Analytical Data
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Gene name
KRTAP13-3
- Application
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Alternative Names
KRTAP13-3; KAP13.3Keratin-associated protein 13-3
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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
Q3SY46
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Expression Region
1-172aa
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AA Sequence
MSYNCCSRNFSSCSHGGYLHYPGSSCGSSYPSNLVYSTDLCSPSTCQLGSSLYRGCQETCWRPNSCQTLCVESSPCHTSCYYPRTHMLCNSCLTMHVGSRGFGSNSCCSLSCGSRSCSSLGCGSNGFRYLNYRIHTSPSQSYRSRFCHPIYFPPRRWFHSSCYQPFCRSGFY
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Molecular Weight
45.6 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
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Protein Description
KRTAP13-3, a member of the keratin-associated protein (KRTAP) family, plays a crucial role in the structure and function of hair and skin. These proteins are known for their involvement in the formation of the hair shaft and contribute to the physical properties of hair, such as tensile strength and elasticity. Research on KRTAP13-3 is particularly significant due to its potential implications in understanding hair disorders, including alopecia and other conditions affecting hair quality. Recent advancements in recombinant protein technology have enabled scientists to produce KRTAP13-3 in vitro, facilitating detailed studies of its biochemical properties and biological functions. By analyzing the structure, expression patterns, and interactions of KRTAP13-3, researchers aim to uncover its role in keratinization processes and its potential as a therapeutic target for hair-related diseases. Understanding the molecular mechanisms involving KRTAP13-3 could lead to novel strategies for managing hair loss and improving hair health, thereby enhancing the quality of life for individuals suffering from these conditions. Furthermore, the exploration of KRTAP13-3 can provide valuable insights into the evolutionary adaptations of hair keratins across different species, enriching the field of dermatological and trichological research.
