Analytical Data
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Gene name
ZMAT5
- Application
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Alternative Names
U11/U12 small nuclear ribonucleoprotein 20KDA protein ;U11/U12 snRNP 20KDA protein ;U11/U12-20K
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UDW3
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Expression Region
1-170aa
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Molecular Weight
36 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
ZMAT5, a member of the ZINC finger protein family, has garnered attention in recent years due to its potential role in various biological processes, including cellular regulation and development. Initial studies have suggested that ZMAT5 may play a pivotal role in modulating gene expression and influencing cellular responses to stress. Its involvement in critical pathways raises the possibility of ZMAT5 as a key player in cancer progression, immune responses, and other pathological conditions. Recent investigations have focused on the characterization of recombinant ZMAT5 protein, aiming to elucidate its structure-function relationships, interactions with other molecular partners, and mechanism of action. By employing advanced techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, researchers are striving to obtain detailed insights into the protein’s conformational dynamics. Moreover, the expression of ZMAT5 as a recombinant protein facilitates the development of antibodies and therapeutic agents targeting this protein, potentially leading to innovative approaches in disease treatment. Overall, the ongoing research surrounding ZMAT5 recombinant protein underscores its significance in fundamental biological research and therapeutic applications, paving the way for future discoveries that may harness its functions for clinical benefit.
