Analytical Data
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Gene name
S100A13
- Application
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Alternative Names
S100A13；Protein S100-A13
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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
Q99584
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Expression Region
1-98aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAAEPLTELEESIETVVTTFFTFARQEGRK DSLSVNEFKELVTQQLPHLLKDVGSLDEKMKSLDVNQDSELKFNEYWRLI GELAKEIRKKKDLKIRKK
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Molecular Weight
14 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
S100A13 is a member of the S100 protein family, known for being calcium-binding proteins that play critical roles in various cellular processes, including cell differentiation, proliferation, and apoptosis. Recent studies have highlighted its involvement in cancer progression, particularly in tumor growth, metastasis, and the modulation of inflammatory responses. The overexpression of S100A13 has been linked to poor prognosis in several malignancies, making it a potential biomarker for cancer diagnosis and a target for therapeutic interventions. Moreover, S100A13 has been shown to interact with other signaling pathways, such as those involving the RAGE receptor, further complicating its role in cellular signaling. Given its diverse functions and implications in both normal physiology and pathological conditions, researchers are increasingly focusing on recombinant S100A13 protein for functional studies. This includes examining its structure-function relationship, investigating its interactions with other proteins, and exploring its potential as a therapeutic target or diagnostic marker in various diseases. The production of recombinant S100A13 allows for in-depth analysis of its biological activities and the development of potential inhibitors or modulators that could alter its function in disease contexts. As understanding the molecular mechanisms underlying S100A13's role in diseases progresses, it holds promise for advancing therapeutic strategies aimed at targeting S100A13-related pathways in oncology and beyond.
