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| Cat.No | ACP18506 | Target Name | OS9 |
|---|---|---|---|
| Target Synonyms | Amplified in osteosarcoma 9; amplified in osteosarcoma; ERLEC2; OS-9 ; Os9; OS9_HUMAN; Osteosarcoma amplified 9 endoplasmic reticulum lectin; Protein OS-9 | Form | Lyophilized powder |
| Expression System | Custom Production. Please inquire and provide the desire expression system. | Expression Range | 26-667 |
| Protein Length | Full Length of Mature Protein | Purity | >85% (SDS-PAGE) |
| Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q13438 |
|---|
Uniprot Id
Q13438
Target Species
Human
Target Name
OS9
Target Full Name
Protein OS-9
Target 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.
Target Subcellular Location
Endoplasmic reticulum lumen.
Target Protein Families
OS-9 family
Target Tissue Specificity
Ubiquitously expressed. Found as well in all tumor cell lines analyzed, amplified in sarcomas. Highly expressed in osteosarcoma SJSA-1 and rhabdomyosarcoma Rh30 cell lines. Isoform 2 is the major isoform detected in all cell types examined.
Target Synonyms
Amplified in osteosarcoma 9; amplified in osteosarcoma; ERLEC2; OS-9 ; Os9; OS9_HUMAN; Osteosarcoma amplified 9 endoplasmic reticulum lectin; Protein OS-9
Target Background
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.
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