GLT25D2 Protein, Human (sf9, His)

GLT25D2 Protein, a beta-galactosyltransferase, crucially catalyzes beta-galactose transfer to collagen hydroxylysine residues, influencing collagen's structural diversity and functional properties. This glycosylation modulates collagen's biochemical and biomechanical characteristics, impacting tissue development, maintenance, and repair. Understanding GLT25D2's role enhances comprehension of collagen modification pathways, with potential therapeutic implications for collagen-related disorders. Further exploration promises insights into collagen biology, advancing knowledge and contributing to therapeutic strategy development. GLT25D2 Protein, Human (sf9, His) is the recombinant human-derived GLT25D2 protein, expressed by Sf9 insect cells, with C-His labeled tag. The total length of GLT25D2 Protein, Human (sf9, His) is 622 a.a., with molecular weight of ~68 kDa.

The GLT25D2 Protein functions as a beta-galactosyltransferase, specifically catalyzing the transfer of beta-galactose to hydroxylysine residues within collagen. This enzymatic activity plays a crucial role in the post-translational modification of collagen, contributing to the structural diversity and functional properties of this essential extracellular matrix protein. By facilitating the glycosylation of hydroxylysine, GLT25D2 participates in the modulation of collagen's biochemical and biomechanical characteristics. Understanding the role of GLT25D2 enhances our comprehension of collagen modification pathways, with potential implications in tissue development, maintenance, and repair. Further exploration of GLT25D2's function holds promise for advancing our knowledge of collagen biology and may contribute to the development of therapeutic strategies targeting collagen-related disorders.

Human

Sf9 insect cells

C-His

Q8IYK4 (M1-S622)

23127  [NCBI]

Approximately 68 kDa

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.