Analytical Data
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Gene name
SLC26A5
- Application
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Alternative Names
Prestin; Solute carrier family 26 member 5; SLC26A5; PRES; Homo sapiens; Human; Motor protein
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Species
Human
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Source
HEK293
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Tag
GFP;C-StrepⅡ;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P58743-1
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Expression Region
M1-A744
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Protein Length
Full Length of Isoform-1
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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
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Protein Description
FABP9, or fatty acid-binding protein 9, is a member of the FABP family that is primarily expressed in the testis and is implicated in various physiological processes, including lipid transport, metabolism, and cellular signaling. Recent research has highlighted its potential role in regulating spermatogenesis and protecting germ cells from apoptosis. Additionally, FABP9 has been associated with several pathophysiological conditions, such as reproductive disorders and certain types of cancers. The recombinant expression of FABP9 provides a valuable tool for studying its structure-function relationships, interactions with fatty acids, and involvement in metabolic pathways. By producing and characterizing FABP9 as a recombinant protein, researchers aim to elucidate its molecular mechanisms, identify potential therapeutic targets, and explore its utility in biomedical applications. Understanding the role of FABP9 in health and disease could lead to novel strategies for treating conditions related to reproductive health and metabolic disorders, making it a significant focus of ongoing research in the fields of biochemistry and reproductive biology.
