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Human CellExp SPAM1, human recombinant protein

SPAM1, PH-20, HYAL3, HYA1, HYAL1, HYAL5, SPAG15

     
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Product info
Primary Accession P38567
Calculated MW This protein is fused with 6×His tag at the C-terminus, has a calculated MW of 52.1 kDa. The predicted N-terminus is Leu 36. DTT-reduced Protein migrates as 64-66 kDa due to glycosylation.
Additional Info
Gene ID 6677
Gene Symbol SPAM1
Other Names SPAM1, PH-20, HYAL3, HYA1, HYAL1, HYAL5, SPAG15
Gene Source Human
Source HEK 293 cells
Assay&Purity SDS-PAGE; ≥92%
Assay2&Purity2 HPLC;
Recombinant Yes
Target/Specificity SPAM1
Application Notes Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
Format Lyophilized powder
Storage -20°C; Lyophilized from 0.22 µm filtered solution in 50 mM Tris, 100 mM NaCl, pH 7.0-7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Citations (0)
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Background

Hyaluronidase PH-20 also known as Sperm adhesion molecule 1 (SPAM1) and Sperm surface protein PH-20, which belongs to the glycosyl hydrolase 56 family, SPAM1 / PH-20 is expressed in testis. SPAM-1 / PH20 random hydrolysis of (1->4)-linkages between N – acetyl – beta – D – glucosamine and D-glucuronate residues in hyaluronate. SPAM-1 / PH20 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. SPAM1 aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.

References

Lin Y.,et al.Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993).
Gmachl M.,et al.FEBS Lett. 336:545-548(1993).
Jones M.H.,et al.Genomics 29:796-800(1995).
Hillier L.W.,et al.Nature 424:157-164(2003).
Scherer S.W.,et al.Science 300:767-772(2003).

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Discontinued
Cat# PBV10877r-10
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