NSJ Bioreagents
SKU:FY13139
TIMM10 Antibody / TIM10 / Mitochondrial import inner membrane translocase subunit Tim10, 100 ug
TIMM10 Antibody / TIM10 / Mitochondrial import inner membrane translocase subunit Tim10, 100 ug
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TIMM10 antibody detects Mitochondrial import inner membrane translocase subunit Tim10, a small chaperone protein essential for protein transport across the mitochondrial inner membrane. The UniProt recommended name is Mitochondrial import inner membrane translocase subunit Tim10 (TIMM10). Also known as Tim10, this protein is a central component of the TIM22 complex, which imports and assembles metabolite carrier proteins into the inner membrane.
Functionally, TIMM10 antibody identifies a 103-amino-acid protein residing in the mitochondrial intermembrane space. TIMM10 forms a hexameric complex with TIMM9 to guide hydrophobic precursor proteins through the aqueous intermembrane environment to the TIM22 translocase. This chaperone-mediated import system maintains mitochondrial protein homeostasis and bioenergetic function.
The TIMM10 gene is located on chromosome 11q13.1 and is expressed in energy-demanding tissues such as heart, brain, and skeletal muscle. TIMM10 ensures proper import of metabolite carriers, including the ADP/ATP translocase and phosphate carrier, which are critical for mitochondrial metabolism.
Pathologically, defects in TIMM10 or its partner subunits lead to mitochondrial protein import deficiencies and oxidative phosphorylation defects. Impaired TIMM10 function can contribute to neurodegenerative and metabolic diseases. Research using TIMM10 antibody supports studies in mitochondrial biology, protein import, and bioenergetics.
TIMM10 antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect mitochondrial translocase components. NSJ Bioreagents provides TIMM10 antibody reagents optimized for mitochondrial function, energy metabolism, and protein transport research.
Structurally, Mitochondrial import inner membrane translocase subunit Tim10 adopts a twin CX3C motif stabilized by disulfide bonds, forming a compact structure for substrate chaperoning. This antibody enables investigation of TIMM10's role in mitochondrial protein import and inner membrane assembly.
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