SLC31A1 Protein, Human (Cell-Free, His-SUMO)

The SLC31A1 protein is an important uniporter that can transport copper(1+) from the extracellular space into the cytoplasm with remarkable specificity and deliver it directly to molecular chaperones such as ATOX1. This process tightly regulates intracellular copper(1+) levels and may be involved in intestinal copper absorption. SLC31A1 Protein, Human (Cell-Free, His-SUMO) is the recombinant human-derived SLC31A1 protein, expressed by E. coli Cell-free , with N-SUMO, N-6*His labeled tag. The total length of SLC31A1 Protein, Human (Cell-Free, His-SUMO) is 190 a.a., the molecular weight are 40 KDa (monomer), 80 KDa (dimer), whiel dimers are generally formed.

SLC31A1, a critical uniporter, orchestrates the transport of copper(1+) from the extracellular space into the cytoplasm, traversing the plasma membrane. This transport is facilitated with remarkable specificity, as SLC31A1 directly delivers copper(1+) to specialized chaperones like ATOX1 through a copper(1+)-mediated transient interaction within its C-terminal domain. This intricate process serves as a regulatory mechanism, tightly controlling intracellular copper(1+) levels. Beyond its canonical role, SLC31A1 exhibits versatility by potentially participating in copper(1+) import from the apical membrane, suggesting a role in intestinal copper absorption. The transport mechanism is sodium-independent, highly-affinity driven, and saturable. Furthermore, SLC31A1 mediates the uptake of silver(1+), and its involvement in the influx of platinum-containing chemotherapeutic agents suggests a potential impact on therapeutic responses. In vitro studies demonstrate SLC31A1's ability to transport cadmium(2+) into cells. Remarkably, SLC31A1 acts not only as a copper transporter but also as a redox sensor, promoting angiogenesis in endothelial cells by transmitting VEGF-induced ROS signals. This process involves sulfenylation at Cys-189, leading to disulfide bond formation between SLC31A1 and KDR, facilitating sustained VEGFR2 signaling. The SLC31A1-KDR complex is co-internalized into early endosomes, contributing to prolonged VEGFR2 signaling. Additionally, SLC31A1 mobilizes copper(1+) out of the endosomal compartment, facilitating its availability for export out of cells. These diverse functions underscore the multifaceted nature of SLC31A1 in cellular copper homeostasis and signaling pathways.

Measured by its binding ability in a functional ELISA. Immobilized SLC31A1 at 0.5 μg/well can bind human LGALS8 at7.6293-1000000 ng/mL, the EC₅₀ of human LGALS8 is 14.063-30.957 μg/mL.

Human

E. coli Cell-free

N-SUMO;N-6*His

O15431 (M1-H190)

1317  [NCBI]

MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH

Approximately 40 kDa & 80 kDa.It is speculated that the protein f orms a dimeric structure 80 kDa.

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

Lyophilized powder.

Lyophilized from a 0.2 μm sterile filtered PBS,0.05% Brij-78,6% Trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US;may vary elsewhere.