Analytical Data
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Gene name
ARFIP1
- Application
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Alternative Names
ARFIP1；Arfaptin-1
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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
Q9JHU5
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Expression Region
1-341aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMAQESPKNSAAEIPVTSNGEVDDSREH SFNRDLKHSLPSGLGLSETQITSHGFDNTKEGVIEAGAFQGGQRTQTKSG PVILADEIKNPAMEKLELVRKWSLNTYKCTRQIISEKLGRGSRTVDLELE AQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQRQLGDAFADLSLKSLE LHEEFGYNADTQKLLAKNGETLLGAINFFIASVNTLVNKTIEDTLMTVKQ YESARIEYDAYRTDLEELNLGPRDANTLPKIEQSQHLFQAHKEKYDKMRN DVSVKLKFLEENKVKVLHNQLVLFHNAIAAYFAGNQKQLEQTLKQFHIKL KTPGVDAPSWLEEQ
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Molecular Weight
41 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
ARFIP1, or ADP-ribosylation factor interactin protein 1, has garnered significant attention in the field of cellular biology due to its crucial role in membrane trafficking and cytoskeletal dynamics. This protein is an essential component of the endosomal-lysosomal pathway and is known to interact with ARF GTPases, which are pivotal regulators of vesicular transport processes. Current research suggests that ARFIP1 is involved in various cellular functions, including endocytosis, exocytosis, and the maintenance of cellular architecture. Dysregulation of ARFIP1 has been implicated in several pathological conditions, including cancer and neurodegenerative diseases, making it a potential target for therapeutic interventions. Recent advances in recombinant protein technology have facilitated the study of ARFIP1, enabling researchers to produce and characterize this protein in vitro. Understanding the structural and functional properties of ARFIP1 through recombinant expression can provide valuable insights into its biological mechanisms and interactions, offering a pathway for developing novel strategies to modulate its activity in disease contexts. As researchers continue to explore the multifaceted roles of ARFIP1, the generation of high-purity, biologically active recombinant ARFIP1 will be critical for elucidating its mechanisms of action and potential as a drug target. The study of ARFIP1 not only enhances our understanding of fundamental cellular processes but also opens new avenues for addressing the complexities of diseases linked to its dysfunction. Thus, the investigation of ARFIP1 through recombinant protein studies represents a significant step toward unraveling its contributions to cell biology and its potential implications in health and disease.
