I fibulin because the 400-residue N-terminus is divided into the Na and Nb sections, with the Na section containing 150-residues and 12 cysteines while the remaining Nb section is cysteine-free (2, 3). The protein is known to form disulfide-linked homodimers, but it can also be secreted as an oligomer (5). Fibulin 2 is highly conserved across species, with the human protein sharing 82% amino acid identity compared to both mouse and rat. Fibulin 2 is considered a multifunctional binding protein due to its association with numerous ECM components, but its specific interactions have yet to be determined (6). Fibulin 2 is localized at the interface between microfibrils and the elastin core and its known interactions include nidogen-1, perlecan, laminin, aggrecan, endostatins, versican, collagen, and tropoelastin (1, 2, 4, 7). It is down-regulated in numerous forms of cancer including breast, colorectal, lung, esophageal, and squamous cell carcinoma, but over-expression has been shown with solid tumors (1, 3, 4). There is also evidence that suggests that Fibulin 2 may play an indirect role in the neurogenesis of adult neural stem cells via interaction with integrins and TGF-beta 1 (8).
- Alcendor et al. (2011) Am. J. Pathol. 179:1443.
- Timpl et al. (2003) Nat. Rev. Mol. Cell Biol. 4:479.
- Kanan et al. (2014) J. Biol. Chem. 289:13419.
- Argraves et al. (2003) EMBO reports 4:1127.
- Pan et al. (1993) J. Cell Biol. 123:1269.
- Fontanil et al. (2014) Oncotarget 5:1253.
- El-Hallous et al. (2007) J. Biol. Chem. 282:8935.
- Radice et al. (2015) Mol. Cell. Neurosci. 67:75.
Citation for Recombinant Human Fibulin 2 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Astrocyte-derived small extracellular vesicles promote synapse formation via fibulin-2-mediated TGF-&beta signaling
Authors: MR Patel, AM Weaver
Cell Reports, 2021;34(10):108829.
Sample Types: Whole Cells
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