癌症的基本特征包括细胞增殖、血管生成、迁移、凋亡逃避机制和细胞永生等。找到癌症发生过程中这些通路的关键标记物和对应的抗体用于检测至关重要。
为您推荐一个泛素化位点预测神器——泛素化分析工具，可以为您的蛋白的泛素化位点作出预测和评分。
细胞自噬受体图形绘图工具为你的蛋白的细胞受体结合位点作出预测和评分，识别结合到自噬通路中的蛋白是非常重要的，便于让我们理解自噬在正常生理、病理过程中的作用，如发育、细胞分化、神经退化性疾病、压力条件下、感染和癌症。
ERO1L Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
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Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q96HE7 |
| Other Accession | NP_055399.1 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 54393 Da |
| Antigen Region | 350-379 aa |
| Gene ID | 30001 |
|---|---|
| Other Names | ERO1-like protein alpha, ERO1-L, ERO1-L-alpha, 184-, Endoplasmic oxidoreductin-1-like protein, Oxidoreductin-1-L-alpha, ERO1L |
| Target/Specificity | This ERO1L antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 350-379 amino acids from the C-terminal region of human ERO1L. |
| Dilution | WB~~1:1000 IHC-P~~1:100~500 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ERO1L Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ERO1A (HGNC:13280) |
|---|---|
| Synonyms | ERO1L |
| Function | Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins (PubMed:29858230). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. |
| Cellular Location | Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Golgi apparatus lumen. Secreted. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8R4A1}. Note=The association with ERP44 is essential for its retention in the endoplasmic reticulum (PubMed:29858230). In neurons, it localizes to dendrites (By similarity). {ECO:0000250|UniProtKB:Q8R4A1, ECO:0000269|PubMed:29858230} |
| Tissue Location | Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin.
REFERENCES
Inaba, K., et al. EMBO J. 29(19):3330-3343(2010)
Appenzeller-Herzog, C., et al. EMBO J. 29(19):3318-3329(2010)
Swiatkowska, M., et al. J. Biol. Chem. 285(39):29874-29883(2010)
Chambers, J.E., et al. J. Biol. Chem. 285(38):29200-29207(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
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