Analytical Data
-
Gene name
GOPC
- Application
-
Alternative Names
GOPC;CAL;FIG;Golgi-associated PDZ and coiled-coil motif-containing Protein
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9HD26
-
Expression Region
2-462aa
-
AA Sequence
SAGGPCPAA AGGGPGGASC SVGAPGGVSM FRWLEVLEKE FDKAFVDVDL LLGEIDPDQA DITYEGRQKM TSLSSCFAQL CHKAQSVSQI NHKLEAQLVD LKSELTETQA EKVVLEKEVH DQLLQLHSIQ LQLHAKTGQS ADSGTIKAKL SGPSVEELER ELEANKKEKM KEAQLEAEVK LLRKENEALR RHIAVLQAEV YGARLAAKYL DKELAGRVQQ IQLLGRDMKG PAHDKLWNQL EAEIHLHRHK TVIRACRGRN DLKRPMQAPP GHDQDSLKKS QGVGPIRKVL LLKEDHEGLG ISITGGKEHG VPILISEIHP GQPADRCGGL HVGDAILAVN GVNLRDTKHK EAVTILSQQR GEIEFEVVYV APEVDSDDEN VEYEDESGHR YRLYLDELEG GGNPGASCKD TSGEIKVLQG FNKKAVTDTH ENGDLGTASE TPLDDGASKL DDLHTLYHKK SY
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
GOPC, or Golgi-associated PDZ and coiled-coil motif-containing protein, plays a crucial role in intracellular transport and protein sorting, particularly within the Golgi apparatus. Research has increasingly focused on GOPC due to its involvement in critical biological processes, including cell signaling, membrane trafficking, and the maintenance of Golgi structure. Alterations in GOPC expression and function have been implicated in various pathological conditions, such as cancer and neurodegenerative diseases, highlighting its potential as a therapeutic target. The study of GOPC recombinant proteins allows for a detailed investigation of its structural and functional properties, facilitating the understanding of its mechanism in cellular processes. This research is further driven by the necessity to develop specific inhibitors or modulators that can manipulate GOPC activity for potential clinical applications. Scientists employ techniques such as recombinant DNA technology and protein expression systems to produce GOPC in sufficient quantities for analysis. The insights gained from these studies not only expand our knowledge of GOPC’s roles in health and disease but also contribute to the broader field of cell biology and therapeutic development.
