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Rabbit Anti-OS9 Recombinant Antibody (CBXO-0142) (CBMAB-O0095-CQ)

This product is a rabbit antibody that recognizes OS9. The antibody CBXO-0142 can be used for immunoassay techniques such as: WB, IP, IHC-P, ICC.
See all OS9 antibodies

Summary

Host Animal
Rabbit
Specificity
Mouse, Rat, Human
Clone
CBXO-0142
Antibody Isotype
IgG
Application
WB, IP, IHC-P, ICC

Basic Information

Specificity
Mouse, Rat, Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
OS9, Endoplasmic Reticulum Lectin
Introduction
This gene encodes a protein that is highly expressed in osteosarcomas. This protein binds to the hypoxia-inducible factor 1 (HIF-1), a key regulator of the hypoxic response and angiogenesis, and promotes the degradation of one of its subunits. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.
Entrez Gene ID
Human10956
Mouse216440
Rat362891
UniProt ID
HumanQ13438
MouseQ8K2C7
RatQ5RKH6
Alternative Names
OS9, Endoplasmic Reticulum Lectin; Osteosarcoma Amplified 9, Endoplasmic Reticulum Lectin; Endoplasmic Reticulum Lectin 2; Amplified In Osteosarcoma 9; Erlectin 2; Osteosarcoma Amplified 9, Endoplasmic Reticulum Associated Protein; Protein OS-9; ERLEC2; OS-9
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.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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