Human Recombinant ORP150 protein, His Tag (V2LY-0526-LY5880)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant ORP150 protein, His Tag consist of Amino Acid: 695-994 and predicts a molecular mass of 35.2 kDa.
Molecule Mass
35.2 kDa
Sequence
Amino Acid: 695-994
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>97% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Hypoxia Up-Regulated 1
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.
Biological Process
Cellular response to hypoxia Source: ParkinsonsUK-UCL
Endoplasmic reticulum to Golgi vesicle-mediated transport Source: ParkinsonsUK-UCL
Negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway Source: Ensembl
Negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
Response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Response to ischemia Source: ParkinsonsUK-UCL
Cellular Location
Endoplasmic reticulum lumen
Involvement in disease
Immunodeficiency 59 and hypoglycemia (IMD59):
An autosomal recessive primary immunologic disorder characterized by combined immunodeficiency, granulocytopenia, B-cell and dendritic cell deficiency, recurrent septic infections of the respiratory tract, skin and mucous membranes, and disturbed glucose metabolism.

Wang, Z., Tan, C., Duan, C., Wu, J., Zhou, D., Hou, L., ... & Hou, X. (2023). FUT2-dependent fucosylation of HYOU1 protects intestinal stem cells against inflammatory injury by regulating unfolded protein response. Redox Biology, 60, 102618.

Wang, W., Jiang, X., Xia, F., Chen, X., Li, G., Liu, L., ... & Chen, C. (2023). HYOU1 promotes cell proliferation, migration, and invasion via the PI3K/AKT/FOXO1 feedback loop in bladder cancer. Molecular Biology Reports, 50(1), 453-464.

Pan, P. K., Wang, K. T., Nan, F. H., Wu, T. M., & Wu, Y. S. (2022). Red Algae “Sarcodia suieae” Acetyl-Xylogalactan Downregulate Heat-Induced Macrophage Stress Factors Ddit3 and Hyou1 Compared to the Aquatic Animal Model of Nile Tilapia (Oreochromis niloticus) Brain Arachidonic Acid Expression. International Journal of Molecular Sciences, 23(23), 14662.

Arab, F., Rezaei, N., Taheri, F., Kouhpeikar, H., Rayzan, E., Mirbeyk, M., ... & Ghadami, M. (2022). The Clinical and Molecular Assessment of Iranian Families with Severe Congenital Neutropenia, Identification of HYOU1 and SHOC2 as Potential Novel Gene Defects. Iranian Journal of Allergy, Asthma and Immunology, 21(3), 344-354.

Hao, A., Wang, Y., Zhang, X., Li, J., Li, Y., Li, D., ... & Sui, G. (2021). Long non-coding antisense RNA HYOU1-AS is essential to human breast cancer development through competitive binding hnRNPA1 to promote HYOU1 expression. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research, 1868(4), 118951.

Rao, S., Oyang, L., Liang, J., Yi, P., Han, Y., Luo, X., ... & Liao, Q. (2021). Biological function of HYOU1 in tumors and other diseases. OncoTargets and therapy, 1727-1735.

Liu, J., & Wang, Y. (2021). Long non-coding RNA KCNQ1OT1 facilitates the progression of cervical cancer and tumor growth through modulating miR-296-5p/HYOU1 axis. Bioengineered, 12(1), 8753-8767.

Wang, J. M., Jiang, J. Y., Zhang, D. L., Du, X., Wu, T., & Du, Z. X. (2021). HYOU1 facilitates proliferation, invasion and glycolysis of papillary thyroid cancer via stabilizing LDHB mRNA. Journal of Cellular and Molecular Medicine, 25(10), 4814-4825.

Lee, M., Song, Y., Choi, I., Lee, S. Y., Kim, S., Kim, S. H., ... & Seo, H. R. (2021). Expression of HYOU1 via reciprocal crosstalk between NSCLC Cells and HUVECs control cancer progression and chemoresistance in tumor spheroids. Molecules and Cells, 44(1), 50.

Li, X., Zhang, N. X., Ye, H. Y., Song, P. P., Chang, W., Chen, L., ... & Wang, N. N. (2019). HYOU1 promotes cell growth and metastasis via activating PI3K/AKT signaling in epithelial ovarian cancer and predicts poor prognosis. European Review for Medical & Pharmacological Sciences, 23(10).

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For research use only. Not intended for any clinical use.

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