Analytical Data
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Gene name
FABP5
- Application
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Alternative Names
FABP5;Fatty acid-binding Protein 5
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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
Q01469
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Expression Region
2-135aa
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AA Sequence
ATVQQLEGRWRLVDSKGFDEYMKELGVGIALRKMGAMAKPDCIITCDGKN LTIKTESTLKTTQFSCTLGEKFEETTADGRKTQTVCNFTDGALVQHQEWD GKESTITRKLKDGKLVVECVMNNVTCTRIYEKVE
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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
Fatty Acid-binding Protein 5 (FABP5) is a member of the FABP family, which plays a critical role in intracellular lipid transport and metabolism. It is primarily expressed in adipose tissue and skin, and emerging research indicates that FABP5 is involved in various physiological processes, including inflammation, cell differentiation, and metabolic regulation. Dysregulation of FABP5 has been linked to several pathological conditions, such as obesity, diabetes, and cancer, underscoring its potential as a therapeutic target. The recombinant expression of FABP5 allows for detailed studies on its structure-function relationship, facilitating the understanding of its role in fatty acid metabolism and signaling pathways. By producing recombinant FABP5 in various systems, researchers can investigate its interactions with lipids and proteins, assess the effects of mutations, and explore its therapeutic implications in metabolic disorders. Progress in this field may pave the way for novel approaches to manipulate FABP5 activity, offering new insights into treatment strategies for diseases associated with lipid dysregulation. Understanding the functional mechanisms of FABP5 through recombinant protein studies remains an active area of research, promising advancements in both basic science and clinical applications.
