Recombinant Human Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3 (ERGIC3) Protein (His-SUMO)

Name: Recombinant Human Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3 (ERGIC3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10220P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Endoplasmic Reticulum-Golgi Intermediate Compartment Protein 3 (ERGIC3) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y282
Target Symbol	ERGIC3
Synonyms	2310015B14Rik; AV318804; C20orf47; CGI 54; D2Ucla1; dJ477O4.2; DKFZp547A2190; Endoplasmic reticulum Golgi intermediate compartment protein 3; endoplasmic reticulum localized protein ERp43; Endoplasmic reticulum-Golgi intermediate compartment protein 3; ERGI3_HUMAN; ERGIC and golgi 3; ergic3; ERV46; NY BR 84; PRO0989; RP23-220D12.2; RP3-477O4.1; SDBCAG84; Serologically defined breast cancer antigen 84; Serologically defined breast cancer antigen NY BR 84; Serologically defined breast cancer antigen NY-BR-84
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGIPVSSEAERHELGKVEVTVFDPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSF
Expression Range	47-341aa
Protein Length	Partial
Mol. Weight	49.7kDa
Research Area	Transport
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Possible role in transport between endoplasmic reticulum and Golgi.
Subcellular Location	Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Note=Cycles between the endoplasmic reticulum and the Golgi.
Protein Families	ERGIC family
Database References	HGNC: 15927 KEGG: hsa:51614 STRING: 9606.ENSP00000349970 UniGene: Hs.472558

Gene Functions References

these data showed that knockdown of ERGIC3 triggers endoplasmic reticulum stress-induced autophagic cancer cell death PMID: 27588471
Results showed that miR-203a downregulation induced ERGIC3 overexpression in non-small cell lung cancer cells. PMID: 26177443
ERGIC3 may play an active role in the development and progression of lung cancer. PMID: 23374247
miR-490-3p modulates cell growth and epithelial to mesenchymal transition of hepatocellular carcinoma cells by targeting endoplasmic reticulum-Golgi intermediate compartment protein 3 (ERGIC3). PMID: 23212913
Plays important roles in cell growth and endoplasmic reticulum stress-induced cell death. PMID: 17020792

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.