Anti-GRIM19/NDUFA13 Antibody Picoband®, PE Conjugate

NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13 is an enzyme that in humans is encoded by the NDUFA13 gene. This gene encodes a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain. The protein is required for complex I assembly and electron transfer activity. The protein binds the signal transducers and activators of transcription 3 (STAT3) transcription factor, and can function as a tumor suppressor. The human protein purified from mitochondria migrates at approximately 16 kDa. Transcripts originating from an upstream promoter and capable of expressing a protein with a longer N-terminus have been found, but their biological validity has not been determined.

Expressed in breast, ductal and invasive ductal carcinomas of the breast, sporadic colorectal adenomas and carcinomas (at protein level). Expressed in fetal brain. Expressed in lung, amygdala, eye, prostate, pancreatic and prostate cancers, head and neck tumors and embryonal tumor.

Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity). Has mainly an anabolic role in energy metabolism. Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins). .

1. Angebault, C., Charif, M., Guegen, N., Piro-Megy, C., Mousson de Camaret, B., Procaccio, V., Guichet, P.-O., Hebrard, M., Manes, G., Leboucq, N., Rivier, F., Hamel, C. P., Lenaers, G., Roubertie, A. Mutation in NDUFA13/GRIM19 leads to early onset hypotonia, dyskinesia and sensorial deficiencies, and mitochondrial complex I instability. Hum. Molec. Genet. 24: 3948-3955, 2015. 2. Angell, J. E., Lindner, D. J., Shapiro, P. S., Hofmann, E. R., Kalvakolanu, D. V. Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-beta and retinoic acid combination, using a genetic approach. J. Biol. Chem. 275: 33416-33426, 2000. 3. Barnich, N., Hisamatsu, T., Aguirre, J. E., Xavier, R., Reinecker, H.-C., Podolsky, D. K. GRIM-19 interacts with nucleotide oligomerization domain 2 and serves as downstream effector of anti-bacterial function in intestinal epithelial cells. J. Biol. Chem. 280: 19021-19026, 2005.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.

Western blot, 0.25-0.5 μg/ml, Mouse, Rat<br> Immunohistochemistry(Paraffin-embedded Section), 2-5 μg/ml, Human<br> Immunocytochemistry/Immunofluorescence, 5 μg/ml, Human<br> Immunofluorescence, 5 μg/ml, Human<br> Flow Cytometry (Fixed), 1-3 μg/1x10⁶ cells, Human<br> ELISA, 0.1-0.5 μg/ml, -<br>

Mitochondrion outer membrane ; Single-pass type III membrane protein . Peroxisome membrane ; Single-pass type III membrane protein . Microsome membrane ; Single-pass type III membrane protein . Endoplasmic reticulum membrane ; Single-pass type III membrane protein .