Analytical Data
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Gene name
ACPP
- Application
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Alternative Names
ACPP；ACPP；Prostatic acid phosphatase
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Species
Human
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Source
E. coli
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Tag
His tag C-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P15309
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Expression Region
33 -386aa
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AA Sequence
KELKFVTLVF RHGDRSPIDT FPTDPIKESS WPQGFGQLTQ LGMEQHYELG EYIRKRYRKF LNESYKHEQV YIRSTDVDRT LMSAMTNLAA LFPPEGVSIW NPILLWQPIP VHTVPLSEDQ LLYLPFRNCP RFQELESETL KSEEFQKRLH PYKDFIATLG KLSGLHGQDL FGIWSKVYDP LYCESVHNFT LPSWATEDTM TKLRELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILNHMK RATQIPSYKK LIMYSAHDTT VSGLQMALDV YNGLLPPYAS CHLTELYFEK GEYFVEMYYR NETQHEPYPL MLPGCSPSCP LERFAELVGP VIPQDWSTEC MTTNSHQGTE DSTDHHHHHH
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Molecular Weight
42 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
ACPP, or Acyl-CoA-binding protein, plays a crucial role in lipid metabolism and cellular signaling by binding long-chain acyl-CoA esters. Recent studies have highlighted its significance in various physiological processes, including energy homeostasis, inflammation, and cellular stress responses. The reconstitution of ACPP into recombinant protein forms has become a focus of research due to its potential applications in drug development and disease treatment, particularly in metabolic disorders and obesity-related conditions. Understanding the structure-function relationship of ACPP through protein engineering and recombinant techniques enables researchers to characterize its binding properties and interactions with different acyl-CoA substrates. This deeper insight can elucidate the molecular mechanisms underlying ACPP's involvement in metabolic pathways and might offer novel therapeutic targets. Moreover, as ACPP has been shown to influence cellular signaling cascades, studying its recombinant forms could provide valuable information on its role in cancer biology and other diseases where lipid metabolism is disrupted. The investigation into ACPP's functionality through reconstitution not only expands our knowledge of lipid-mediated cellular processes but also opens avenues for innovative strategies in treating illnesses where lipid dysregulation is a key factor.
