Recombinant Mouse Slit1 (aa 1126-1531) Protein, CF

2μg/lane of Recombinant Mouse Slit1 was resolved with SDS-PAGEunder reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 60 - 68 kDa.

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

Recombinant Mouse Slit1 (aa 1126-1531) Protein, CF Summary

• Details of Functionality: Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Recombinant Mouse Slit1, immobilized at 1.25-2.5 μg/mL on a 96 well plate, is able to significantly enhance neurite outgrowth.
• Source: Mouse myeloma cell line, NS0-derived mouse Slit1 protein
  Ser1126-Ala1531, with a C-terminal 6-His tag
• Accession #: Q80TR4
• N-terminal Sequence: Ser1126
• 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: 60-68 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °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 Mouse Slit1 (aa 1126-1531) Protein, CF

• KIAA0813
• MEGF4
• MEGF4slit (Drosophila) homolog 1
• MGC164811
• Multiple EGF-like domains protein 4
• Multiple epidermal growth factor-like domains protein 4
• SLIL1
• slit homolog 1 (Drosophila)
• slit homolog 1 protein
• Slit1
• Slit-1slit1
• SLIT3

Background

Slit1 is a member of the Slit family of large secreted axon guidance molecules that are ligands for Robo receptors (1, 2). Like other mammalian family members, the 1531 amino acid (aa), ~200 kDa Slit1 contains a 33 aa signal sequence followed by 23 leucine-rich repeats (LRR, aa 34-900) and 9 EGF-like sequences (aa 930-1451) (2). Mammalian Slits also contain a laminin-G domain between EGF6 and EGF7 (aa 1163-1336), and a C-terminal cysteine-rich domain (cysteine knot; aa 1456-1531) (2). Heparin sulfates are required for interaction of Robo with Slit LRR domains (2, 3). The C-terminal fragment (aa 1126-1531) of mouse Slit 1 shares 96% and 99% aa identity with human and rat respectively. Slit1 and Slit2 (or in some cases Slit3) are expressed in complementary locations during development of the optic and olfactory tracts and the forebrain, and appear to work together to mediate Robo guidance of retinal, olfactory, hippocampal and motor axons (1, 4-9). Deletion of either Slit1 or Slit2 has less effect than deletion of both, which allows axons to wander from tracts and inappropriately cross or recross the midline (4, 5, 7-9). In the injured spinal cord, presence of Slit1 along with Slit3 and Netrin-1 may be responsible for failure of axons to regenerate in the adult CNS (10). Slit1 also promotes dendrite growth and branching of cortical neurons indicating it may exert important influence on the final morphology of cortical neurons (11). Although Slit1 has mainly been found in the fetal and adult brain, it is also detected in the heart and kidney. The C-terminal cysteine knot, which may mediate interaction with other proteins, is absent in the rat brain splicing variant, Slit1 alpha (12).

1. Yuan, W. et al. (1999) Dev. Biol. 212:290.
2. Hohenester, E. (2008) Biochem. Soc. Trans. 36:251.
3. Hussain, S-A. et al. (2006) J. Biol. Chem. 281:39693.
4. Thompson, H. et al. (2006) Dev. Biol. 296:476.
5. Plump, A. S. et al. (2002) Neuron 33:219.
6. Cho, J. H. et al. (2007) J. Neurosci. 27:9094.
7. Nguyen-Ba-Charvet, K. T. et al. (2002) J. Neurosci. 22:5473.
8. Bagri, A. et al. (2002) Neuron 33:233.
9. DiMeglio, T. et al. (2008) J. Neurosci. 28:6285.
10. Wehrle, R. et al. (2005) Eur. J. Neurosci. 22:2134.
11. Whitford, K. L. et al. (2002) Neuron 33:47.
12. Tanno, T. et al. (2004) J. Biochem. 136:575.

Bioinformatics

• Uniprot:
  • Q80TR4()