Analytical Data
-
Gene name
ERGIC2
- Application
-
Alternative Names
ERGIC2; ERV41; PTX1; CDA14; Endoplasmic reticulum-Golgi intermediate compartment protein 2
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96RQ1
-
Expression Region
1-215aa
-
AA Sequence
MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVSLIAFTTMALLTIMEFSVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMFASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGHLYVNKVAGNFHITVGQFHILVVMHIWQHLSTMNLTIFLIE
-
Molecular Weight
51 kDa
-
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
ERGIC2, or ER-Golgi intermediate compartment protein 2, is an essential component of the secretory pathway, particularly involved in the transport between the endoplasmic reticulum (ER) and the Golgi apparatus. The study of ERGIC2 has gained traction due to its significant role in protein sorting and trafficking, which are critical processes for maintaining cellular homeostasis and function. Dysregulation of these processes can contribute to various diseases, including neurodegenerative disorders and certain types of cancer. Recent research has focused on understanding the molecular mechanisms underlying ERGIC2's function and its interactions with other cellular components, such as coat protein complexes and molecular chaperones. These investigations utilize advanced techniques, including cryo-electron tomography and live-cell imaging, to visualize ERGIC2 dynamics within the cellular context. Additionally, studies have explored the potential of ERGIC2 as a biomarker for specific pathologies and its implications in therapeutic strategies aimed at restoring normal cellular transport mechanisms. The ongoing exploration of ERGIC2 not only enhances our understanding of the fundamental aspects of intracellular trafficking but also positions this protein as a potential target for drug development in diseases linked to protein misfolding and transport defects.
