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146281 Rabbit Anti-GPAM (GPAT1, KIAA1560, Glycerol-3-phosphate Acyltransferase 1, Mitochondrial, GPAT-1, MGC26846, RP11-426E5.2)

Specifications
References
Clone Type
Polyclonal
Host
Rabbit
Source
Human
Isotype
IgG
Grade
Affinity Purified
Applications
E IF IHC WB
Crossreactivity
Hu Mo Rt
Shipping Temp
Blue Ice
Storage Temp
-20°C

Glycerol-3-phosphate acyltransferase 1 (GPAT1), one of four known GPAT isoforms, is located on the mitochondrial outer membrane, allowing reciprocal regulation with carnitine palmitoyltransferase-1. It is thought to be critical for the development of hepatic steatosis; steatosis triggered by GPAT1 overexpression leads to hepatic and possibly peripheral insulin resistance. GPAT1 is transcriptionally upregulated by insulin and sterol regulatory element binding protein (SREBP-1) and downregulated by AMP-activated protein kinase. Mice deficient in GPAT1 exhibit decreased triacylglycerol (TAG) in cardiomyocytes even in high-fat diets, suggesting that GPAT1 contributes significantly to TAG accumulation in heart tissue during lipogenic or high fat diets. At least two isoforms of GPAT1 are known to exist.

Applications
Suitable for use in ELISA, Western Blot, Immunofluorescence and Immunohistochemistry. Other applications not tested.
Recommended Dilution
Western Blot: 1-2ug/ml Immunofluorescence: 20ug/ml Immunohistochemistry (Formalin fixed paraffin embedded): 2.5ug/ml Optimal dilutions to be determined by the researcher.
Positive Control
Rat Brain Tissue Lysate
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic peptide corresponding to 15aa from near the C-terminus of human GPAT1.
Form
Supplied as a liquid in PBS, 0.02% sodium azide.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human GPAT1. Species Crossreactivity: mouse and rat.
References
1. Coleman RA and Lee DP. Enzymes of triacylglycerol synthesis and their regulation. Prog. Lipid Res. 2004; 43:134-76. 2. Linden D, William-Olsson L, Ahnmark A, et al. Liver-directed overexpression of mitochondrial glycerol-3-phosphate acyltransferase results in hepatic steatosis, increased triacylglycerol secretion and reduced fatty acid oxidation. FASEB J. 2006; 20:434-43. 3. Eberle D, Hegarty B, Bossard P, et al. SREBP transcription factors: master regulators of lipid homeostasis. Biochimie 2004; 86:839-48.|4. Lewin TM, de Jong H, Schwerbrock NJ, et al. Mice deficient in glycerol-3-phosphate acyltransferase-1 have diminished myocardial triacylglycerol accumulation during lipogenic diet and altered phospholipid fatty acid composition. Biochim. Biophys. Acta 2008; 1781:352-8.
USBio References
No references available
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