Rabbit Anti-OS9 Recombinant Antibody (
26H3) (V2LY-0725-LY1534)

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Tested Data
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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal
Rabbit
Clone
26H3
Application
ELISA, WB, IHC
Immunogen
A synthesized peptide derived from human OS9.
Host Species
Rabbit
Specificity
Human, Mouse
Antibody Isotype
IgG
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:500-1:2,000
IHC1:50-1:200

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

Format
Liquid
Buffer
PBS, glycerol
Preservative
Sodium azide
Concentration
Batch dependent
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.
More Infomation

Target

Full Name
OS9, Endoplasmic Reticulum Lectin
Entrez Gene ID
UniProt ID
Function
Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.
Biological Process
Endoplasmic reticulum unfolded protein responseIEA:InterPro
Negative regulation of retrograde protein transport, ER to cytosolManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Protein retention in ER lumenManual Assertion Based On ExperimentIDA:UniProtKB
Protein targetingIEA:Ensembl
Protein ubiquitinationManual Assertion Based On ExperimentIMP:UniProtKB
Response to endoplasmic reticulum stressManual Assertion Based On ExperimentIDA:UniProtKB
Retrograde protein transport, ER to cytosolManual Assertion Based On ExperimentIBA:GO_Central
Ubiquitin-dependent ERAD pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Ubiquitin-dependent protein catabolic processManual Assertion Based On ExperimentIMP:UniProtKB
Cellular Location
Endoplasmic reticulum lumen
PTM
Intramolecular disulfide bonds.
Isoform 1 and isoform 2 are N-glycosylated.

Frachon, N., Demaretz, S., Seaayfan, E., Chelbi, L., Bakhos-Douaihy, D., & Laghmani, K. (2024). AUP1 Regulates the Endoplasmic Reticulum-Associated Degradation and Polyubiquitination of NKCC2. Cells, 13(5), 389.

Erzurumlu, Y., Catakli, D., & Dogan, H. K. (2023). Circadian Oscillation Pattern of Endoplasmic Reticulum Quality Control (ERQC) Components in Human Embryonic Kidney HEK293 Cells. Journal of Circadian Rhythms, 21.

Li, P., Guo, Z., Feng, R., Wu, N., Zhong, X., Fang, Z., ... & Ge, J. (2022). Multi‐omics analysis reveals the regulation of SIRT6 on protein processing of endoplasmic reticulum to alleviate oxidative stress in endothelial cells. Clinical and Translational Medicine, 12(8).

Ninagawa, S., George, G., & Mori, K. (2021). Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins. Biochimica et biophysica acta (BBA)-General subjects, 1865(3), 129812.

Wen, Y., Zong, S., Liu, T., Du, P., Li, H., & Xiao, H. (2021). Tauroursodeoxycholic acid attenuates cisplatin-induced ototoxicity by inhibiting the accumulation and aggregation of unfolded or misfolded proteins in the endoplasmic reticulum. Toxicology, 453, 152736.

Shaukat, I., Bakhos‐Douaihy, D., Zhu, Y., Seaayfan, E., Demaretz, S., Frachon, N., ... & Laghmani, K. (2021). New insights into the role of endoplasmic reticulum‐associated degradation in Bartter Syndrome Type 1. Human Mutation, 42(8), 947-968.

Lemmer, I. L., Willemsen, N., Hilal, N., & Bartelt, A. (2021). A guide to understanding endoplasmic reticulum stress in metabolic disorders. Molecular metabolism, 47, 101169.

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

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