Recombinant Human ERp44 Protein (C-6His)

Name: Recombinant Human ERp44 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-2360NP
Availability: InStock

BL-2360NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Human ER Resident Protein 44 is produced by our Mammalian expression system and the target gene encoding Glu30-Asp402 is expressed with a 6His tag at the C-terminus.
Accession	Q9BS26
Synonym	Thioredoxin domain-containing protein 4; ER protein 44; KIAA0573; TXNDC4
Gene Background	Endoplasmic reticulum resident protein 44 (TXNDC4) is is a 406 amino acid protein that contains one thioredoxin domain. TXNDC4 mediates thiol-dependent retention in the early secretory pathway and forms mixed disulfides with substrate proteins through its conserved CRFS motif.It can inhibit the calcium channel activity of ITPR1.It may have a role in the control of oxidative protein folding in the endoplasmic reticulum.
Molecular Mass	44.2 KDa
Apmol Mass	50 KDa, reducing conditions
Formulation	Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 10% Glycerol, pH 7.5.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution
Storage	Store at ≤-70°C, stable for 6 months after receipt. Store at ≤-70°C, stable for 3 months under sterile conditions after opening. Please minimize freeze-thaw cycles.
Shipping	The product is shipped on dry ice/polar packs. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum.
Subcellular Location	Endoplasmic reticulum lumen.
Database References	HGNC: 18311 OMIM: 609170 KEGG: hsa:23071 STRING: 9606.ENSP00000262455 UniGene: Hs.154023

Gene Functions References

Endogenous ERp44 is O-glycosylated and secreted by human primary endometrial cells, suggesting possible pathophysiological roles of these processes. PMID: 25097228
findings indicated that overexpression of miR-101 could downregulate ERp44 PMID: 24804790
the decrease in 5-HT uptake rates of GDM trophoblast is the consequence of defective insulin signaling, which entraps SERT with ERp44 and impairs its glycosylation. PMID: 25512553
The ERp44 assembly control cycle couples secretion fidelity and efficiency downstream of the calnexin/calreticulin and BiP-dependent quality control cycles. PMID: 23685074
ERp44 together with Ero1-Lalpha plays an important role in disulfide formation of SERT, which may be a prerequisite step for the assembly of SERT molecules in oligomeric form. PMID: 22451649
contains a thioredoxin domain with a CRFS motif and is induced during ER stress PMID: 11847130
Ero1alpha and Ero1beta are retained in the endoplasmic reticulum by interactions with PDI and ERp44 PMID: 16677073
ERGIC-53 provides a platform that receives micro(2)L(2) subunits from the BiP-dependent checkpoint, assisting polymerization. In this process, ERp44 couples thiol-dependent assembly and quality control. PMID: 17805346
ERp44-mediated retention of FGE, indicating that noncovalent interactions between ERp44 and FGE are sufficient to mediate ER retention. PMID: 18178549
Study shows that SUMF1 interacts with protein disulfide isomerase (PDI) and ERp44, two thioredoxin family members residing in the early secretory pathway, and with ERGIC-53, a lectin that shuttles between the ER and the Golgi. PMID: 18508857
Crystal structure of ERp44 at a resolution of 2.6 A, is presented. PMID: 18552768

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.