| Host: | HEK293 |
| Note: | STRICTLY FOR FURTHER RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
| Short Description : | Recombinant-Human SPAM1 (PH-20)-protein was developed from hek293. For use in research applications. |
| Conjugation: | Unconjugated |
| Formulation: | Lyophilised from 0.2 Mu m filtered PBS solution, pH7.2, 5% Trehalose. |
| Dilution Range: | Spin the vial and reconstite in distilled water to a concentration not less than 0.1 mg/mL. This can then be diluted into other buffers. |
| Storage Instruction: | Can be stored in working aliquots at 2°C-8°C C for one month, or at-20°C to-70°C for 1 year. Avoid repeated freeze/thaw cycles. NA |
| Endotoxin: | Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg (1EU/µg). NA |
| Gene Symbol: | SPAM1 |
| Gene ID: | 6677 |
| Uniprot ID: | HYALP_HUMAN |
| Immunogen Region: | ECD |
| Immunogen: | Optimized DNA sequence encoding extracellular domain of human SPAM1 (PH20) (LEU36-TYR482 ) including a C-terminal His tag was expressed in HEK293 cells. NA |
| Tissue Specificity | Testis. |
| Post Translational Modifications | N-glycosylated. |
| Function | Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid. |
| Protein Name | Hyaluronidase Ph-20Hyal-Ph20Hyaluronoglucosaminidase Ph-20Sperm Adhesion Molecule 1Sperm Surface Protein Ph-20 |
| Database Links | Reactome: R-HSA-2534343 |
| Cellular Localisation | Cell MembraneLipid-AnchorGpi-Anchor |
| Alternative Protein Names | Hyaluronidase Ph-20 proteinHyal-Ph20 proteinHyaluronoglucosaminidase Ph-20 proteinSperm Adhesion Molecule 1 proteinSperm Surface Protein Ph-20 proteinSPAM1 proteinHYAL3 proteinPH20 protein |
Information sourced from Uniprot.org