Analytical Data
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Gene name
ERAF
- Application
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Alternative Names
AHSP; AHSP_HUMAN; Alpha hemoglobin stabilizing protein; Alpha-hemoglobin-stabilizing protein; EDRF; ERAF; Erythroid associated factor; Erythroid differentiation associated factor; Erythroid differentiation related factor
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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
Q9NZD4
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Expression Region
1-102aa
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AA Sequence
MALLKANKDLISAGLKEFSVLLNQQVFNDPLVSEEDMVTVVEDWMNFYINYYRQQVTGEPQERDKALQELRQELNTLANPFLAKYRDFLKSHELPSHPPPSS
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Molecular Weight
38.8 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
ERAF, or Erythroid-Associated Factor, is a crucial protein that has garnered significant attention in the field of molecular biology due to its role in erythropoiesis and various hematological disorders. Initially identified as a key regulator in the maturation of erythroid cells, ERAF is believed to play a pivotal role in the differentiation and survival of these cells in the bone marrow. Recent studies have highlighted its involvement not only in normal erythropoiesis but also in pathophysiological conditions such as anemia and other blood disorders. Understanding the mechanisms underlying ERAF's function can provide insights into potential therapeutic strategies for these conditions. Additionally, ERAF has been linked to various signaling pathways that influence cell proliferation and apoptosis, making it a subject of interest in cancer research as well. The ongoing exploration of ERAF's structure and functional properties aims to elucidate its precise role in both normal and malignant cells, paving the way for novel approaches to target its pathways in treatment protocols. The integration of advanced techniques in biochemistry and molecular genetics continues to enhance our understanding of ERAF, marking it as a significant factor in both basic research and clinical applications.
