FABP5 Protein (AA 2-135) (His tag)

Catalog No. ABIN7505390

This Recombinant FABP5 protein is expressed in Escherichia coli (E. coli).

Quick Overview for FABP5 Protein (AA 2-135) (His tag) (ABIN7505390)

Target: FABP5 (Fatty Acid Binding Protein 5 (Psoriasis-Associated) (FABP5))

Protein Type: Recombinant

Origin: Mouse

Source: Escherichia coli (E. coli)

Purity: > 95 % as determined by reducing SDS-PAGE.

Product Details

Protein Characteristics: AA 2-135

Purification tag / Conjugate: This FABP5 protein is labelled with His tag.

Sequence: Ala 2-Gln 135

Characteristics: A DNA sequence encoding the Mouse FABP5 protein (Q05816) (Ala2-Gln135) was expressed with a N-His .

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Expiry Date: 12 months

Target Details

Target: FABP5 (Fatty Acid Binding Protein 5 (Psoriasis-Associated) (FABP5))

Alternative Name: FABP5

Background:

Abbreviation: FABP5

Target Synonym: Fatty acid-binding protein 5,Epidermal-type fatty acid-binding protein,E-FABP,Fatty acid-binding protein,epidermal,Keratinocyte lipid-binding protein,Psoriasis-associated fatty acid-binding protein homolog,PA-FABP

Background: Fatty acid binding proteins (FABP) are small cytoplasmic lipid binding proteins that are expressed in a tissue specific manner and are involved in intracellular lipid transport. All FABPs bind free fatty acids, cholesterol, and retinoids, which differ in their selectivity, affinity and binding mechanism. Circulating FABP levels are used as indicators of tissue damage. Some FABP polymorphisms have been associated with disorders of lipid metabolism and the development of atherosclerosis. FABPs are structurally conserved, consisting of a water-filled, ligand-binding pocket surrounded by ten anti-parallel beta-barrel structures, capped by an N-terminal helix-turn-helix motif. The helical N-terminus is involved in the regulation of FA transfer from membranes. FABP5, also known as epidermal fatty acid binding protein (E-FABP), is highly expressed in epidermal cells, but also in a plethora of other tissues, including mammary gland, brain, liver, kidney, lung, adipocytes, macrophages, tongue and testis. It is associated with keratinocytes and adipocytes and is suggested to promote fatty acid availability to enzymes, protect cell structures from fatty acid attack, and target fatty acids to nuclear transcription factors. The amino acid sequence of human FABP5 is 80 % , 81 % and 92 % identical to that of mouse, rat and bovine FABP5, respectively.

Molecular Weight:

Calculated MW: 14.63 kDa

Observed MW: 16 kDa

UniProt: Q05816