详细说明
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Bioassay data are not available.
Source
E. coli-derived Met1-Val132, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
AnalysisMet1
Predicted Molecular Mass
16 kDa
SDS-PAGE
15 kDa, reducing conditions
9488-CL |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT. | ||
Reconstitution Reconstitute at 1 mg/mL in PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: FABP9/T-FABP
Fatty acid binding protein-9 (FABP9; also named Testis lipid-binding protein, Testis-type fatty acid-binding protein, TLBP, T- FABP, PERF, or PERF15) is a member of a large superfamily of lipid binding proteins that are expressed in a tissue specific manner (1, 6, 7). FABP9 is one of ten cytoplasmic FABPs that are 14-15 kDa in size and range from 126-140 amino acids (aa) in length (1, 2, 3). Although all are highly conserved in their tertiary structure, there is only modest aa identity between any two members. The FABP family members are subdivided based on organ or tissue type it was originally expressed or identified; liver- (L-FABP), intestine- (I‑FABP), heart- (H-FABP), adipocyte- (A-FABP), epidermal- (E-FABP), ileal- (Il-FABP), brain- (B-FABP), myelin- (M-FABP) and testis-FABP (T-FABP) (1). Human T‑FABP, the product of the FABP9 gene, is a 132 aa cytosolic protein that shows a flattened beta -barrel structure generated by a series of antiparallel beta -strands and two alpha ‑helices (4, 8). One molecule of FABP-9 is capable of binding one long-chain fatty acid (1, 5). It is suggested that ligands first bind to the outside of the molecule, and this binding subsequently induces a conformational change in the binding protein, resulting in "internalization" of the ligand (4, 5). Human FABP-9 is 71%, 68% and 62% aa identical to mouse, rat and canine FABP-9, respectively. It also shows 26% and 28% aa identity to human L-FABP and I‑FABP, respectively.
References:
Smathers, R & Petersen, D. (2011) Human Genomics 5:170.
Storch, J. & Thumser, AE. (2000) Biochim Biophys Acta. 1486:28.
Zimmerman, A.W. & Veerkamp, J.H. (2007) Protein Sci. 9:2042.
Bernlohr, D. et al. (1997) Ann. Rev. of Nut. 17:277.
Majava,V. et al. (2010) PLoS One. 5:e10300.
Zimmerman, A.W. and J.H. Veerkamp (2002) Cell. Mol. Life Sci. 59:1096.
Haunerland, N.H. and F. Spener (2004) Prog. Lipid Res. 43:328.
Oko, R. & Morales, C.R. (1994) Dev Biol. 166:235.
Long Name:
Fatty Acid-Binding Protein 9
Entrez Gene IDs:
646480 (Human); 21884 (Mouse)
Alternate Names:
FABP9; FABP-9; Fatty Acid Binding Protein 9, Testis; Fatty Acid-Binding Protein 9; Lipid-Binding Protein; PERF 15; PERF; PERF15; Testis Lipid Binding Protein; Testis Lipid-Binding Protein; Testis-Type Fatty Acid-Binding Protein; TFABP; T-FABP; TLBP