Recombinant Human Fibrillin-1/FBN1 Fc Chimera 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.

1 μg/lane of Recombinant Human Fibrillin-1/FBN1 Fc Chimera (Catalog # 10224-FI) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 97-108 kDa and 190-220 kDa, respectively.

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

Recombinant Human Fibrillin-1/FBN1 Fc Chimera 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) that produces 50% of the optimal binding response is 0.1-0.6 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived human Fibrillin-1/FBN1 protein
  

  Human Fibrillin-1 (Ala25-Thr660) Accession # P35555	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: P35555
• N-terminal Sequence: Ala25
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 95 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: 97-108 kDa

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 under reducing conditions and visualized by silver stain.
• 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 Fibrillin-1/FBN1 Fc Chimera Protein, CF

• ACMICD
• Asprosin
• FBN
• FBN1
• fibrillin 1 (Marfan syndrome)
• Fibrillin 1
• fibrillin 15
• fibrillin-1
• GPHYSD2
• MASS
• MFS1
• OCTD
• SGS
• SSKS
• WMS
• WMS2

Background

Fibrillins are glycoproteins forming the backbone of microfibrils in elastic and non-elastic tissues. They interact with other components of the extracellular matrix (ECM) and play essential roles in tissue development, homeostasis and repair. Fibrillin-1 is a calcium-binding protein that assembles to form the structural component of the 10-12 nm microfibrils of the ECM. The human Fibrillin-1 has multiple domains, primarily consisting of epidermal growth factor (EGF)-like and other modules (1, 2). The calcium-binding modules in some of the EGF domains provide structural stability and the characteristic rod-like shape of the protein (3-8). Mature human Fibrillin-1 shares 97% amino acid (aa) sequence identity with mature mouse Fibrillin-1. Human Fibrillin-1 is synthesized as an approximately 350-kDa precursor molecule, which is then proteolytically processed by furin into its biologically active form (9-10). Fibrillin microfibers are further engaged in a number of cell matrix interactions such as with integrins, bone morphogenetic proteins (BMPs) and the large latent complex of transforming growth factor-beta (11). Fibrillin-1 mutations are associated with a range of heritable connective disorders, including Marfan syndrome and acromelic dysplasias (11-12).

1. Robertson, I. et al. (2011) Biochem. J. 433:263.
2. Corson, G.M. et al. (1993) Genomics 17:476.
3. Maslen, C.L. et al. (1991) Nature 352:334.
4. Hanford, P.A. et al. (1991) Nature 353:395.
5. Werner, J.M. et al. (2000) J. Mol. Biol. 296:1065.
6. Downing, A.K. et al. (1996) Cell 85:597.
7. Smallridge, R.S. et al. (2003) J. Biol. Chem. 278:12199.
8. Reinhardt, D.P. et al. (1997) J. Biol. Chem. 272:7368.
9. Raghunath, M. et al. (1999) J. Cell. Sci. 112:1093.
10. Wallis, D.D. et al. (2003) J. Cell. Sci. 90:641.
11. Jensen, S.A. et al. (2016) Biochem. J. 473:827.
12. Sherratt, M.J. et al. (2001) Micron. 32:185.

FAQs for Fibrillin 1 (10224-FI). (Showing 1 - 1 of 1 FAQ).

1. Hi - I have been looking at the fibrillin1 antibodies on your website. You indicate that some may be suitable for canine tissue on your website. could you let me know which of the 10 antibodies is the most suitable for canine.
   • We have unfortuantely not tested any of our products in canine samples. If you would like to try one of our product with canine samples, you would qualify for our Innovator's Reward Program. In exchange for a review of our product in an untested application or species, we would issue you a credit voucher for the purchase price. If you would like us to check the homology of a certain product against the canine sequence, just contact our technical support department at technical@novusbio.com.

Bioinformatics

• Uniprot:
  • P35555()