Mouse bone morphogenetic protein 9 ELISA Kit | BMP-9 elisa kit

Mouse bone morphogenetic protein 9 (BMP-9) ELISA Kit

Cat. Num. AAA283446

• Gene Names: ERO1A; ERO1L; ERO1-L; ERO1LA; Ero1alpha; ERO1-alpha; ERO1-L-alpha
• Reactivity: Mouse
• Synonyms: bone morphogenetic protein 9; Mouse bone morphogenetic protein 9 (BMP-9) ELISA Kit; BMP-9 elisa kit

• Reactivity: Mouse

• Samples: Serum, Plasma, Other biological fluids
• Assay Type: Sandwich
• Sample Volume: 1-200 uL
• Detection Wavelength: 450 nm
• Preparation and Storage: Store at 2-8 degree C.

Related Product Information for BMP-9 elisa kit

Principle of the Assay: This assay employs a two-site sandwich ELISA to quantitate ERO1L in samples. An antibody specific for ERO1L has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyERO1L present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for ERO1L is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of ERO1L bound in the initial step. The color development is stopped and the intensity of the color is measured.

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: endoplasmic reticulum oxidoreductase 1 alpha
• NCBI Official Symbol: ERO1A
• NCBI Official Synonym Symbols: ERO1L; ERO1-L; ERO1LA; Ero1alpha; ERO1-alpha; ERO1-L-alpha
• NCBI Protein Information: ERO1-like protein alpha
• UniProt Protein Name: ERO1-like protein alpha
• UniProt Gene Name: ERO1A
• UniProt Synonym Gene Names: ERO1-L; ERO1-L-alpha

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: EC 1.8.4.-; Oxidoreductase; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 14q22.1

Cellular Component: dendrite; endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; intracellular membrane-bound organelle; membrane

Molecular Function: disulfide oxidoreductase activity; oxidoreductase activity; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; protein binding; protein disulfide isomerase activity; protein disulfide oxidoreductase activity

Biological Process: 4-hydroxyproline metabolic process; brown fat cell differentiation; cell redox homeostasis; cellular protein modification process; cellular response to hypoxia; cellular response to oxidative stress; chaperone cofactor-dependent protein folding; endoplasmic reticulum unfolded protein response; extracellular matrix organization; organ senescence; protein folding; protein maturation via protein folding; release of sequestered calcium ion into cytosol; response to temperature stimulus