Recombinant Human SCG3 His-tag Protein, CF

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When Recombinant Human SCG3 His-tag (10374-SC) is immobilized at 1 μg/mL (100 μL/well), Recombinant Human Chromogranin A His-tag (10422-CH) binds with an ED50 of 50-400 ng/mL.
2 μg/lane of Recombinant Human SCG3 His-tag (Catalog # 10374-SC) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at kDa.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human SCG3 His-tag Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human SCG3 His-tag (Catalog # 10374-SC) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human Chromogranin A His-tag  (Catalog # 10422-CH) binds with an ED50 of 50-400 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human SCG3 protein
Phe20-Leu468, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Phe20
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
52 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
50-70 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.
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 SCG3 His-tag Protein, CF

  • SCG3
  • Secretogranin III
  • secretogranin IIIFLJ90833
  • Secretogranin-3
  • SGIII

Background

Secretogranin III, also known as SCG3, is a member of the chromogranin-secretogranin family of neuroendocrine secretory proteins, collectively referred to as granins (1). Additional members of this family include secretogranin II, IV, and V, chromogranin A and B, and a few additional related proteins (1, 2). SCG3 is synthesized as an N-glycosylated protein and two isoforms can be generated from alternative splicing (2). Mature SCG3 contains three functional regions: an N‑terminal cholesterol-binding domain, a chromogranin A binding domain and a C-terminal carboxypeptidase E binding domain (3). Human SCG3 shares 88% and 87% amino acid sequence identity with mouse and rat SCG3, respectively. Granins are highly acidic proteins that are a major component of secretory granules of endocrine, neuroendocrine, and neuronal cells (4-6). Calcium binding at low pH and intermolecular aggregation plays a role in granins' sorting of secretory proteins at the trans-Golgi network (3-6). Within the trans-Golgi network, SCG3 binds to chromogranin A (CgA), membrane-associated carboxypeptidase E (CPE), and cholesterol‑rich membrane domain (3-5). SCG3 has been implicated in diabetic retinopathy (DR) and retinopathy of prematurity (ROP) as a disease-associated endothelial ligand, thus suggesting SCG3 is a promising target for novel antiangiogenic therapy of DR and ROP (7, 8).
  1. Peinado, J. R. et al. (2006) Endocrinology. 147:1408.
  2. Bartolomucci, A. et al. (2011) Endocr. Rev. 32:755.
  3. Hosaka M. et al. (2010) Endocr. J. 57:275.
  4. Sun, M. et al. (2013) Traffic. 14:205.
  5. Hosaka, M. et al. (2004) J. Biol. Chem. 279:3627.
  6. Hosaka, M. et al. (2005) J. Cell Sci. 118:4785.
  7. LeBlanc, M. E. et al. (2017) J. Exp. Med. 214:1029.
  8. Tang, F. et al. (2017) Biochem. Biophys. Res. Commun. 495:781.

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