Recombinant Human Endoplasmic Reticulum Resident Protein 29 (ERP29) Protein (GST)

Name: Recombinant Human Endoplasmic Reticulum Resident Protein 29 (ERP29) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03600P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Endoplasmic Reticulum Resident Protein 29 (ERP29) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P30040
Target Symbol	ERP29
Synonyms	ERP29; C12orf8; ERP28Endoplasmic reticulum resident protein 29; ERp29; Endoplasmic reticulum resident protein 28; ERp28; Endoplasmic reticulum resident protein 31; ERp31
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	PLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSASSDDLLVAEVGISDYGDKLNMELSEKYKLDKESYPVFYLFRDGDFENPVPYTGAVKVGAIQRWLKGQGVYLGMPGCLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAF
Expression Range	40-251aa
Protein Length	Partial
Mol. Weight	51.0kDa
Research Area	Signal Transduction
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	Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
Subcellular Location	Endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Database References	HGNC: 13799 OMIM: 602287 KEGG: hsa:10961 STRING: 9606.ENSP00000261735 UniGene: PMID: 28874138 The anti-aggregation peptide ReACp53 significantly decreased ERP29 expression and suppressed the chemoresistant effect. These findings highlight a role of ERP29 in the acquired chemoresistance of cancer cells expressing the aggregating p53 mutant Arg282Trp. PMID: 28534505 Results of further analyses by using a CNX mutant imply that ERp29 and ERp57 recognize the same domain of CNX, whereas the mode of interaction with CNX might be somewhat different between them. PMID: 28456374 High ERP29 expression is associated with pancreatic ductal adenocarcinomas. PMID: 26887611 our studies prove a novel function of ERp29\MGMT in cancer cell survival against radiation. Targeting ERp29\MGMT axis may be useful for providing better treatment efficacy in combination with radiotherapy in breast cancer. PMID: 26420420 Endoplasmic reticulum protein 29 attenuates CSE-induced ER stress and enhances cell viability and barrier integrity of RPE cells, and therefore may act as a protective mechanism for RPE survival and activity. PMID: 26431474 CLIC4, ERp29, and Smac/DIABLO integrated into a novel panel based on cancer stem-like cells in association with metastasis stratify the prognostic risks of colorectal cancer. PMID: 24916695 overexpression of ERp29 may play a key role in apoptosis in HTR-8/SVneo cells via activation of p38, which may participate in the pathogenesis of intrahepatic cholestasis of pregnancy PMID: 24780196 ERp29 directs ENaC toward the Golgi, where it undergoes cleavage during its biogenesis and trafficking to the apical membrane. PMID: 24944201 Apoptosis related proteins ERp29, PRDX6 and MPO were differentially expressed in placentas of pregnant women with intrahepatic cholestasis and in healthy pregnant women. PMID: 24391750 S1P1 overexpression or ERp29 absence is related to the carcinogenesis and progression, and may be potential biomarkers for early detection of gallbladder adenocarcinoma. PMID: 23558074 ERp29 is a novel molecule that regulates MET and epithelial cell integrity in breast cancer cells. PMID: 22543584 Overexpression of ERp29 increases the radioresistance in nasopharyngeal carcinoma. PMID: 21479953 Suggest that ERp29 associates with radioresistance in nasopharyngeal carcinoma and may be potential biomarker for predicting response to radiotherapy. PMID: 22160175 Eurycomanone affects the transcription of Erp28, annexin 1 and prohibitin resulting in reduced expression of these proteins. PMID: 21903368 interplay between p38 phosphorylation and p58(IPK) upregulation has key roles in modulating ERp29-induced cell-growth arrest and survival PMID: 22064321 ERp29 is a 4PBA-regulated ER chaperone that regulates WT-CFTR biogenesis and can promote DeltaF508-CFTR trafficking in CF epithelial cells PMID: 21525008 Results identify ERp29 as a novel regulator of PERK and provide evidence for the role of ER resident factors in the regulation of chemotherapeutic efficacy. PMID: 21419175 High expression of ERp29 inversely correlates to tumor progression. PMID: 20920593 Expression and tissue distribution of ERp29 [review] PMID: 12362325 ERp29 is an unusual redox-inactive member of the thioredoxin family [review] PMID: 16677078 ERP29 is expressed in a subset of basal-cell carcinoma of the skin, with the infiltrating carcinomas exhibiting the highest incidence of immunopositivity. PMID: 17012915 Results found that ERp29 comprises significant alpha-helical structure. PMID: 17073718 mutants of the D-domain of ERp29 prevent transport of a substrate protein (Pipe) in a manner consistent with the presence of a discrete, conserved peptide binding site in the D-domain PMID: 17296603 ERp29-activated polyomavirus perforates the physiologically relevant ER membrane, an event that likely initiates viral penetration. PMID: 17881435 lactating mammary glands were expressing ERp29 while the resting glands did not PMID: 18395818 there are two putative peptide binding sites of ERp29 and different processing activity of the human and Drosophila proteins in vivo does not stem from differences in peptide binding properties. PMID: 19084538 The level of ER protein 29 (ERp29) was shown to be decreased in the CK19-expressing BT549 breast cancer cell line. PMID: 19265690 This supports a new role for ERp29 as a chaperone that helps stabilize monomeric Cx43 to enable oligomerization to occur in the Golgi apparatus. PMID: 19321666 ERp29 is a novel regulator leading to cell growth arrest and cell transition from a proliferative to a quiescent state. PMID: 19770839

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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.