Analytical Data
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Gene name
GOLPH3L
- Application
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Alternative Names
GLP3L_HUMAN; Golgi phosphoprotein 3-like; golph3l; GPP34-related protein; GPP34R
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H4A5
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Expression Region
1-285aa
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AA Sequence
MTTLTHRARR TEISKNSEKK MESEEDSNWE KSPDNEDSGD SKDIRLTLME EVLLLGLKDK EGYTSFWNDC ISSGLRGGIL IELAMRGRIY LEPPTMRKKR LLDRKVLLKS DSPTGDVLLD ETLKHIKATE PTETVQTWIE LLTGETWNPF KLQYQLRNVR ERIAKNLVEK GILTTEKQNF LLFDMTTHPV TNTTEKQRLV KKLQDSVLER WVNDPQRMDK RTLALLVLAH SSDVLENVFS SLTDDKYDVA MNRAKDLVEL DPEVEGTKPS ATEMIWAVLA AFNKS
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Molecular Weight
59.2 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
GOLPH3L, a member of the GOLPH family of proteins, has garnered increasing attention in the field of cellular biology and disease research. It is primarily involved in the regulation of Golgi integrity and function, playing a crucial role in maintaining the structure of this vital organelle. Emerging studies suggest that GOLPH3L is implicated in various cellular processes, including vesicle trafficking, protein sorting, and cell proliferation. Notably, its potential involvement in cancer progression has highlighted the need for comprehensive research on GOLPH3L. Abnormal expression levels of GOLPH3L have been linked to tumor growth and metastasis, indicating that it might serve as a biomarker for certain cancers. Researchers are now focused on the functional characterization of GOLPH3L, exploring its interactions with other cellular components and the underlying molecular mechanisms that govern its activity. The development of recombinant GOLPH3L proteins is essential for these studies, as they offer a controlled means to investigate the protein’s structure and function. By generating purified GOLPH3L through recombinant technology, scientists aim to elucidate its role in cellular processes and its potential as a therapeutic target. Understanding GOLPH3L's mechanisms may provide valuable insights into cancer biology and open avenues for novel treatment strategies aimed at targeting Golgi-associated pathways in tumor cells.
