Recombinant Human Hypoxia Up-Regulated Protein 1 (HYOU1) Protein (His)

Name: Recombinant Human Hypoxia Up-Regulated Protein 1 (HYOU1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00225P
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 Hypoxia Up-Regulated Protein 1 (HYOU1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	Q9Y4L1
Target Symbol	HYOU1
Synonyms	(150 kDa oxygen-regulated protein)(ORP-150)(170 kDa glucose-regulated protein)(GRP-170)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MVEEIGVELVVLDLPDLPEDKLAQSVQKLQDLTLRDLEKQEREKAANSLEAFIFETQDKLYQPEYQEVSTEEQREEISGKLSAASTWLEDEGVGATTVMLKEKLAELRKLCQGLFFRVEERKKWPERLSALDNLLNHSSMFLKGARLIPEMDQIFTEVEMTTLEKVINETWAWKNATLAEQAKLPATEKPVLLSKDIEAKMMALDREVQYLLNKAKFTKPRPRPKDKNGTRAEPPLNASASDQGEKVIPPAGQTEDAEPISEPEKVETGSEPGDTEPLELGGPGAEPEQKEQSTGQKRPL
Expression Range	695-994aa
Protein Length	Partial
Mol. Weight	37.8 kDa
Research Area	Cancer
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	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.