Analytical Data
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Gene name
KRTAP3-3
- Application
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Alternative Names
KRTAP3-3; KAP3.3; KRTAP3.3Keratin-associated protein 3-3; High sulfur keratin-associated protein 3.3; Keratin-associated protein 3.3
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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
Q9BYR6
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Expression Region
1-98aa
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AA Sequence
MDCCASRGCSVPTGPATTICSSDKSCRCGVCLPSTCPHTVWLLEPTCCDNCPPPCHIPQPCVPTCFLLNSCQPTPGLETLNLTTFTQPCCEPCLPRGC
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Molecular Weight
36.8 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
KRTAP3-3, a member of the keratin-associated protein (KRTAP) family, has gained significant interest in research due to its role in the structure and function of hair fibers. These proteins are integral to the composition of the hair keratin matrix, influencing hair properties such as strength, texture, and growth. Understanding KRTAP3-3 is crucial because it directly affects the mechanical resilience and overall quality of hair, which can have implications in both health and cosmetic industries. Studies have indicated that variations in KRTAP genes can be associated with different hair types and disorders, underscoring the importance of genetic factors in phenotypic expressions of hair. Additionally, exploring the recombinant expression of KRTAP3-3 provides insights into its functional characteristics and potential applications in therapeutic strategies for hair loss and related conditions. As advancements in molecular biology techniques continue to evolve, the ability to produce and analyze KRTAP3-3 in vitro allows for a deeper understanding of its biochemical pathways and interactions with other keratin-associated proteins, paving the way for novel interventions and treatments in dermatological and cosmetic applications. Ultimately, this research not only enhances our knowledge of keratin biology but also opens up avenues for developing products that can improve hair health and aesthetics.
