| Source: |
Escherichia coli |
| Molecular Weight: |
Approximately 19.8 kDa, a single non-glycosylated polypeptide chain containing 176 amino acids. |
| AA Sequence: |
IVIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG |
| Purity: |
> 95% by SDS-PAGE and HPLC analyses. |
| Biological Activity: |
Fully biologically active when compared to standard. The ED50 as determined by inducing alkaline phosphatase production of murine C3H10T1/2 cells is 0.5 - 1.0 μg/mL. |
| Physical Appearance: |
Sterile filtered white lyophilized (freeze-dried) powder. |
| Formulation: |
Lyophilized from a 0.2 μm filtered concentrated solution in PBS, pH7.4. |
| Endotoxin: |
Less than 1 EU/μg of rMuSHH as determined by LAL method. |
| Reconstitution: |
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20°C. Further dilutions should be made in appropriate buffered solutions. |
| Stability & 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. |
| Synonyms: |
SHH, HHG-1 |
| Background: |
Sonic hedgehog (SHH) is part of the hedgehog family of mammalian signaling proteins, alongside desert hedgehog (DHH) and Indian hedgehog (IHH). Among these homologues, SHH plays the most crucial developmental role. It acts as a morphogen that influences the patterning of various systems, such as the limb, midline structures of the brain and spinal cord, the thalamus via the zona limitans intrathalamica, and the development of teeth.
SHH undergoes auto-processing to produce two functional domains: a 20 kDa N-terminal signaling domain (SHH-N) from residues 24 to 197, and a 25 kDa C-terminal domain (residues 198 to 462) which does not have any known signaling function. |
