Goat ERO1A / ERO1L Polyclonal Antibody | anti-ERO1A antibody

Goat Polyclonal to Human ERO1A / ERO1L

Cat. Num. AAA243472

• Gene Names: ERO1L; ERO1A; ERO1-L; ERO1LA; ERO1-alpha; ERO1-L-alpha
• Reactivity: Bat, Gibbon, Dog, Gorilla, Human, Rabbit; Predicted Reactivity: Monkey, Mouse, Rat, Bovine, Horse, Pig (at least 90% immunogen sequence identity)
• Applications: Immunohistochemistry, Western Blot, ELISA
• Purity: Immunoaffinity Purified
• Synonyms: ERO1A / ERO1L; Polyclonal Antibody; Goat Polyclonal to Human ERO1A / ERO1L; Anti-ERO1A / ERO1L Antibody (Internal) IHC-plus; ERO1L; ERO1-like (S. cerevisiae); ERO1 (S. cerevisiae)-like; ERO1A; ERO1-alpha; ERO1-L-alpha; ERO1-like protein alpha; Oxidoreductin-1-L-alpha; ERO1-L; Human ERO1A; anti-ERO1A antibody

• Host: Goat
• Reactivity: Bat, Gibbon, Dog, Gorilla, Human, Rabbit; Predicted Reactivity: Monkey, Mouse, Rat, Bovine, Horse, Pig (at least 90% immunogen sequence identity)
• Clonality: Polyclonal
• Specificity: Human ERO1L.
• Purity/Purification: Immunoaffinity Purified
• Form/Format: Tris-buffered saline, pH 7.3, 0.5% BSA, 0.02% sodium azide
• Concentration: 0.5 mg/ml (varies by lot)
• Sequence Length: 468

• Applicable Applications for anti-ERO1A antibody: Immunohistochemistry (IHC - Paraffin), Western Blot (WB), ELISA (EIA)
• Application Notes: ELISA (1:32000), IHC-P (5 ug/ml), WB (0.1 - 0.3 ug/ml); Usage: Peptide ELISA: antibody detection limit dilution 1:32000. Western blot: Approx 70kD band observed in lysates of cell lines A431, HeLa, Jurkat (calculated MW of 54.4kD according to NP_055399.1). The observed molecular weight corresponds to the glycosy...
• Target Species: Human
• Immunogen Description: Synthetic peptide C-QSDEVPDGIKSASY from an internal region of human ERO1L (NP_055399.1). Percent identity by BLAST analysis: Human, Gorilla, Gibbon, Monkey, Elephant, Panda, Dog, Bat, Rabbit (100%); Marmoset, Mouse, Rat, Bovine, Horse, Pig (93%).
• Immunogen Type: Synthetic peptide
• Immunogen: ERO1A / ERO1L antibody was raised against synthetic peptide C-QSDEVPDGIKSASY from an internal region of human ERO1L (NP_055399.1). Percent identity by BLAST analysis: Human, Gorilla, Gibbon, Monkey, Elephant, Panda, Dog, Bat, Rabbit (100%); Marmoset, Mouse, Rat, Bovine, Horse, Pig (93%); Turkey, Platypus (86%).
• Antigen Modification: Internal
• Preparation and Storage: Short term 4 degree C, long term aliquot and store at -20 degree C, avoid freeze thaw cycles.

Immunohistochemistry (IHC)

(Anti-ERO1L antibody IHC of human small intestine. Immunohistochemistry of formalin-fixed, paraffin-embedded tissue after heat-induced antigen retrieval. Antibody concentration 5 ug/ml.)

Western Blot (WB)

(ERO1L antibody (0.3 ug/ml) staining of A431 lysate (35 ug protein/ml in RIPA buffer). Primary incubation was 1 hour. Detected by chemiluminescence.)

NCBI and Uniprot Product Information

• NCBI GI #: 7657069
• NCBI GeneID: 30001
• NCBI Accession #: NP_055399.1
• NCBI GenBank Nucleotide #: NM_014584.2
• UniProt Accession #: Q96HE7; Q7LD45; Q9P1Q9; Q9UKV6; A8K9X4; A8MYW1
• Molecular Weight: 54,393 Da
• NCBI Official Full Name: ERO1-like protein alpha
• NCBI Official Synonym Full Names: ERO1-like (S. cerevisiae)
• NCBI Official Symbol: ERO1L
• NCBI Official Synonym Symbols: ERO1A; ERO1-L; ERO1LA; ERO1-alpha; ERO1-L-alpha
• NCBI Protein Information: ERO1-like protein alpha; oxidoreductin-1-L-alpha; endoplasmic oxidoreductin-1-like protein
• UniProt Protein Name: ERO1-like protein alpha
• Protein Family: ERO1-like protein
• UniProt Gene Name: ERO1L
• UniProt Synonym Gene Names: ERO1-L; ERO1-L-alpha
• UniProt Entry Name: ERO1A_HUMAN

Uniprot Description

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; endoplasmic reticulum lumen

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: extracellular matrix organization and biogenesis; protein maturation via protein folding; protein folding; chaperone cofactor-dependent 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