Analytical Data
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Gene name
KLK15
- Application
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Alternative Names
KLK15;Kallikrein-15
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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
Q9H2R5
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Expression Region
22-256aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSLLEGDEC APHSQPWQVA LYERGRFNCG ASLISPHWVL SAAHCQSRFM RVRLGEHNLR KRDGPEQLRT TSRVIPHPRY EARSHRNDIM LLRLVQPARL NPQVRPAVLP TRCPHPGEAC VVSGWGLVSH NEPGTAGSPR SQVSLPDTLH CANISIISDT SCDKSYPGRL TNTMVCAGAE GRGAESCEGD SGGPLVCGGI LQGIVSWGDV PCDNTTKPGV YTKVCHYLEW IRETMKRN
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Molecular Weight
28 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
KLK15, or Kallikrein-related peptidase 15, is a member of the kallikrein gene family, which comprises serine proteases implicated in various physiological and pathological processes. Research on KLK15 has gained traction due to its potential roles in cancer biology, particularly in breast cancer progression, where elevated levels of this protein have been correlated with malignancy. Moreover, KLK15 is investigated for its involvement in other conditions such as endometriosis and various reproductive functions, highlighting its significance in both health and disease. The recombinant form of KLK15 has been developed to aid in the elucidation of its biological functions and mechanisms. By generating KLK15 as a recombinant protein, researchers aim to better understand its enzymatic properties, substrate specificity, and regulatory pathways. This recombinant protein facilitates the study of KLK15’s role in cellular signaling, including its interactions with various substrates and inhibitors, thus providing insights into its potential as a biomarker for diagnosis or therapeutic target. Recent studies have begun to explore the implications of KLK15 in tumor microenvironments and its interaction with immune cells, paving the way for novel therapeutic strategies in cancer treatment. Overall, the research on KLK15 and its recombinant protein underscores its importance in advancing our understanding of disease mechanisms and developing innovative diagnostic and therapeutic approaches.
