Analytical Data
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Gene name
GOLGA7
- Application
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Alternative Names
GOLGA7;GCP16;Golgin subfamily A member 7
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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
Q7Z5G4
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Expression Region
1-137aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMRPQQAPVSGKVFIQRDYSSGTRCQFQ TKFPAELENRIDRQQFEETVRTLNNLYAEAEKLGGQSYLEGCLACLTAYT IFLCMETHYEKVLKKVSKYIQEQNEKIYAPQGLLLTDPIERGLRVIEITI YEDRGMSSGR
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Molecular Weight
18 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
GOLGA7, a member of the golgin family of proteins, plays a crucial role in the maintenance of the Golgi apparatus and intracellular trafficking. Recent studies have highlighted its involvement in various cellular processes, including protein sorting and organelle communication, which are essential for maintaining proper cellular function. The significance of GOLGA7 becomes particularly evident in the context of various diseases, including cancer, where its expression levels can be altered, potentially affecting tumor progression and metastasis. Researchers have increasingly focused on the recombinant form of GOLGA7 to better understand its structure-function relationships and to explore its potential as a therapeutic target. By producing GOLGA7 as a recombinant protein, scientists aim to investigate its biochemical properties, interaction with other cellular components, and role in Golgi-related pathways more comprehensively. Additionally, recombinant GOLGA7 can serve as a valuable tool for developing assays to screen for small molecules or peptides that may modulate its activity, offering novel avenues for therapeutic intervention. Overall, the study of recombinant GOLGA7 holds great promise for advancing our understanding of Golgi dynamics and its implications in health and disease.
