Analytical Data
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Gene name
SYK
- Application
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Alternative Names
p72-Syk; Spleen tyrosine kinase
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P43405
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Expression Region
374~635aa
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Molecular Weight
34kDa
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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
Identification
Protein Description
The study of SYK (Spleen Tyrosine Kinase) recombinant protein has gained significant attention in recent years due to its pivotal role in various cellular processes, particularly in immune signaling and hematopoiesis. SYK is a non-receptor tyrosine kinase that is primarily expressed in immune cells, including B cells and myeloid cells, where it acts as a crucial mediator in the signaling pathways following engagement of immunoreceptors such as B-cell receptors and Fc receptors. Abnormal SYK activity has been implicated in several diseases, including autoimmune disorders, allergies, and cancers, which makes it a potential therapeutic target. Recent advancements in molecular cloning and protein expression technologies have enabled the production of recombinant SYK proteins, facilitating studies on its structure, function, and regulation. Additionally, understanding the mechanisms by which SYK contributes to disease pathogenesis has opened new avenues for drug development, highlighting the need for detailed characterization of SYK and its signaling networks. Thus, the research on SYK recombinant proteins not only enhances our comprehension of immune system functions but also holds promise for innovative therapeutic strategies to treat SYK-related conditions.
