Analytical Data
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Gene name
KLK5
- Application
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Alternative Names
KLK5;SCTE;Kallikrein-5
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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
Q9Y337
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Expression Region
23-293aa
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AA Sequence
VTEHVLANNDVSCDHPSNTVPSGSNQDLGAGAGEDARSDDSSSRIINGSD CDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYS LSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPI NVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYP RQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRP GVYTNLCKFTKWIQETIQANSVDHHHHHH
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Molecular Weight
31 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
KLK5, or Kallikrein-related peptidase 5, is a member of the kallikrein family of serine proteases and plays a crucial role in various physiological and pathological processes, including skin homeostasis and keratinocyte differentiation. Its expression is primarily observed in the epidermis, and it has been implicated in the regulation of extracellular matrix remodeling and inflammatory responses. The study of KLK5 recombinant protein has gained interest due to its potential therapeutic applications, particularly in dermatological conditions like psoriasis and acne, as well as in cancer research where it may influence tumor progression and metastasis. Research efforts have focused on the expression, purification, and characterization of KLK5 to understand its enzymatic function and substrate specificity. Additionally, producing KLK5 as a recombinant protein allows for detailed studies on its role in skin biology and its interactions with other proteins in the extracellular environment. Understanding KLK5’s mechanisms can lead to the development of novel treatment modalities that leverage its proteolytic activity, thereby potentially improving outcomes for patients suffering from skin disorders or malignancies. This ongoing research underscores the importance of KLK5 in both health and disease, highlighting its potential as a biomarker and therapeutic target in various clinical settings.
