SLC1A5 Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [PSH07-74] (HA751186)

UNIPROT #

Q15758

PROTEIN NAME

SLC1A5

SYNONYMS

ASCT2 antibody;AAAT antibody;AAAT_HUMAN antibody;ATB(0) antibody;ATBO antibody;Baboon M7 virus receptor antibody;FLJ31068 antibody;M7V1 antibody;M7VS1 antibody;Neutral amino acid transporter B(0) antibody;R16 antibody;RD114/simian type D retrovirus receptor antibody;RDR antibody;RDRC antibody;SLC1A5 antibody;Sodium dependent neutral amino acid transporter type 2 antibody;Sodium-dependent neutral amino acid transporter type 2 antibody;Solute carrier family 1 (neutral amino acid transporter), member 5 antibody;Solute carrier family 1 member 5 antibody

SUBCELLULAR LOCATION

Cell membrane, Melanosome.

FUNCTION

Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion. The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation. The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system. Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons. Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development.