Analytical Data
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Gene name
CEBPa
- Application
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Alternative Names
CEBPa;CEBP;CCAAT/enhancer-binding Protein alpha
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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
P49715
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Expression Region
1-358aa
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AA Sequence
MESADFYEAE PRPPMSSHLQ SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG GGGGDFDYPG APAGPGGAVM PGGAHGPPPG YGCAAAGYLD GRLEPLYERV GAPALRPLVI KQEPREEDEA KQLALAGLFP YQPPPPPPPS HPHPHPPPAH LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA LGAAGLPGPG SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL VKAMGNCA
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Molecular Weight
37.5 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
CEBPa (CCAAT/enhancer binding protein alpha) is a key transcription factor that plays a crucial role in various biological processes, including hematopoiesis, adipogenesis, and liver function. Aberrant expression or mutations in CEBPa have been implicated in several diseases, particularly in acute myeloid leukemia (AML), where it functions as a tumor suppressor. Research has shown that CEBPa is essential for normal myeloid differentiation, and its loss can lead to the proliferation of myeloid progenitors and ultimately contribute to leukemogenesis. As a result, there is a growing interest in characterizing CEBPa through recombinant protein studies. These studies focus on the protein's structure, DNA-binding properties, and interactions with other regulatory proteins, which are critical for understanding its functional mechanisms. The production of CEBPa as a recombinant protein allows for detailed biochemical analyses, facilitating the identification of its functional domains and post-translational modifications. Additionally, recombinant CEBPa can be utilized in various in vitro assays to study its effect on gene expression and the molecular pathways it regulates. Understanding CEBPa's role in cellular processes holds significant potential for therapeutic interventions, as targeting its regulatory networks could pave the way for novel treatments in AML and other diseases linked to CEBPa dysfunction. Research in this area is advancing rapidly, highlighting the importance of CEBPa not only as a fundamental aspect of cell biology but also as a potential target for drug development.











