YB91985Hu01

Fatty Acid Binding Protein 5, Epidermal (FABP5)

Organism: Homo sapiens (Human)

Instruction manual

FOR IN VITRO USE AND RESEARCH USE ONLY

NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES

1th Edition (Revised in February, 2012)

[ DESCRIPTION ]

Protein Names: Fatty Acid Binding Protein 5, Epidermal

Gene Names: FABP5

Size: 100µg

Source: Recombinant

Expression Host: E.coli

Function: High specificity for fatty acids. Highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity. May be involved in keratinocyte differentiation.

Subcellular Location: Cytoplasm.

Tissue Specificity: Keratinocytes; highly expressed in psoriatic skin.

[ PROPERTIES ]

Residues: Ala2~Glu135 (Accession # Q01469), with a N-terminal His-tag.

Grade & Purity: >97%, 16.3 kDa as determined by SDS-PAGE reducing

conditions.

Form & Buffer: Supplied as lyophilized form in PBS, pH 7.4.

Endotoxin Level: <1.0 EU per 1μg (determined by the LAL method).

Applications: SDS-PAGE; WB; ELISA; IP.

(May be suitable for use in other assays to be determined by the end user.)

Predicted Molecular Mass: 16.3 kDa

[ PREPARATION ]

Reconstitute in PBS.

[ STORAGE AND STABILITY ]

Storage: Store at 4oC for short term storage (1-2 weeks). Aliquot and store at -20oC or -80oC for long term storage. Avoid repeated freeze/thaw cycles.

Valid period: 12 months stored at -80oC.

[ BACKGROUND]

The target protein is fused with a His-tag and its sequence is listed below. The first Met is an initiator amino acid. Moreover, Gly and Ser are added to improve the flexibility of N-terminus at both ends of the His-tag, which will increase the chelating ability of the tag to Ni-Sepharose during purification.

MGHHHHHHSGS-ATVQQLEGR WRLVDSKGFD EYMKELGVGI ALRKMGAMAK PDCIITCDGK NLTIKTESTL

KTTQFSCTLG EKFEETTADG RKTQTVCNFT DGALVQHQEW DGKESTITRK LKDGKLVVEC VMNNVTCTRI

YEKVE

[ REFERENCES ]

1.Madsen P.S., et al. (1992) J. Invest. Dermatol. 99:299-305.

2.Gutierrez-Gonzalez L.H., et al. (2002) Biochem. J. 364:725-737.

3.Hohoff C., et al. (1999) Biochemistry 38:12229-12239.

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