Measured by the ability of the immobilized protein to support the adhesion of HFL1 human fetal lung fibroblast cells. The ED50 for this effect is 0.15-0.9 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived human Fibulin 2 protein Ala28-Leu1184 (Thr854Ala), with an N-terminal HA tag
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
125 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
150-175 kDa, reducing conditions
Publications
Read Publication using 9559-FB in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Fibulin 2 Protein, CF
FBLN2
FIBL-2
Fibulin 2
Fibulin-2
Background
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.
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