Analytical Data
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Gene name
Klk1b22
- Application
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Alternative Names
Klk1b22；Klk-22；Klk22；Kallikrein 1-related peptidase b22
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Species
Mouse
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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
P15948
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Expression Region
25-259aa
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AA Sequence
ILGGFKCEKNSQPWQVAVYYLDEYLCGGVLLDRNWVLTAAHCYEDKYNIWLGKNKLFQDEPSAQHRLVSKSFPHPDFNMSLLQSVPTGADLSNDLMLLRLSKPADITDVVKPIDLPTTEPKLGSTCLASGWGSINQLIYQNPNDLQCVSIKLHPNEVCVKAHILKVTDVMLCAGEMNGGKDTCKGDSGGPLICDGVLQGITSWGSTPCGEPNAPAIYTKLIKFTSWIKDTMAKNP
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Molecular Weight
41.8 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
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Protein Description
Klk1b22, a member of the kallikrein family, has garnered attention in recent research due to its potential roles in various physiological and pathological processes. Kallikreins are serine proteases that play critical roles in proteolytic pathways affecting blood pressure regulation, fertility, and cancer progression. Klk1b22, specifically, has been implicated in the modulation of inflammatory responses and tissue remodeling. Recent studies suggest that it may have a role in the pathogenesis of certain diseases, including prostate cancer, where aberrant expression levels have been observed. Given the complexity of kallikrein functions, researchers have focused on the recombinant production of Klk1b22 to elucidate its biochemical properties, substrate specificity, and potential clinical applications. By producing this recombinant protein, scientists aim to better understand its enzymatic activity and develop diagnostic or therapeutic strategies targeting Klk1b22-related pathways. Moreover, characterizing Klk1b22 could reveal insights into its possible utility as a biomarker for disease states or as a target for novel interventions. As such, ongoing research into Klk1b22 is crucial for unraveling its biological significance and advancing our knowledge of kallikrein-mediated mechanisms in health and disease.
