Analytical Data
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Gene name
SPIN4
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简介
The SPIN4 protein exhibits H3K4me3 binding activity, demonstrating affinity for lysine 4 trimethylated histone H3. This unique combination suggests a role in recognizing specific chromatin modifications, potentially regulating gene expression or chromatin dynamics. SPIN4 Protein, Human is the recombinant human-derived SPIN4 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
SPIN4; Spindlin-4
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q56A73
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Expression Region
S2-P249
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Protein Length
Partial
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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
The studies surrounding the ClpB protein, a member of the heat shock protein family, have gained significant attention due to its crucial role in protein homeostasis and stress responses in cells. ClpB is a bacterial disaggregase, involved in the refolding of denatured proteins, and operates in conjunction with ATP to facilitate the solubilization of aggregated proteins, thereby assisting in the recovery of proper protein functionality under stress conditions. Given its importance in cellular health, ClpB has been extensively researched in various microorganisms, particularly in bacteria like Escherichia coli. Its ability to enhance protein refolding offers promising applications in biotechnology, including improved protein production systems and the development of therapeutic proteins. Moreover, ClpB's potential role in pathogenesis in certain bacteria makes it an interesting target for drug design. Research into the structure-function relationships of ClpB, its interaction with other molecular chaperones, and the mechanisms underlying its disaggregation activity continues to be pivotal in understanding bacterial adaptation to stress and offers insights into developing innovative strategies to combat bacterial infections. The ongoing exploration of recombinant ClpB protein not only sheds light on fundamental biological processes but also has translational implications in medicine and industrial biotechnology.
