Analytical Data
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Gene name
CML2
- Application
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Alternative Names
NAT8B; CML2; Putative N-acetyltransferase 8B; Acetyltransferase 1; ATase1; Camello-like protein 2
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UHF3
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Expression Region
1-143aa
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AA Sequence
MAEHAPATFRRLLKLPRTLILLLGGALALLLVSGSWILALVFSLSLLPALWFLAKKPWTRYVDIALRTDMSDITKSYLSECGSCFWVGESEEKVVGTVGALPVDDPTLREKRLQLFHLSVDNEHRGQGIAKALVRTVLQFARD
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Molecular Weight
42.3 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
CML2 (Chronic Myeloid Leukemia Type 2) is linked to the Philadelphia chromosome and is characterized by the BCR-ABL fusion gene resulting from a chromosomal translocation. The study of CML2 recombinant proteins has gained significant attention due to their potential to elucidate the molecular mechanisms underlying CML and to develop targeted therapies. CML presents a distinct advancement in cancer treatment with the introduction of tyrosine kinase inhibitors (TKIs), which specifically target the BCR-ABL fusion protein. However, resistance to treatment and the development of mutations in the BCR-ABL gene pose significant challenges. Research into CML2 recombinant proteins allows for a deeper understanding of these mutations, their structural implications, and the resulting biochemical pathways disrupted in CML. Utilizing recombinant DNA technology, scientists are able to produce large quantities of these proteins for functional studies, which help identify potential therapeutic targets and biomarkers for disease progression. By studying the interactions of CML2 with various cellular components and signaling pathways, researchers aim to design more effective treatment strategies that mitigate resistance and improve patient outcomes. The ongoing investigation into CML2 recombinant proteins not only enhances our understanding of the disease at the molecular level but also paves the way for innovative therapeutic approaches to combat chronic myeloid leukemia more effectively.
