Adipocyte Fatty Acid Binding Protein Human E. coli Tag free

Cat. No.	Size	Price 1 - 4 pcs / 5 - 9 pcs / 10+ pcs
RD172036100	0.1 mg	$421 / $370 / On request

Technical Data

Type

Recombinant protein

Description

Total 132 AA. MW: 14.7 kDa (calculated). UniProtKB acc.no. P15090. 131 AA of recombinant Human AFABP and one extra AA, N-terminal methionin.

Amino Acid Sequence

MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDVITIKSESTFKNTEISFILGQEFDEVTADDRKVKSTITLDGGVLVHVQKWDGKSTTIKRKREDDKLVVECVMKGVTSTRVYERA

Source

E. coli

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

12% SDS-PAGE separation of Human AFABP
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and heated sample, 5μg/lane
3. non-reduced and non-heated sample, 5μg/lane

Endotoxin

< 1.0 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/mL solution in phosphate buffered saline, pH 7.4

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.
SDS PAGE to determine purity of the protein. Endotoxin level determination.

Note

This product is intended for research use only.

Summary

Research topic

Diabetology - Other Relevant Products, Energy metabolism and body weight regulation

Summary

Adipocyte fatty acid binding protein AFABP is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. AFABP is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells . In mice, targeted mutations in AFABP provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from AFABP-deficient mice also have reduced efficiency of lipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated AFABP expression in macrophages upon differentiation and activation. In these cells, AFABP modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific AFABP deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for AFABP in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.

Product References (2)

References

Ayyar BV, Hearty S, O'Kennedy R. Highly sensitive recombinant antibodies capable of reliably differentiating heart-type fatty acid binding protein from noncardiac isoforms. Anal Biochem. 2010 Dec 15;407(2):165-71. doi: 10.1016/j.ab.2010.07.033. Epub 2010 Aug 7. PubMed PMID: 20696127. See more on PubMed
Nagata S, Fujii K, Matsushima T, Fukui M, Sadoshima S, Kuwabara Y, Abe H. Evaluation of EC-IC bypass for patients with atherosclerotic occlusive cerebrovascular disease: clinical and positron emission tomographic studies. Neurol Res. 1991 Dec;13(4):209-16. doi: 10.1080/01616412.1991.11739994. PubMed PMID: 1687329. See more on PubMed

Summary References (15)

References to Adipocyte Fatty Acid Binding Protein

Makowski L, Brittingham KC, Reynolds JM, Suttles J and Hotamisligil GS: The Fatty Acid-binding Protein, aP2, Coordinates Macrophage Cholesterol Trafficking and Inflammatory Activity. J Biol Chem. 2005 Apr 1.280(13):12888–95.
Maeda K, Cao H, Kono K, Gorgun CZ, Furuhashi M, Uysal KT, Cao Q, AtsumiG, Malone H, Krishnan B, Minokoshi Y, Kahn BB, Parker RA and Hotamisligil GS: Adipocyte/macrophage fatty acid binding proteins control integrated metabolic responses in obesity and diabetes. Cell Metabolism, Volume 1, Issue 2, February 2005, Pages 107–119.
Boord JB, Maeda K, Makowski L, Babaev VR, Fazio S, Linton MF, Hotamisligil GS: Combined adipocyte-macrophage fatty acid-binding protein deficiency improves metabolism, atherosclerosis, and survival in apolipoprotein E-deficient mice. Circulation. 2004 Sep 14;110(11):1492–8.
Lehmann F, Haile S, Axen E, Medina C, Uppenberg J, Svensson S, Lundback T, Rondahl L, Barf T: Discovery of inhibitors of human adipocyte fatty acid-binding protein, a potential type 2 diabetes target. Bioorg Med Chem Lett. 2004 Sep 6;14(17):4445–8.
Damcott CM, Moffett SP, Feingold E, Barmada MM, Marshall JA, Hamman RF, Ferrell RE: Genetic variation in fatty acid-binding protein-4 and peroxisome proliferatoractivated receptor gamma interactively influence insulin sensitivity and body composition in males. Metabolism. 2004 Mar;53(3):303–9.
Jenkins-Kruchten AE, Bennaars-Eiden A, Ross JR, Shen WJ, Kraemer FB, Bernlohr DA: Fatty acid-binding protein-hormone-sensitive lipase interaction. Fatty acid dependence on binding. J Biol Chem. 2003 Nov 28;278(48):47636–43.
Hertzel AV, Bennaars-Eiden A, Bernlohr DA: Increased lipolysis in transgenic animals overexpressing the epithelial fatty acid binding protein in adipose cells. J Lipid Res. 2002 Dec;43(12):2105–11.
Fu Y, Luo N, Lopes-Virella MF, Garvey WT: The adipocyte lipid binding protein (ALBP/aP2) gene facilitates foam cell formation in human THP-1 macrophages. Atherosclerosis. 2002 Dec;165(2):259–69.
Storch J, Veerkamp JH, Hsu KT: Similar mechanisms of fatty acid transfer from human anal rodent fatty acid-binding proteins to membranes: liver, intestine, heart muscle, and adipose tissue FABPs. Mol Cell Biochem. 2002 Oct;239(1–2):25–33.
Fisher RM, Hoffstedt J, Hotamisligil GS, Thorne A, Ryden M: Effects of obesity and weight loss on the expression of proteins involved in fatty acid metabolism in human adipose tissue. Int J Obes Relat Metab Disord. 2002 Oct;26(10):1379–85.
Boord JB, Maeda K, Makowski L, Babaev VR, Fazio S, Linton MF, Hotamisligil GS: Adipocyte fatty acid-binding protein, aP2, alters late atherosclerotic lesion formation in severe hypercholesterolemia. Arterioscler Thromb Vasc Biol. 2002 Oct 1;22(10):1686–91.
Fisher RM, Eriksson P, Hoffstedt J, Hotamisligil GS, Thorne A, Ryden M, Hamsten A, Arner P: Fatty acid binding protein expression in different adipose tissue depots from lean and obese individuals. Diabetologia. 2001 Oct;44(10):1268–73.
Scheja L, Makowski L, Uysal KT, Wiesbrock SM, Shimshek DR, Meyers DS, Morgan M, Parker RA, Hotamisligil GS: Altered insulin secretion associated with reduced lipolytic efficiency in aP2-/- mice. Diabetes. 1999 Oct;48(10):1987–94.
Coe NR, Simpson MA, Bernlohr DA: Targeted disruption of the adipocyte lipid-binding protein (aP2 protein) gene impairs fat cell lipolysis and increases cellular fatty acid levels. J Lipid Res. 1999 May;40(5):967–72.
Baxa CA, Sha RS, Buelt MK, Smith AJ, MatareseV, Chinander LL, Boundy KL and Bernlohr DA: Human adipocyte lipid-binding protein: purification of the protein and cloning of its complementary DNA. Biochemistry. 1989; 28 (22), 8683–8690.

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