Analytical Data
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Gene name
KLK12
- Application
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Alternative Names
KLK12；KLKL5；Kallikrein-12
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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
Q9UKR0
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Expression Region
18-248aa
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AA Sequence
ATPKIFNGTECGRNSQPWQVGLFEGTSLRCGGVLIDHRWVLTAAHCSGSRYWVRLGEHSLSQLDWTEQIRHSGFSVTHPGYLGASTSHEHDLRLLRLRLPVRVTSSVQPLPLPNDCATAGTECHVSGWGITNHPRNPFPDLLQCLNLSIVSHATCHGVYPGRITSNMVCAGGVPGQDACQGDSGGPLVCGGVLQGLVSWGSVGPCGQDGIPGVYTYICKYVDWIRMIMRNN
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Molecular Weight
32.4 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
KLK12, or Kallikrein-related peptidase 12, is part of the kallikrein-related peptidase family, which comprises serine proteases implicated in various physiological and pathological processes. Research on KLK12 has gained significance due to its potential roles in human health, including its association with cancers, particularly in the context of tumor progression and metastasis. Elevated levels of KLK12 have been observed in certain types of cancer, suggesting its possible utility as a biomarker for diagnosis or prognosis. Additionally, KLK12 is thought to be involved in the modulation of the extracellular matrix, influencing cell migration and invasion, which are critical factors in cancer biology. Furthermore, its involvement in physiological processes such as tissue remodeling and inflammatory responses positions KLK12 as a potential therapeutic target. Current studies aim to elucidate the exact mechanisms by which KLK12 exerts its effects, exploring its interactions with other proteins and its regulation in various cellular contexts. Understanding KLK12's structure-function relationship through recombinant protein studies can provide insights into its biological roles and pave the way for the development of novel diagnostic and therapeutic strategies. The ongoing research focuses on the characterization of KLK12's enzymatic activity, substrate specificity, and the impact of its dysregulation in disease states, highlighting the importance of this protein in both basic and clinical research.
