Recombinant human SPAM1 protein is a Human Fragment protein, in the 36 to 482 aa range, expressed in HEK 293, with >92% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes DTT-reduced Protein migrates as 64-66 kDa due to glycosylation. |
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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.
HYAL3, PH20, SPAM1, Hyaluronidase PH-20, Hyal-PH20, Hyaluronoglucosaminidase PH-20, Sperm adhesion molecule 1, Sperm surface protein PH-20
Recombinant human SPAM1 protein is a Human Fragment protein, in the 36 to 482 aa range, expressed in HEK 293, with >92% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
pH: 7.4
Constituents: 5% Trehalose, 0.61% Tris, 0.58% Sodium chloride
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.
Belongs to the glycosyl hydrolase 56 family.
N-glycosylated.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This product was previously labelled as Hyaluronidase PH20. The protein migrates as 64-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
SPAM1 also known as sperm adhesion molecule 1 or PH-20 refers to a glycoprotein found on the sperm cell surface. Its molecular mass is approximately 64 kDa. This protein is primarily expressed in the testes and epididymis where it plays a role in sperm maturation. SPAM1 possesses hyaluronidase activity breaking down hyaluronic acid present in the cumulus cell matrix of the female reproductive tract during fertilization. It aids sperm in penetrating the egg's outer layers which is important for successful fertilization.
SPAM1 participates in sperm penetration through the zona pellucida an essential step in fertilization. It acts independently facilitating sperm passage by degrading surrounding extracellular matrices. SPAM1 while not part of a larger protein complex interacts directly with the female reproductive tract's biochemical structures. These interactions ensure an efficient sperm-vs-egg recognition process that aids in sperm-egg fusion. Its enzymatic activity is central to this sperm-egg binding and membrane fusion.
SPAM1 contributes significantly to the fertilization pathway specifically the Acrosome Reaction. It interacts indirectly with proteins like ZP3 a zona pellucida protein that triggers the acrosome reaction necessary for sperm to penetrate the ovum. Additionally SPAM1 plays a minor role in the hyaluronan-mediated motility pathway interacting faintly with the extracellular matrix components to enhance sperm motility and penetration.
SPAM1 has been implicated in certain infertility cases particularly those involving the failure of sperm to penetrate the egg successfully. This condition might relate to defects or alterations in SPAM1 activity or expression. Moreover some studies suggest a possible link between SPAM1 and testicular cancer where aberrant expression could influence tumorigenesis. SPAM1 anomalies may associate with other proteins like EZH2 involved in various cancers suggesting broader functional implications beyond reproductive biology.
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SDS-PAGE analysis of reduced ab174000 stained overnight with Coomassie Blue.
DTT-reduced Protein migrates as 64-66 kDa due to glycosylation.
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