Analytical Data
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Gene name
KRTAP3-2
- Application
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Alternative Names
KRTAP3-2; KAP3.2; KRTAP3.2Keratin-associated protein 3-2; High sulfur keratin-associated protein 3.2; Keratin-associated protein 3.2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BYR7
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Expression Region
1-98aa
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AA Sequence
MDCCASRSCSVPTGPATTICSSDKSCRCGVCLPSTCPHTVWLLEPICCDNCPPPCHIPQPCVPTCFLLNSCQPTPGLETLNLTTFTQPCCEPCLPSTI
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Molecular Weight
37.18 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
KRTAP3-2, a member of the keratin-associated protein (KRTAP) family, plays a significant role in the structural composition of hair and wool. These proteins, particularly prevalent in mammals, contribute to the unique properties of keratin fibers, influencing characteristics such as tensile strength, elasticity, and texture. Recent studies have highlighted the importance of KRTAP3-2 in dermatological conditions related to hair disorders, as well as in agricultural biotechnology for improving fleece quality in sheep. The recombinant production of KRTAP3-2 has garnered interest in both basic research and applied sciences, offering insights into keratin biosynthesis and potential applications in tissue engineering, where keratin-based materials could mimic natural structures. Investigating KRTAP3-2 at the molecular level can further elucidate its functional mechanisms and interaction with other keratin molecules, potentially leading to novel therapeutic strategies for hair loss and enhancement of livestock quality traits. Overall, the research surrounding KRTAP3-2 not only expands our understanding of keratin biology but also paves the way for innovations in cosmetic and agricultural industries.
