Recombinant Human Slit2 (aa1122-1529) Protein, CF

Recombinant Human Slit2 (Catalog # 9379‑SL) Induces Cortical Neurite Outgrowth. A) Untreated E16-E18 embryonic rat cortical neurons. B) Neurite outgrowth in E16-E18 embryonic rat cortical neurons treated with 625 ng/mL of Recombinant Human Slit2.

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

Recombinant Human Slit2 (aa1122-1529) Protein, CF Summary

• Details of Functionality: Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Human Slit2, immobilized at 625 ng/ml on a 96-well plate, is able to significantly enhance neurite outgrowth.
• Source: Human embryonic kidney cell, HEK293-derived human Slit2 protein
  Thr1122-Ser1529, with a C-terminal 6-His tag
• Accession #: O94813-1
• N-terminal Sequence: Thr1122
• 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: 45 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: 53-64 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 MOPS and NaCl.
• 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 Slit2 (aa1122-1529) Protein, CF

• FLJ14420
• SLIL3
• slit (Drosophila) homolog 2
• slit homolog 2 (Drosophila)
• slit homolog 2 protein
• Slit2
• Slit-2SLIL3

Background

Slit Homolog 2 (Slit2) is a member of the Slit family of secreted extracellular matrix glycoproteins that are best known for their role in axon guidance (1). It is widely expressed in the developing and adult brain and spinal cord, as well as in fetal lung and kidney, and the adult adrenal gland, thyroid gland, and trachea (1-3). Slit2 is composed of multiple domains including seven EGF-like domains, twenty Leucine-rich repeats (LRRs), one Laminin G-like domain, one C-terminal cysteine knot-like (CTCK) domain, and four N-terminal and four C-terminal LRR domains (1, 3). Slit2 has a molecular weight of approximately 200 kDa (4). However, proteolytic cleavage between the fifth and sixth EGF-like domains produces a membrane-bound 140 kDa N-terminal protein, termed Slit2-N, and a 55-60 kDa C-terminal fragment, termed Slit2-C (4, 5). Mature human Slit2 shares 96% amino acid sequence identity with the mouse and rat orthologs. Slit2 has been shown to have various important functions in the nervous system. Slit2 induces growth cone collapse, inhibits oligodendrocyte precursor cell migration, and promotes axon elongation, branch formation, and fasciculation (5-9). Slit2 C-terminal fragment can mediate axon guidance through binding to Plexin A1 receptor (10). Slit2-C has also been shown to bind to Glypican-1 and promote motor axon migration (5). Outside the nervous system, C-terminal fragment of Slit2 activates a thermogenic PKA pathway in adipocytes and improves glucose homeostasis (11).

1. Ypsilanti, A.R. et al. (2010) Development 137:1939.
2. Itoh, A. et al. (1998) Brain Res. Mol. Brain Res. 62:175.
3. Holmes, G.P. et al. (1998) Mech. Dev. 79:57.
4. Chédotal, A. (2007) Adv. Exp. Med. Biol. 621:65.
5. Nguyen Ba-Charvet, K.T. et al. (2001) J. Neurosci. 21:4281.
6. Wang, K.H. et al. (1999) Cell 96:771.
7. Wong, E.V. et al. (2004) J. Neurobiol. 59:66.
8. Liu, X. et al. (2012) J. Biol. Chem. 287:17503.
9. Jaworski, A. and Tessier-Lavigne, M. (2012) Nat. Neurosci. 15:367.
10. Delloye-Bourgeois, C. et.al. (2014) Nat. Neurosci. 18(1):36.
11. Svensson, K.J. et al. (2016) Cell Metabolism. 23:1.

Bioinformatics

• Uniprot:
  • O94813-1()