Analytical Data
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Gene name
Normal
- Application
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Alternative Names
Breast normal epithelial cell associated serine protease; Kallikrein related peptidase 10; Kallikrein-10; Kallikrein10; KLK 10; KLK10; KLK10_HUMAN; NES 1; NES1; Normal epithelial cell specific 1; Normal epithelial cell-specific 1; Protease serine like 1; Protease serine-like 1; PRSS L1; PRSSL 1; PRSSL1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43240
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Expression Region
31-274aa
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AA Sequence
AEAALLPQNDTRLDPEAYGSPCARGSQPWQVSLFNGLSFHCAGVLVDQSWVLTAAHCGNKPLWARVGDDHLLLLQGEQLRRTTRSVVHPKYHQGSGPILPRRTDEHDLMLLKLARPVVLGPRVRALQLPYRCAQPGDQCQVAGWGTTAARRVKYNKGLTCSSITILSPKECEVFYPGVVTNNMICAGLDRGQDPCQSDSGGPLVCDETLQGILSWGVYPCGSAQHPAVYTQICKYMSWINKVIR
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Molecular Weight
30.8kDa
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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
Normal protein recombination research focuses on the systematic study of proteins that are crucial for various biological functions and pathways. This area of study arose from the recognition that understanding protein structure and function is essential for advancing fields such as biochemistry, molecular biology, and biotechnology. With the advent of techniques like recombinant DNA technology, scientists have been able to manipulate genetic sequences to produce proteins with specific traits or functions. Normal recombinant proteins, which are typically designed to closely mimic their naturally occurring counterparts, serve as vital tools for understanding protein interactions, signaling pathways, and cellular mechanisms. These proteins are often used in therapeutic applications, such as the development of vaccines, enzyme replacement therapies, and monoclonal antibodies. Additionally, they play an important role in basic research, helping to elucidate the role of proteins in health and disease. As research progresses, the refinement of techniques for protein expression, purification, and characterization continues to enhance our ability to produce high-quality recombinant proteins, thus broadening their application in medical and industrial settings. This ongoing research aims to provide deeper insights into protein functionality and its implications for human health, making normal recombinant proteins a cornerstone of contemporary scientific exploration.
