Analytical Data
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Gene name
GOLPH3
- Application
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Alternative Names
Coat protein GPP34 (Mitochondrial DNA absence factor) (MIDAS)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H4A6
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Expression Region
1-298aa
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Molecular Weight
39.8 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
GOLPH3 (Golgi phosphoprotein 3) is a Golgi-localized protein implicated in various cellular processes, including Golgi apparatus function, cell proliferation, and cancer biology. Understanding GOLPH3 has garnered considerable attention due to its overexpression in several types of cancer, such as breast, lung, and colorectal cancers, linking it to tumorigenesis and cancer progression. Research has shown that GOLPH3 plays a crucial role in regulating the mTOR (mammalian target of rapamycin) signaling pathway, which is vital for cell growth and metabolism. Furthermore, GOLPH3 is involved in the transport of glycoproteins and lipids from the Golgi apparatus to the plasma membrane, suggesting that it may contribute to the maintenance of cellular homeostasis and lipid metabolism. The investigation of GOLPH3's structure and function through recombinant protein studies enables researchers to elucidate its molecular mechanisms and interactions within various signaling pathways. By producing and characterizing recombinant GOLPH3, scientists aim to develop therapeutic strategies to target its aberrant activity in cancer. The ongoing studies on GOLPH3 not only provide insights into its biological roles but also hold potential for the development of innovative diagnostic and therapeutic approaches in oncology. Thus, GOLPH3 stands out as a significant focal point in the intersection of cell biology and cancer research, necessitating further exploration to unlock its full potential in clinical applications.
