Recombinant Human Slit2 (aa 26-1118) Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Slit2 (aa 26-1118) Protein, CF Summary

Details of Functionality
Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Mouse Slit2 immobilized at 2.5 μg/mL is able to significantly induce neurite outgrowth.
Source
Human embryonic kidney cell, HEK293-derived human Slit2 protein
Gln26-Val1118, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
No results obtained. Gln26 inferred from enzymatic pyroglutamate treatment revealing Ala27
Structure / Form
Noncovalently-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
SLIT2
Purity
>90%, 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
123 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
120-144 kDa, reducing conditions
Publications
Read Publications using
8616-SL in the following applications:

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, NaCl and Ethylene Glycol.
Purity
>90%, 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 Human Slit2 (aa 26-1118) 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, 20 Leucine-rich repeats (LRRs), one Laminin G-like domain, one C-terminal cysteine knot-like (CTCK) domain, and 4 N-terminal and 4 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 bind to multiple receptors including ROBO-1, -2, -3, and -4, Laminin-1, DAN, Gremlin, and Glypican-1 (1, 6-8). Depending upon the target, Slit2 can promote a number of diverse effects. Slit2 regulates axon guidance by binding to ROBO receptors and initiating axon repulsion (1, 5, 9-12). Slit2 has also been shown to induce growth cone collapse, inhibit oligodendrocyte precursor cell migration, and promote axon elongation, branch formation, and fasciculation (5, 13-16). Additionally, Slit2-N and Slit2-C have been shown to have distinct activities. Slit2-N binds to ROBO-1 and repels motor axon migration, while Slit2-C binds to Glypican-1 and promotes motor axon migration (5). Outside the nervous system, Slit2 plays a role in a wide range of biological processes including cell adhesion and migration, tumor progression and metastasis, angiogenesis, lymphangiogenesis, HIV-1 replication, platelet function and thrombus formation, and stem cell senescence (1, 8, 17-30).

  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. Nguyen-BA-Charvet, K.T. et al. (2001) Mol. Cell. Neurosci. 17:1048.
  7. Hagino, S. et al. (2003) Glia 42:130.
  8. Chen, B. et al. (2004) J. Immunol. 173:5914.
  9. Yuan, W. et al. (1999) Dev. Biol. 212:290.
  10. Erskine, L. et al. (2000) J. Neurosci. 20:4975.
  11. Shu, T. et al. (2003) J. Neurosci. 23:8176.
  12. Kim, M. et al. (2014) Neural Dev. 9:17.
  13. Wang, K.H. et al. (1999) Cell 96:771.
  14. Wong, E.V. et al. (2004) J. Neurobiol. 59:66.
  15. Liu, X. et al. (2012) J. Biol. Chem. 287:17503.
  16. Jaworski, A. and Tessier-Lavigne, M. (2012) Nat. Neurosci. 15:367.
  17. Guan, H. et al. (2003) J. Immunol. 171:6519.
  18. Liu, D. et al. (2006) Circ. Res. 98:480.
  19. Prasad, A. et al. (2007) J. Leukoc. Biol. 82:465.
  20. Tole, S. et al. (2009) J. Leukoc. Biol. 86:1403.
  21. Kim, H.K. et al. (2008) Neoplasia 10:1411.
  22. Prasad, A. et al. (2008) J. Biol. Chem. 283:26624.
  23. Tseng, R.C. et al. (2010) Cancer Res. 70:543.
  24. Alajez, N.M. et al. (2011) Cancer Res. 71:2381.
  25. Zhang, Q.Q. et al. (2015) Oncotarget 6:3123.
  26. Dunaway, C.M. et al. (2011) Mol. Cell. Biol. 31:404.
  27. Yang, X.M. et al. (2010) Biochem. Biophys. Res. Commun. 396:571.
  28. Anand, A.R. et al. (2011) AIDS 25:2105.
  29. Patel, S. et al. (2012) Circulation 126:1385.
  30. Harburg, G. et al. (2014) Stem Cell Reports 3:385.

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Publications for Slit2 (8616-SL)(3)

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Bioinformatics

Gene Symbol SLIT2
Uniprot