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  • ERO1L Antibodies

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ERO1L Monoclonal Antibody (1G12E11), CoraLite® 594

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Protocols
Questions & Answers

Cite ERO1L Monoclonal Antibody (1G12E11), CoraLite® 594

  • Antibody Testing Data (2)
ERO1L Antibody in Immunohistochemistry (Paraffin) (IHC (P))
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ERO1L Antibody in Immunohistochemistry (Paraffin) (IHC (P))
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FIGURE: 1 / 2

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ERO1L Antibody (CL59467416100UL) in IHC (P)

Immunofluorescent analysis of (4% PFA) fixed human stomach cancer tissue using CoraLite 594 ERO1L antibody (Product # CL59467416100UL), Clone: 1G12E11 ) at dilution of 1:200. {{ $ctrl.currentElement.advancedVerification.fullName }} validation info. View more
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ERO1L Antibody in Immunohistochemistry (Paraffin) (IHC (P))
ERO1L Antibody in Immunohistochemistry (Paraffin) (IHC (P))
ERO1L Monoclonal Antibody (1G12E11), CoraLite® 594

Product Details

CL59467416100UL

Applications
Tested Dilution
Publications

Immunohistochemistry (Paraffin) (IHC (P))

1:200
-

Immunocytochemistry (ICC/IF)

1:50-1:500
-
Product Specifications

Species Reactivity

Human, Mouse, Rat

Host/Isotype

Mouse / IgG2b

Class

Monoclonal

Type

Antibody

Clone

1G12E11

Conjugate

CoraLite® 594 CoraLite® 594 CoraLite® 594
  • Unconjugated
  • CoraLite Plus 488
  • Request custom conjugation

Excitation/Emission Max

593/614 nm

Form

Liquid

Concentration

1 mg/mL

Purification

Protein A

Storage buffer

PBS, pH 7.3, with 0.5% BSA, 50% glycerol

Contains

0.05% ProClin 300

Storage conditions

-20°C, Avoid Freeze/Thaw Cycles, store in dark

Shipping conditions

Wet ice

Target Information

ERO1L (endoplasmic oxidoreductin-1-like protein) is localized in ER membrane as peripheral membrane protein on the lumenal side. Its association with ERP44 is essential for its retention in the ER and is unique in coupling oxygen reduction to de novo disulfides formation. The ERO1L enzyme is broadly distributed at low levels in several tissues with highest levels in the upper digestive tract and is stimulated by hypoxia via HIF-signaling. ERO1L generally exists as monomer, but has the ability to function as monomer or homodimer and interacts with PDILT. After translation, ERO1L gets n-glycosylated and the disulfide bonds constitute the redox-active center whereby the Cys-94/Cys-99 disulfide bond accepts an electron from P4HB followed by funneling the same to the active site disulfide Cys-394/Cys-397. ERO1L acts by oxidizing directly to P4HB/PDI isomerase through direct disulfide exchange and associates with ERP44. ERO1L is implicated in immunoglobulin folding, oxidative stress, release of unfolded cholera toxin from reduced P4HB/PDI upon Vibrio cholerae infection, and plays a key role in ER stress-induced CHOP-dependent apoptosis through inositol 1,4,5-trisphosphate receptor IP3R1 activation.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.

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Bioinformatics

Protein Aliases: Endoplasmic oxidoreductin-1-like protein; endoplasmic reticulum oxidation 1; Endoplasmic reticulum oxidoreductase alpha; Endoplasmic reticulum oxidoreductin-1-like protein; ero1; ERO1-L; ERO1-L-alpha; ERO1-like protein alpha; Global ischemia-induced protein 11; Oxidoreductin-1-L-alpha

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Gene Aliases: ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1A; Ero1alpha; ERO1L; ERO1LA; Giig11; UNQ434/PRO865

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UniProt ID: (Human) Q96HE7, (Mouse) Q8R180, (Rat) Q8R4A1

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Entrez Gene ID: (Human) 30001, (Mouse) 50527, (Rat) 171562

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Function(s)
protein disulfide isomerase activity protein binding protein disulfide oxidoreductase activity disulfide oxidoreductase activity oxidoreductase activity oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor peptide-methionine (S)-S-oxide reductase activity peptide-methionine (R)-S-oxide reductase activity methionine-R-sulfoxide reductase activity
Process(es)
protein folding transport apoptotic process 4-hydroxyproline metabolic process protein maturation by protein folding extracellular matrix organization endoplasmic reticulum unfolded protein response response to endoplasmic reticulum stress cell redox homeostasis brown fat cell differentiation chaperone mediated protein folding requiring cofactor release of sequestered calcium ion into cytosol oxidation-reduction process intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress response to reactive oxygen species cellular protein modification process response to temperature stimulus organ senescence cellular response to hypoxia
It has to be done as per old AB suggested Products section.
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