Analytical Data
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Gene name
PHA
- Application
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Alternative Names
PHA；C15orf1；LANP；MAPM；Acidic leucine-rich nuclear phosphoProtein 32 family member A
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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
P39687
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Expression Region
1-249aa
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AA Sequence
MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD
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Molecular Weight
28.5 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
Related Products
Protein Description
PHA (Polyhydroxyalkanoates) recombinant proteins have gained significant attention in recent years due to their biodegradability and potential applications in various fields such as medicine, agriculture, and environmental science. As a form of biopolymer, PHAs are produced by the fermentation of microbial organisms and serve as an eco-friendly alternative to conventional plastics. Research in this area focuses on utilizing genetic engineering techniques to enhance the production of PHA by introducing specific genes into host organisms such as bacteria, yeast, or plants. These recombinant proteins can facilitate improved metabolic pathways for more efficient PHA synthesis, leading to higher yields and better material properties. Furthermore, the ability to tailor the properties of PHAs by manipulating the genetic makeup opens new avenues for developing specialized materials with unique functionalities for targeted applications. As concerns over plastic pollution and environmental sustainability grow, the exploration of PHA recombinant proteins represents a promising frontier in the quest for innovative, sustainable solutions that harness biological processes for material production.
