Recombinant Human PDILT protein is a Human Full Length protein, in the 21 to 584 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application HPLC | Reactivity Reacts | Dilution info - | Notes - |
Probable redox-inactive chaperone involved in spermatogenesis.
Protein disulfide-isomerase-like protein of the testis, PDILT
Recombinant Human PDILT protein is a Human Full Length protein, in the 21 to 584 aa range, expressed in HEK 293, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.88% Sodium chloride, 0.32% Tris HCl
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. ab152027 is 0.2 µM filtered.
Probable redox-inactive chaperone involved in spermatogenesis.
Belongs to the protein disulfide isomerase family.
N-glycosylated.
PDILT also known as Protein Disulfide Isomerase-Like Testis Expressed is a member of the protein disulfide isomerase (PDI) family. This protein has a molecular mass of approximately 70 kDa and a unique structure. PDILT lacks one of the two active CGHC motifs usually seen in this family while it possesses the ER-retention signal KDEL. This protein is expressed mainly in the testis with a strong association to male germ cells. Its expression links to the endoplasmic reticulum suggesting a role in protein folding and quality control.
PDILT plays an essential role in ensuring proper sperm development. Although it is not formally part of a larger protein complex it interacts with other proteins in the testis to facilitate the assembly of protein disulfide bonds. These interactions ensure the correct formation of complex disulfide-bonded proteins which are necessary for sperm structure and function. PDILT is involved in managing oxidative stress within the cells during the process of spermatogenesis.
PDILT plays an important part in the oxidative protein folding pathway within the endoplasmic reticulum. This pathway is critical for forming disulfide bonds in proteins a process important for their stability and function. PDILT has connections with proteins like Calnexin an important component of the quality control pathway in the ER. Its functional synergy with other PDI family members highlights its role in maintaining the balance of protein homeostasis during reproduction.
PDILT has shown links to male infertility particularly regarding improper sperm motility or structure. Its malfunction can lead to a disruption in the formation of sperm disulfide bonds resulting in structural abnormalities. This dysfunction associates with other proteins like Calreticulin which is also involved in proper protein folding. Current research continues to investigate PDILT's broader implications in fertility emphasizing its significance in maintaining reproductive health.
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