Sample type Serum, Plasma, Cell Culture Supernatant, Other liquid samples
Components
Break apart microtiter test strips each coated single wells
8 x 12 (96 Total)
Lyophilized Standard
2 x vial
Biotin-labeled Antibody(Concentrated, 100X)
120 uL
HRP-Streptavidin Conjugate(Concentrated, 100X)
120 uL
Washing solution concentrate (25X)
30 mL
Sample Dilution buffer
20 mL
Antibody Dilution buffer
10 mL
Streptavidin Dilution buffer
10 mL
Stopping solution
10 mL
TMB Substrate (ready-to-use)
10 mL
Plate seals
3
Storage Store at 2-8°C.
target relevance
anti-Idactamab antibody Anti-drug antibodies (ADAs) generated in subjects following administration of Idactamab.
Idactamab Idactamab biologic drug binds Homo sapiens SLC1A5 Neutral amino acid transporter B(0)
Homo sapiens SLC1A5 Neutral amino acid transporter B(0)
Protein names Neutral amino acid transporter B(0)
Alternative names Baboon M7 virus receptor, RD114/simian type D retrovirus receptor, Sodium-dependent neutral amino acid transporter type 2, Solute carrier family 1 member 5
Gene names SLC1A5
Protein family Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family. SLC1A5 subfamily
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 (PubMed:17094966, PubMed:23756778, PubMed:26492990, PubMed:29872227, PubMed:34741534, PubMed:8702519, PubMed:39095408, PubMed:27272177). 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 (PubMed:23756778, PubMed:24953180). 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 (PubMed:32733894). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (PubMed:17094966). 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 (PubMed:10708449, PubMed:23492904, PubMed:38671230)
Structure Homotrimer (Probable) (PubMed:29872227, PubMed:38671230, PubMed:39095408). Interacts with secreted ERVH48-1/suppressyn (via RBD domain); this interaction decreases SLC1A5 transport rate and may negatively regulate syncytialization (PubMed:23492904, PubMed:38671230). Interacts with ERVW-1/syncytin (via RBD domain); this interaction decreases SLC1A5 transport rate (PubMed:38671230)
Keywords 3D-structure, Acetylation, Alternative initiation, Alternative splicing, Amino-acid transport, Antiport, Cell membrane, Glycoprotein, Host cell receptor for virus entry, Host-virus interaction, Membrane, Metal-binding, Phosphoprotein, Proteomics identification, Receptor, Reference proteome, Sodium, Transmembrane, Transmembrane helix, Transport
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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from the PubMed database provided by the United States National Library of Medicine at the National Institutes of Health.
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