Analytical Data
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Gene name
ASPH
- Application
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Alternative Names
ASPH；BAH；Aspartyl/asparaginyl beta-hydroxylase
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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
Q12797
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Expression Region
75-270aa
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AA Sequence
FDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPDT
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Molecular Weight
38.2kDa
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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
ASPH (Asparaginyl Hydroxylase) is a crucial enzyme that plays a significant role in post-translational modifications of proteins, specifically in the hydroxylation of asparagine residues. The interest in ASPH has grown due to its involvement in key biological processes, including cell signaling, metabolism, and the regulation of various developmental pathways. Abnormal expression of ASPH has been linked to numerous pathological conditions, including cancer, where it contributes to tumor progression and metastasis by altering the function of specific signaling pathways. Given its importance in both normal physiology and disease states, researchers have focused on producing recombinant ASPH proteins to study their functional mechanisms and potential as therapeutic targets. The recombinant forms allow for high yields and purity, facilitating structural and functional analyses, as well as screening for inhibitors that could modulate its activity. These studies may pave the way for novel strategies in cancer treatment and other diseases associated with aberrant ASPH function, making it a significant subject of interest in biochemical and medical research.
