Analytical Data
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Gene name
HK1/KLK1
- Application
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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
P06870
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Expression Region
19-262aa
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AA Sequence
PPIQSRIVGGWECEQHSQPWQAALYHFSTFQCGGILVHRQWVLTAAHCIS DNYQLWLGRHNLFDDENTAQFVHVSESFPHPGFNMSLLENHTRQADEDYS HDLMLLRLTEPADTITDAVKVVELPTQEPEVGSTCLASGWGSIEPENFSF PDDLQCVDLKILPNDECKKVHVQKVTDFMLCVGHLEGGKDTCVGDSGGPL MCDGVLQGVTSWGYVPCGTPNKPSVAVRVLSYVKWIEDTIAENSVDHHHH HH
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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
HK1 (Hexokinase 1) and KLK1 (Kallikrein 1) are proteins that have garnered significant attention in biomedical research due to their roles in various physiological and pathological processes. HK1 is an essential enzyme in the glycolytic pathway, responsible for phosphorylating glucose, thus playing a crucial role in cellular energy metabolism. Its involvement in cancer metabolism has led to investigations into its potential as a therapeutic target, where altered expression levels may influence tumor growth and survival. On the other hand, KLK1, a member of the kallikrein-related peptidase family, is implicated in cardiovascular regulation and has been associated with inflammatory processes and tumor progression. Research has shown that KLK1 can enhance angiogenesis and promote cancer cell invasion, making it a potential biomarker for certain cancers. The recombination of HK1 and KLK1 proteins aims to explore their functional interactions in metabolic disorders and cancer biology, possibly yielding new therapeutic strategies or diagnostic tools. Recent advancements in recombinant protein technology facilitate the production of these proteins in vitro, allowing for thorough biochemical and biophysical characterization and the investigation of their roles in disease contexts. Understanding the mechanisms of HK1 and KLK1 at a molecular level could provide insights into their contributions to disease and pave the way for innovative treatments targeting these pathways.
