Fatty acid free serum albumin

Manufactured by Merck Group

Sourced in Morocco

Fatty acid-free serum albumin is a lab reagent used as a stabilizer and carrier protein in various biochemical and cell culture applications. It is derived from bovine serum and has been processed to remove any fatty acids. This product provides a source of high-purity albumin without the potential interference from bound lipids.

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Lab products found in correlation

Dulbecco modified eagle medium (dmem), by Thermo Fisher Scientific (2 mentions) Free glycerol determination kit, by Merck Group (1 mentions) Fatty acid free bsa, by Merck Group (1 mentions) Indomethacin, by Merck Group (1 mentions)

Spelling variants of this product

Fatty acid-free bovine serum albumin (128 citations) Fatty acids (54 citations) Free fatty acids (15 citations) Fatty acid-free human serum albumin (11 citations) Fatty acid-free albumin (8 citations) Fatty acid-free bovine serum albumin (BSA) fraction V (8 citations) Fatty acid free bovine serum albumin (FAF-BSA) (7 citations) Albumins ( (2 citations) Fatty acid-free albumin from human serum (2 citations) Fatty acid-free bovine serum albumin (FF-BSA) (2 citations)

3 protocols using fatty acid free serum albumin

Epididymal Fat Pad Glycerol Release

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Epididymal fat pads were surgically removed from male mice and washed
with ice-cold PBS. Fat pads (100 mg, n = 4/mouse) were preincubated for 1 h in
140 μl of DMEM (Life Technologies) containing 2% fatty acid-free serum
albumin (Sigma-Aldrich). Subsequently, fat pads were incubated in 250 μl
of KRH buffer (125 mM NaCl, 5 mM KCl, 1.8 mM CaCl2, 2.6 mM MgSO4, 5 mM HEPES, pH
7.2) plus 2% BSA (fatty acid free) for 2h at 37°C. Free glycerol content
was quantified for each sample in the medium using the Free Glycerol
Determination Kit (Wako Diagnostics). Glycerol release from each sample was
normalized to the weight of each fat pad.

Dumas S.N., Guo C.A., Kim J.K., Friedline R.H, & Ntambi J.M. (2018). Interleukin-6 derived from cutaneous deficiency of stearoyl-CoA desaturase- 1 may mediate metabolic organ crosstalk among skin, adipose tissue and liver. Biochemical and biophysical research communications, 508(1), 87-91.

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Measuring Glycerol Release in Mammary Fat Pads

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Mammary fat pads were surgically removed from 16-week-old MMTV-rtTA/TRE-TAZ^4SA or wild-type mice and washed with ice-cold PBS. Mammary Fat pads (n = 6) were pre-incubated for 1 h in 140 µl of DMEM (Life Technologies, MA) containing 2% fatty acid-free serum albumin (Sigma-Aldrich, MO). Subsequently, mammary fat pads were incubated in 250 ul of KRH buffer (125 mM NaCl, 5 mM KCl, 1.8 mM CaCl₂, 2.6 mM MgSO₄, 5 mM HEPES, pH 7.2) plus 2% fatty acid free BSA (Sigma-Aldrich, MO) for 2 h at 37 °C. Free glycerol content was quantified for each sample in the medium using the Free Glycerol Determination Kit (Sigma-Aldrich, MO). Glycerol release from each sample was normalized to the weight of each mammary fat pad.

Denson K.E., Mussell A.L., Shen H., Truskinovsky A., Yang N., Parashurama N., Chen Y., Frangou C., Yang F, & Zhang J. (2018). The Hippo Signaling Transducer TAZ Regulates Mammary Gland Morphogenesis and Carcinogen-induced Mammary Tumorigenesis. Scientific Reports, 8, 6449.

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Ex vivo Mouse Calvarial Culture

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Ex vivo organ culture from neonatal mouse calvaria was performed as previously described.^{28 (link), 29 (link)} Bone explants from calvaria were obtained by dissecting parietal bones and frontal bones from 7-day-old Men1^flox or Men1^Dmp1Cre mice. Calvaria were cut through the sagittal suture and each half was cultured in one well of a 24-well plate. Calvarial halves were treated with 1 μM indomethacin (Sigma-Aldrich) in α-MEM supplemented with fatty acid-free serum albumin (Sigma-Aldrich). After overnight incubation, calvarial halves were treated with CXCL10-neutralizing antibody (20 ng/ml) or IgG in α-MEM supplemented with 10 nM 1,25-dihydroxyvitamin D3 for 5 days. Medium was collected for CTX enzyme-linked immunosorbent assay (ELISA) and calvarial halves were used for RNA isolation or histology.

Liu P., Lee S., Knoll J., Rauch A., Ostermay S., Luther J., Malkusch N., Lerner U.H., Zaiss M.M., Neven M., Wittig R., Rauner M., David J.P., Bertolino P., Zhang C.X, & Tuckermann J.P. (2017). Loss of menin in osteoblast lineage affects osteocyte–osteoclast crosstalk causing osteoporosis. Cell Death and Differentiation, 24(4), 672-682.

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