Analytical Data
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Gene name
AP1AR
- Application
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Alternative Names
AP1AR;C4orf16;AP-1 complex-associated regulatory Protein
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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
Q63HQ0
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Expression Region
1-302aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGNCCWTQCF GLLRKEAGRL QRVGGGGGSK YFRTCSRGEH LTIEFENLVE SDEGESPGSS HRPLTEEEIV DLRERHYDSI AEKQKDLDKK IQKELALQEE KLRLEEEALY AAQREAARAA KQRKLLEQER QRIVQQYHPS NNGEYQSSGP EDDFESCLRN MKSQYEVFRS SRLSSDATVL TPNTESSCDL MTKTKSTSGN DDSTSLDLEW EDEEGMNRML PMRERSKTEE DILRAALKYS NKKTGSNPTS ASDDSNGLEW ENDFVSAEMD DNGNSEYSGF VNPVLELSDS GIRHSDTDQQ TR
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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
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Protein Description
AP1AR (Adaptor Protein 1 Cargo Recognition) is a key component in the cellular transport system, primarily involved in the sorting and trafficking of proteins within the endosomal-lysosomal pathway. Research into AP1AR has gained momentum given its critical role in various cellular processes, including endocytosis, receptor recycling, and membrane trafficking. Understanding the structure and function of AP1AR is essential for elucidating its mechanisms in cellular homeostasis and its implications in disease states, such as cancer and neurodegenerative disorders. Recent studies have demonstrated that alterations in AP1AR functionality can disrupt normal cellular transport and contribute to pathological conditions. Thus, reassembled or recombinant forms of AP1AR protein are being explored as tools to dissect its role in cellular signaling and trafficking pathways. The investigation of AP1AR through recombinant protein expression systems enables researchers to study its interactions with other proteins and its involvement in the formation of transport vesicles. These findings could reveal novel therapeutic targets and strategies for manipulating cellular transport mechanisms in disease contexts, highlighting the importance of AP1AR in both basic biology and potential clinical applications.











