Recombinant Mouse CTRP9/C1qTNF9 His-tag Protein, CF

When Recombinant Mouse CTRP9/C1qTNF9 (Catalog # 2132-TN) is coated at 0.5 μg/mL, 100 μL/well, Biotinylated Recombinant Human CL-K1/COLEC11 binds with an ED50 of 15-90 ng/mL.

2 μg/lane of Recombinant Mouse CTRP9/C1qTNF9 was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 39-43 kDa and 39-43 & 80-90 kDa, respectively.

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

Recombinant Mouse CTRP9/C1qTNF9 His-tag Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse CTRP9/C1qTNF9 is immobilized at 0.5 µg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human CL-K1/COLEC11 that produces 50% of the optimal binding response is 15-90 ng/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse CTRP9/C1qTNF9 protein
  

  Mouse C1qTNF9 (Gln20-Ser333) Accession # Q4ZJN1	HPGGGSGGGSGGGS	HHHHHH
  N-terminus		C-terminus

• Accession #: Q4ZJN1
• N-terminal Sequence: No results obtained. Gln20 inferred from enzymatic pyroglutamate treatment revealing Asp21.
• 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: 34 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: 39-43 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 with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in water.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse CTRP9/C1qTNF9 His-tag Protein, CF

• AQL1
• C1q and tumor necrosis factor related protein 9
• C1qTNF9
• C1QTNF9AComplement C1q tumor necrosis factor-related protein 9
• complement C1q tumor necrosis factor-related protein 9A
• CTRP9
• MGC48915

Background

C1qTNF9, also known as CTRP9, is an approximately 40 kDa member of the C1q and TNF-related protein family (1). Like all members of this protein family, C1qTNF9 consists of a short variable region, a collagenous domain that can be hydroxylated, and a C1q-like globular domain (1). Mouse C1qTNF9 shares 86% and 98% amino acid sequence identity with the human and rat orthologs, respectively. Both the mouse and human C1qTNF9 proteins are expressed mostly in adipose tissue, but the mouse protein has also been detected in the heart, lung, muscle, kidney, testis, lymph node, smooth muscle, prostate, thymus, and uterus (1, 2). C1qTNF9 has been shown to be secreted as trimers and higher order multimers and also to form hetero-oligomers with Adiponectin (1, 2). Mouse C1qTNF9 can stimulate the phosphorylation of AMPK, Akt, and eNOS (1, 3, 4). Also in mice, C1qTNF9 may have an important role in cardiac and metabolic health. Its expression has a cardioprotective effect following acute myocardial infarction that may be dependent on AMPK activation (4-6). Additionally, transgenic mice overexpressing C1qTNF9 are resistant to high fat diet‑induced obesity (7). This metabolic role may be conserved, since C1qTNF9 serum levels have been shown to inversely correlate with metabolic syndrome in humans (8).

1. Wong, G.W. et al. (2009) FASEB J. 23:241.
2. Peterson, J.M. et al. (2009) Biochem. Biophys. Res. Commun. 388:360.
3. Zheng, Q. et al. (2011) Arterioscler. Thromb. Vasc. Biol. 31:2616.
4. Kambara, T. et al. (2012) J. Biol. Chem. 287:18965.
5. Su, H. et al. (2013) Basic Res. Cardiol. 108:315.
6. Sun, Y. et al. (2013) Circulation 128:S113.
7. Peterson, J.M. et al. (2013) Am. J. Physiol. Regul. Integr. Comp. Physiol. 305: R522.
8. Hwang, Y.C. et al. (2014) Int. J. Obes. (Lond) 38:1207

Bioinformatics

• Uniprot:
  • Q4ZJN1()