ELISA/assay

Human ERO1 like protein Alpha (ERO1L) ELISA Kit

MBS7247929

48-Strip-Wells

440 USD

ELISA Kit

Human ERO1 like protein Alpha (ERO1L) ELISA Kit

[ERO1 like protein Alpha (ERO1L)]

[ERO1-like protein alpha; ERO1-like protein alpha; ERO1-like protein alpha; ERO1-L; ERO1-L-alpha; oxidoreductin-1-L-alpha; endoplasmic oxidoreductin-1-like protein; ERO1-like (S. cerevisiae); Endoplasmic oxidoreductin-1-like protein; Oxidoreductin-1-L-alpha]

[ERO1L]

[ERO1L; ERO1L; ERO1A; ERO1LA; ERO1-alpha; UNQ434/PRO865; ERO1-L; ERO1-L-alpha]

ERO1A_HUMAN

Human

This assay has high sensitivity and excellent specificity for detection of ERO1L. No significant cross-reactivity or interference between ERO1L and analogues was observed. NOTE: Limited by current skills and knowledge, it is impossible for us to complete the cross-reactivity detection between ERO1L and all the analogues, therefore, cross reaction may still exist in some cases.

Store all reagents at 2-8 degree C.

Typical Standard Curve/Testing Data

Samples: Serum, plasma, Cell Culture Supernatants, body fluid and tissue homogenate. Assay Type: Competitive. Detection Range: 1.0-25ng/mL. Sensitivity: 0.1ng/mL

Intended Uses: This ERO1L ELISA kit is a 1.5 hour solid-phase ELISA designed for the quantitative determination of Human ERO1L. This ELISA kit for research use only, not for therapeutic or diagnostic applications!. Principle of the Assay: ERO1L ELISA kit applies the competitive enzyme immunoassay technique utilizing a polyclonal anti-ERO1L antibody and an ERO1L-HRP conjugate. The assay sample and buffer are incubated together with ERO1L-HRP conjugate in pre-coated plate for one hour. After the incubation period, the wells are decanted and washed five times. The wells are then incubated with a substrate for HRP enzyme. The product of the enzyme-substrate reaction forms a blue colored complex. Finally, a stop solution is added to stop the reaction, which will then turn the solution yellow. The intensity of color is measured spectrophotometrically at 450nm in a microplate reader. The intensity of the color is inversely proportional to the ERO1L concentration since ERO1L from samples and ERO1L-HRP conjugate compete for the anti-ERO1L antibody binding site. Since the number of sites is limited, as more sites are occupied by ERO1L from the sample, fewer sites are left to bind ERO1L-HRP conjugate. A standard curve is plotted relating the intensity of the color (O.D.) to the concentration of standards. The ERO1L concentration in each sample is interpolated from this standard curve.

7657069

NP_055399.1

NM_014584.1

54,393 Da

Cellular Responses To Stress Pathway (645258); Detoxification Of Reactive Oxygen Species Pathway (941400); Insulin Processing Pathway (105903); Metabolism Of Proteins Pathway (106230); Peptide Hormone Metabolism Pathway (771603); Protein Processing In Endoplasmic Reticulum Pathway (167325); Protein Processing In Endoplasmic Reticulum Pathway (167190); Vibrio Cholerae Infection Pathway (83101); Vibrio Cholerae Infection Pathway (513)

ERO1L: 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. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Belongs to the EROs family. Protein type: Secreted, signal peptide; EC 1.8.4.-; Oxidoreductase; Secreted. Chromosomal Location of Human Ortholog: 14q22.1. Cellular Component: endoplasmic reticulum membrane; intracellular membrane-bound organelle; membrane; endoplasmic reticulum lumen; endoplasmic reticulum. Molecular Function: protein binding; protein disulfide oxidoreductase activity; protein disulfide isomerase activity; oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor. Biological Process: protein maturation via protein folding; extracellular matrix organization and biogenesis; chaperone cofactor-dependent protein folding; protein folding; unfolded protein response; protein modification process; response to temperature stimulus; response to reactive oxygen species; cellular protein metabolic process; 4-hydroxyproline metabolic process; cell redox homeostasis; release of sequestered calcium ion into cytosol; brown fat cell differentiation

48-Strip-Wells

440 USD

96-Strip-Wells

640

5x96-Strip-Wells

2895

10x96-Strip-Wells

5415