Recombinant Human KAL1 Protein, CF

When Recombinant Human FGF basic 146 aa (Catalog # 233-FB) is coated at 1.5 µg/mL, Recombinant Human KAL1 (Catalog # 9314-KA) binds with an ED50 of 8-48 ng/mL.

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

Recombinant Human KAL1 Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human FGF basic 146 aa Recombinant Human FGF basic 146 aa (Catalog # 233-FB) is coated at 1.5 µg/mL, 100 μL/well, Recombinant Human KAL1 binds with an ED₅₀ of 8-48 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human KAL1 protein
  Ala25-Tyr680, with a C-terminal 6-His tag
• Accession #: EAW98759
• N-terminal Sequence: Ala25
• 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: 75 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: 84-103 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 PBS and NaCl with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 200 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 KAL1 Protein, CF

• Adhesion molecule-like X-linked
• ADMLX
• ADMLXHHA
• ANOS1
• Anosmin 1
• anosmin-1
• HH1
• HHA
• KAL
• KAL1
• KALIG1
• KALIG-1
• Kallmann syndrome 1 sequence
• Kallmann syndrome interval gene 1
• Kallmann syndrome protein
• Kallmann syndrome-1 sequence (anosmin-1)
• KMS

Background

Anosmin-1, also known as Kal-1, is a 100 kDa secreted glycoprotein that regulates neuronal adhesion and migration. Mutations in Anosmin-1 are associated with the development of X-linked Kallman syndrome which can be accompanied by hearing loss (1). Mature human Anosmin-1 contains one WAP domain and four Fibronectin type-III domains (2). It is expressed by cerebellar Purkinje cells and deep nuclear neurons (2, 3), piriform cortex and olfactory bulb mitral cells (2, 4), optic tectum and retinal ganglion axons (2, 5, 6), and oligodendrocyte progenitor cells (OPC) (4). Anosmin-1 binds to Integrin beta 1/CD29, FGF R1, L1CAM, and complexes of FGF R1 with FGF basic and heparan sulfate proteoglycans, and it enhances signaling through FGF R1 (6-9). It mediates OPC adhesion, inhibits FGF basic-induced OPC migration, and enhances oligodendrocyte-mediated axon myelination (5, 6, 10, 11). It also cooperates with FGF basic to promote olfactory axon elongation and neurite outgrowth (3, 4, 8, 9, 12, 13). In addition, Anosmin-1 is up-regulated in glioblastoma and gastric cancer where it enhances tumor cell proliferation and migration (7, 14).

1. Korsensky, L. and D. Ron (2016) Semin. Cell Dev. Biol. 53:101.
2. Soussi-Yanicostas, N. et al. (1996) J. Cell Sci. 109:1749.
3. Gianola, S. et al. (2009) Neuroscience 158:570.
4. Soussi-Yanicostas, N. et al. (2002) Cell 109:217.
5. Bribian, A. et al. (2008) Dev. Neurobiol. 68:1503.
6. Bribian, A. et al. (2006) Mol. Cell. Neurosci. 33:2.
7. Choy, C.T. et al. (2013) Endocr. Relat. Cancer 21:85.
8. Diaz-Balzac, C.A. et al. (2015) Cell Rep. 11:1377.
9. Gonzalez-Martinez, D. et al. (2004) J. Neurosci. 24:10384.
10. Clemente, D. et al. (2011) J. Neurosci. 31:14899.
11. Murcia-Belmonte, V. et al. (2016) Brain Struct. Funct. 221:1365.
12. Soussi-Yanicostas, N. et al. (1998) J. Cell Sci. 111:2953.
13. Garcia-Gonzalez, D. et al. (2016) Brain Struct. Funct. 221:239.
14. Kanda, M. et al. (2016) Int. J. Cancer 138:721.

Bioinformatics

• Uniprot:
  • EAW98759()