Analytical Data
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Gene name
KRT37
- Application
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Alternative Names
KRT37; HHA7; HKA7; KRTHA7; Keratin; type I cuticular Ha7; Hair keratin; type I Ha7; Keratin-37; K37
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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
O76014
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Expression Region
1-449aa
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AA Sequence
MTSFYSTSSCPLGCTMAPGARNVFVSPIDVGCQPVAEANAASMCLLANVAHANRVRVGSTPLGRPSLCLPPTSHTACPLPGTCHIPGNIGICGAYGKNTLNGHEKETMKFLNDRLANYLEKVRQLEQENAELETTLLERSKCHESTVCPDYQSYFRTIEELQQKILCSKAENARLIVQIDNAKLAADDFRIKLESERSLHQLVEADKCGTQKLLDDATLAKADLEAQQESLKEEQLSLKSNHEQEVKILRSQLGEKFRIELDIEPTIDLNRVLGEMRAQYEAMVETNHQDVEQWFQAQSEGISLQAMSCSEELQCCQSEILELRCTVNALEVERQAQHTLKDCLQNSLCEAEDRYGTELAQMQSLISNLEEQLSEIRADLERQNQEYQVLLDVKARLENEIATYRNLLESEDCKLPCNPCSTPASCTSCPSCGPVTGGSPSGHGASMGR
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Molecular Weight
75.79 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
KRT37, or Keratin 37, is a member of the keratin family, which plays a crucial role in the structural integrity and function of epithelial tissues. Keratins are intermediate filament proteins that are fundamental components of the cytoskeleton in epithelial cells, contributing to mechanical stability and resilience against physical stress. Research on KRT37 is particularly relevant in the contexts of skin biology and pathology, including wound healing, skin diseases, and tumorigenesis. Alterations in keratin expression, including KRT37, have been implicated in various dermatological conditions and cancers, highlighting its potential as a biomarker for disease diagnosis and prognosis. Furthermore, KRT37 is expressed primarily in stratified squamous epithelia, and its regulation is linked to cellular differentiation and development. Recent studies have focused on the characterization of KRT37's structure and function, as well as its interactions with other cellular components. By developing recombinant KRT37 protein, researchers aim to investigate its specific roles in cellular processes and to explore therapeutic applications. Understanding the functions of KRT37 could lead to novel strategies for treating skin disorders and contribute to the growing body of knowledge regarding keratin biology and its implications in health and disease.
