MCT4/SLC16A3 Antibody [D23C24] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Usage Information

Dilution
WB1:1000 IHC1:100 IF1:100 FCM1:500

Application
WB, IHC, IF, FCM

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
49 kDa 20-250 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
MCT4/SLC16A3 Antibody [D23C24] detects endogenous levels of total MCT4/SLC16A3 protein.

Clone
D23C24

Synonym(s)
CD365, Kim1, Tim1, Timd1, Havcr1, Hepatitis A virus cellular receptor 1 homolog, HAVcr-1, Kidney injury molecule 1, T-cell immunoglobulin mucin receptor 1, KIM-1, TIMD-1, TIM-1

Background
MCT4 (SLC16A3) is a proton‑coupled monocarboxylate transporter of the SLC16 family that mediates efflux of lactate and other glycolytic monocarboxylates from metabolically active cells with high glycolytic rates. It is an integral plasma membrane protein with multiple transmembrane segments that requires the accessory glycoprotein CD147/Basigin for proper folding, trafficking, and surface stability, so functional MCT4 resides predominantly in CD147‑containing complexes. Its transport cycle couples outward movement of lactate anions to inward movement of protons, a mechanism that lowers cytosolic lactate and helps preserve intracellular pH while contributing to acidification of the pericellular space. In skeletal muscle, immune cells, and many solid tumors, MCT4 expression increases in parallel with glycolytic flux and hypoxia‑inducible factor‑1α activity, and high SLC16A3 transcript and protein levels align with transcriptional signatures of glycolysis, hypoxia response, and angiogenesis. In tumor tissue, MCT4‑dependent lactate export supports maintenance of an acidic microenvironment that favors matrix remodeling, stabilizes HIF‑1α, and promotes expression of pro‑angiogenic and pro‑inflammatory mediators such as IL‑8, linking transporter activity to vascular changes and inflammatory tone. High MCT4 expression correlates with increased infiltration of immunosuppressive lymphocyte populations, elevated expression of immune checkpoint molecules, and reduced overall survival across several cancer types, indicating that SLC16A3 status marks an immunometabolic state associated with immune evasion and poor prognosis. Co‑localization of MCT4 with CD147 and matrix metalloproteinase‑14 at invadopodia and other invasive structures connects lactate export to localized extracellular matrix degradation and cell migration, and experimental reduction of MCT4 expression decreases invasive behavior and enhances sensitivity to effector lymphocyte‑mediated cytotoxicity.

Background

MCT4 (SLC16A3) is a proton‑coupled monocarboxylate transporter of the SLC16 family that mediates efflux of lactate and other glycolytic monocarboxylates from metabolically active cells with high glycolytic rates. It is an integral plasma membrane protein with multiple transmembrane segments that requires the accessory glycoprotein CD147/Basigin for proper folding, trafficking, and surface stability, so functional MCT4 resides predominantly in CD147‑containing complexes. Its transport cycle couples outward movement of lactate anions to inward movement of protons, a mechanism that lowers cytosolic lactate and helps preserve intracellular pH while contributing to acidification of the pericellular space. In skeletal muscle, immune cells, and many solid tumors, MCT4 expression increases in parallel with glycolytic flux and hypoxia‑inducible factor‑1α activity, and high SLC16A3 transcript and protein levels align with transcriptional signatures of glycolysis, hypoxia response, and angiogenesis. In tumor tissue, MCT4‑dependent lactate export supports maintenance of an acidic microenvironment that favors matrix remodeling, stabilizes HIF‑1α, and promotes expression of pro‑angiogenic and pro‑inflammatory mediators such as IL‑8, linking transporter activity to vascular changes and inflammatory tone. High MCT4 expression correlates with increased infiltration of immunosuppressive lymphocyte populations, elevated expression of immune checkpoint molecules, and reduced overall survival across several cancer types, indicating that SLC16A3 status marks an immunometabolic state associated with immune evasion and poor prognosis. Co‑localization of MCT4 with CD147 and matrix metalloproteinase‑14 at invadopodia and other invasive structures connects lactate export to localized extracellular matrix degradation and cell migration, and experimental reduction of MCT4 expression decreases invasive behavior and enhances sensitivity to effector lymphocyte‑mediated cytotoxicity.

References
https://pubmed.ncbi.nlm.nih.gov/35509603/ https://pubmed.ncbi.nlm.nih.gov/40927315/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%