Recombinant Human MFAP4 Protein, CF

When Recombinant Human MFAP4 (Catalog # 10230-MF) is coated at 0.5 μg/mL, 100 μL/well, Recombinant Human Fibrillin-1/FBN1 Fc Chimera (Catalog # 10224-FI) binds with an ED50 of 0.1-0.6 μg/mL.

2 μg/lane of Recombinant Human MFAP4 (Catalog # 10230-MF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 35-45 kDa and 70-90 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human MFAP4 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human MFAP4 (Catalog # 10230-MF) is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Human Fibrillin-1/FBN1 Fc Chimera (Catalog # 10224-FI) nbsp; that produces 50% of the optimal binding response is 0.1-0.6 μg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human MFAP4 protein
  Val22-Ala255, with an N-terminal c-Myc Tag
• Accession #: P55083
• N-terminal Sequence: Glu (c-Myc Tag)
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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: 28 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: 35-45 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: 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 with Trehalose.
• Purity: >95%, 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 MFAP4 Protein, CF

• MFAP4
• MFAP-4
• microfibril-associated glycoprotein 4
• microfibrillar-associated protein 4

Background

Microfibrillar-associated protein 4 (MFAP4) is an extracellular glycoprotein found in elastic fibers that may support elastic fiber maintenance and assembly (1). It contains fibrinogen-like domains and an RGD sequence in the N-terminus that serves as the ligand motif for the cell receptor integrin (2). MFAP4 exists as a disulfide-linked dimer that is able to form higher oligomeric structures (3). Mature human FAP4 shares 95% amino acid sequence identity with mouse and bovine MFAP4. Binding analysis revealed that MFAP4 specifically binds tropoelastin and firillin-1 and -2, as well as the elastin cross-linking amino acid desmosine, and it co‑localizes with fibrillin-1 positive fibers in vivo (1). MFAP4 contributes to the development of elastic fiber and may play a potential role in extracellular matrix (ECM) turnover during fibrogenesis (2, 4). Immunohistochemical studies showed that MFAP4 is highly abundant in hepatic stellate cells and cirrhotic ECM, but not in hepatic parenchyma or normal liver (4). MFAP4 interacts with different collectins in the lung and might fix them in the ECM during inflammation (5). Serum MFAP4 concentrations increased with progressive stages (fibrosis stage 0-4) of hepatic fibrosis in patients and has been proposed as a biomarker for hepatic fibrosis (6, 7).

1. Pilecki, B. et al. (2016) J. Biol. Chem. 291:1103.
2. Gressner, O.A. et al. (2007) J. Cell Mol. Med. 11:1031.
3. Schlosser A. et al. (2006) Scand J Immunol. 64:104.
4. Hunes RO. (1992) Cell. 69:11.
5. Kasamatsu, S. et al. (2011) Sci. Rep. 1:164.
6. Lausen, M. et al. (2017) J. Biol. Chem. 274:32234.
7. Molleken, C. et al. (2009) Hepatology. 49:1257.

Bioinformatics

• Uniprot:
  • P55083()