Analytical Data
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Gene name
sak
- Application
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Alternative Names
sak；SAK；STK18；Serine/threonine-Protein kinase PLK4
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Species
E.coli
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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
P15240
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Expression Region
28-163aa
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AA Sequence
SSSFDKGKYK KGDDASYFEP TGPYLMVNVT GVDGKRNELL SPRYVEFPIK PGTTLTKEKI EYYVEWALDA TAYKEFRVVE LDPSAKIEVT YYDKNKKKEE TKSFPITEKG FVVPDLSEHI KNPGFNLITK VVIEKK
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Molecular Weight
15.6 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
The SAK (streptokinase-activated plasminogen) protein has garnered considerable interest in the field of biomedicine due to its role as a potent thrombolytic agent. Initially derived from Streptococcus bacteria, SAK facilitates the conversion of plasminogen into plasmin, an enzyme that plays a crucial role in breaking down blood clots. This property makes it a valuable candidate for treating conditions such as myocardial infarction and stroke, where thrombus formation can critically impede blood flow. Research efforts have focused on understanding the biochemical mechanisms underlying SAK activation and its interactions with various substrates, paving the way for the optimization of its therapeutic applications. Additionally, the potential for recombinant DNA technology to produce SAK in a more controlled and efficient manner has opened new avenues for clinical use. In the context of drug development, studies have explored modifications to improve SAK's stability, efficacy, and safety profile, addressing challenges such as the risk of bleeding associated with thrombolytic therapies. Furthermore, the exploration of SAK’s structure-function relationships through techniques like X-ray crystallography and electron microscopy has shed light on its active sites and binding affinities, which are critical for designing more effective thrombolytic agents. Overall, the ongoing research into SAK recombinant proteins aims to enhance their clinical applicability and provide innovative solutions in the management of thrombotic diseases.
