Recombinant Mouse Slit1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse Slit1 Protein, CF Summary

Details of Functionality
Measured by its ability to enhance neurite outgrowth of dissociated E13 chick embryonic dorsal root ganglia (DRG) neurons. Able to significantly enhance neurite outgrowth when immobilized as a 3 μL droplet containing 90 ng on a nitrocellulose-coated microplate.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse Slit1 protein
Cys34-Glu900, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Cys34
Protein/Peptide Type
Recombinant Proteins
Purity
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
97.6 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
110 kDa, under reducing conditions
Publications
Read Publications using
5199-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 MOPS and NaCl.
Purity
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse Slit1 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). Mouse Slit1 shares 99, 96, 89, 87 and 80% aa identity with rat, human, canine, Xenopus and zebrafish Slit1, respectively, within the LRR domains. Mouse Slits 1, 2 and 3 share 68 - 74% aa identity within the LRR domains. 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.

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Publications for Slit1 (5199-SL)(4)

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