Analytical Data
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Gene name
HFABP
- Application
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Alternative Names
HFABP；Fatty acid-binding Protein. heart
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05413
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Expression Region
1-133aa
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AA Sequence
MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDIL TLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDG QETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
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Molecular Weight
16 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Heart-type fatty acid-binding protein (HFABP) has garnered significant attention in recent years due to its pivotal role in fatty acid metabolism and its potential as a biomarker for various cardiovascular diseases. HFABP is primarily expressed in cardiac and skeletal muscle tissues, where it facilitates the intracellular transport of fatty acids, thus influencing energy metabolism and cardiac function. Research indicates that elevated levels of HFABP in plasma are associated with heart conditions such as acute myocardial infarction and heart failure, underscoring its diagnostic relevance. The recombinant production of HFABP has become essential for the study of its structure-function relationships, as well as for the development of novel therapeutic strategies targeting lipid metabolism disorders. Moreover, recombinant HFABP allows researchers to investigate its binding properties with various ligands, enabling insights into its conformational dynamics and interactions within metabolic pathways. As obesity and metabolic syndromes continue to rise globally, understanding the biological functions of HFABP through recombinant technologies could lead to innovative approaches in managing cardiovascular health and related metabolic diseases. This growing research landscape emphasizes the need for detailed studies on HFABP to fully capitalize on its therapeutic and diagnostic potential.
