Recombinant Human C1qTNF1 Protein, CF

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WhenRecombinant Human BAI3 is coated at 4 µg/mL, Recombinant Human C1qTNF1 (Catalog #9268-TN) binds with an ED50 of 0.6-3.6 µg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human C1qTNF1 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human BAI3 is coated at 4 µg/mL, Recombinant Human C1qTNF1 (Catalog # 9268-TN) binds with an
ED50 = 0.6-3.6 µg/mL.
Source
Mouse myeloma cell line, NS0-derived human CTRP1/C1qTNF1 protein
Arg26-Pro281, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Arg26
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
30 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
33-41 kDa, 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 HEPES and NaCl.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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 C1qTNF1 Protein, CF

  • C1q and tumor necrosis factor related protein 1
  • C1qTNF1
  • CTRP1
  • CTRP1G protein-coupled receptor-interacting protein
  • FLJ90694
  • G protein coupled receptor interacting protein
  • GIPcomplement C1q tumor necrosis factor-related protein 1
  • ZSIG37

Background

C1qTNF1 (CTRP1) is an approximately 35 kDa member of the C1q family of secreted proteins and plays a role in energy metabolism and inflammation (1, 2). C1qTNF1 contains a collagen-like region and one C1q-like domain (3). Mature human C1qTNF1 shares 80% aa sequence identity with mouse and rat C1qTNF1. Circulating levels of C1qTNF1 are elevated in obesity, hypertension, and diabetes but can be decreased in the serum of diet-induced obese mice (4-6). C1qTNF1 expression is up-regulated in atherosclerotic plaques or adipose tissue by oxidized LDL or inflammatory cytokines (3, 7, 8). In turn, it induces the expression of inflammatory cytokines (7, 9) and the up-reglation of adhesion proteins on vascular endothelial cells (8). Systemically administered C1qTNF1, in contrast, can limit tissue damage following myocardial infarction (9). In skeletal muscle, C1qTNF1 promotes fatty acid oxidation, energy expenditure, insulin sensitivity, and glucose uptake and glycolysis (6, 10). It also induces the proliferation of immature chondrocytes (11) and aldosterone synthesis in the adrenal cortex (4). R&D Systems in-house testing indicates that C1qTNF1 binds to BAI3, consistent with the reported interactions between BAI3 and C1qL proteins (12).
  1. Grebrehiwet, B. et al. (2012) Front. Immunol. 5:3.
  2. Seldin, M.M. et al. (2014) Rev. Endocr. Metab. Disord. 15:111.
  3. Kim, K.-Y. et al. (2006) FEBS Lett. 580:3953.
  4. Jeon, J.H. et al. (2008) FASEB J. 22:1502.
  5. Xin, Y. et al. (2014) Endocr. J. 61:841.
  6. Peterson, J. M. et al. (2012) J. Biol. Chem. 287:1576.
  7. Wang, X.Q. et al. (2016) Atherosclerosis 250:38.
  8. Lu, L. et al. (2016) Eur. Heart J. 37:1762.
  9. Yuasa, D. et al. (2016) FASEB J. 30:1065.
  10. Han, S. et al. (2016) J. Nutr. Biochem. 27:43.
  11. Akiyama, H. et al. (2013) Mol. Cell. Endocrinol. 369:63.
  12. Bolliger, M.F. et al. (2011) Proc. Natl. Acad. Sci. USA 108:2534.

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