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SEMG1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00482

Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.

SEMG1 Protein, Human, Recombinant (His)

SEMG1 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00482
Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.
Pack SizePriceAvailabilityQuantity
10 μg$1297-10 days
50 μg$3907-10 days
500 μg$1,7307-10 days
1 mg$2,7307-10 days
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.
Species
Human
Expression System
HEK293 Cells
TagC-6xHis
Accession NumberAAH07096.1
Synonyms
α-Inhibin-92,α-Inhibin-31,SGI,Seminal Basic Protein,SEMG1,SEMG,Semenogelin-1,Semenogelin I,Alpha-Inhibin-92,Alpha-Inhibin-31
Amino Acid
Gln24-Thr402
Construction
Gln24-Thr402
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight25-55 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM Hac-NaAc, 150 mM NaCl, pH 4.5.
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
Research Background
Semenogelin-1 (SEMG1) is the predominant protein in semen; it is a secretory protein involved in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, each possibly having a separate function. In the proteolysis process, Alpha-inhibin-92 and alpha-inhibin-31 are produced; they inhibit the secretion of pituitary follicle-stimulating hormone. At the same time, it breaks down the gel matrix, allowing the spermatozoa to move more freely.

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