Recombinant Human HYOU1 Protein (C-10His)

Name: Recombinant Human HYOU1 Protein (C-10His)
Brand: Beta LifeScience
SKU: BL-1973NP
Availability: InStock

BL-1973NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

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Product Overview

Description	Recombinant Human Hypoxia Up-regulated Protein 1 is produced by our Mammalian expression system and the target gene encoding Met695-Leu999 is expressed with a 10His tag at the C-terminus.
Accession	Q9Y4L1
Synonym	Hypoxia up-regulated protein 1; 150 kDa oxygen-regulated protein; ORP-150; 170 kDa glucose-regulated protein; GRP-170; HYOU1; ORP150
Gene Background	Hypoxia up-regulated protein 1(HYOU1) is a member of the heat shock protein 70 family. Seven members from four different heat shock protein (HSP) families were identified including HYOU1, HSPC1(HSP86), HSPA5(Bip), HSPD1(HSP60), and several isoforms of the two testis-specific HSP70 chaperones HSPA2 and HSPA1L. HYOU1 is highly expressed in many tissues, such as liver, pancreas, macrophages within aortic atherosclerotic plaques, and in breast cancers. HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. Suppression of HYOU1 is associated with accelerated apoptosis. It is suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor in vasiveness.
Molecular Mass	36 KDa
Apmol Mass	60-80 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
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	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target Function	Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. May play a role as a molecular chaperone and participate in protein folding.
Subcellular Location	Endoplasmic reticulum lumen.
Protein Families	Heat shock protein 70 family
Database References	HGNC: 16931 OMIM: 601746 KEGG: hsa:10525 STRING: 9606.ENSP00000384144 UniGene: PMID: 29448096 Findings establish a general function of Grp170 during ERAD and suggest that positioning this client-release factor at the retrotranslocation site may afford a mechanism to couple client release from BiP and retrotranslocation. PMID: 27030672 Data reveal that Grp170 participates in preparing mutant proinsulin for degradation while enabling wild-type proinsulin escape from the endoplasmic reticulum. PMID: 28028074 High ORP150 expression is associated with thyroid cancer. PMID: 26700459 Two NEFs, Grp170 and Sil1, trigger toxin release from BiP to enable successful retrotranslocation and clarify the fate of the toxin after it disengages from BiP. PMID: 25877869 Grp170 induces nucleotide exchange of BiP and releases SV40 virus from BiP, promoting SV40 ER-to-cytosol transport and infection. PMID: 25653441 HYOU1 also modulates vIL-6's ability to induce CCL2. PMID: 24920810 Here we show that Grp170 can bind directly to a variety of incompletely folded protein substrates in the endoplasmic reticulum, and as expected for a bona fide chaperone, it does not interact with folded secretory proteins. PMID: 24327659 inducible overexpression of ORP150, in ER stress conditions, exerts inhibitory effect on apoptosis and senescence in human breast carcinoma cells but not in normal fibroblasts PMID: 23757447 Data indicate that Grp170 (Lhs1 ortholog) coprecipitate with alphaENaC. PMID: 23645669 AICAR infusion enhanced ORP150 expression, resulting in the marked amelioration of hepatic ER stress and apoptosis PMID: 21296878 Report ORP-150 levels in autopsy tissue after hypoxia/ischemia events in term neonates. PMID: 20626887 ORP150 exerts cytoprotective effects in renal tubular epithelia subjected to I/R injury and suggest a key role for ER stress in the renal tubular response to acute renal failure PMID: 15240565 Hypoxia results in an enhancement of ORP 150 expression in several tumour cell lines. PMID: 16543725 These findings suggest that ORP150 is structurally and functionally well conserved in distant species PMID: 17131193 Our observations led to the hypothesis that ORP150 protects against MPTP/MPP(+)-induced neurotoxicity, and indicate the importance of the ER environment in maintaining the nigrostriatal pathways. PMID: 17330988 data indicate ORP150 inhibits oxLDL-induced apoptosis by blocking calcium signaling & apoptosis; calcium released from ER stores is inhibited by ORP150; ORP150 is expressed in advanced atherosclerotic lesions PMID: 18404158 The forced expression of ORP150 highlights its new protective role against oxLDL-induced ER stress and subsequent apoptosis PMID: 19106412 the increased expression of ORP150 is a factor which protects collagen against intracellular degradation induced by glucose deprivation. PMID: 19225868 The ORP150-precursor peptide complex can elicit a cytotoxic T-lymphocyte response through cross-presentation, as well as the CD4-positive T cell response by dendritic cells. PMID: 19812200

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.

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Recombinant Human HYOU1 Protein (C-10His)

Recombinant Human HYOU1 Protein (C-10His)

Product Overview

Target Details

FAQs