protein

MMP-10 Protein, Human (P. pastoris, His)

HY-P700571

20 μg;50 μg;100 μg

125;240;380 USD

MMP-10 Protein, Human (P. pastoris, His)

proteins

P. pastoris

20 μg;50 μg;100 μg

125;240;380 USD

MMP-10 protein is a member of the matrix metalloproteinase family and plays a crucial role in extracellular matrix remodeling by promoting the degradation of various substrates. As a protease, MMP-10 is involved in tissue homeostasis, wound healing, and inflammatory responses. MMP-10 Protein, Human (P. pastoris, His) is the recombinant human-derived MMP-10 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of MMP-10 Protein, Human (P. pastoris, His) is 378 a.a., with molecular weight of 45 kDa.

Human

TSPO, initially characterized as the peripheral-type benzodiazepine receptor, exhibits the ability to bind protoporphyrin IX, suggesting a potential role in porphyrin and heme transport. Beyond benzodiazepines, TSPO can also bind isoquinoline carboxamides. Its involvement in cholesterol transport across mitochondrial membranes and potential contributions to lipid metabolism have been documented, although its precise physiological role remains a subject of debate. While some reports suggest it is dispensable for steroid hormone biosynthesis, indicating controversy in its functional implications, TSPO interacts with proteins such as TSPOAP1, MOST-1, and may also engage with STAR, highlighting its versatile molecular interactions.

EC 3.4.24; EC 3.4.24.22; matrix metallopeptidase 10 (stromelysin 2); matrix metalloprotease 10; matrix metalloproteinase 10 (stromelysin 2); Matrix metalloproteinase-10; MMP10; MMP-10; SL-2; STMY2stromelysin-2; Stromelysin 2; transin 2; transin-2

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.

Room temperature in continental US; may vary elsewhere.