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48-602MAG
Buffer Detection Kit for Magnetic Beads
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This Anti-Endorphin Antibody, β, clone 3-E7 is validated for use in ELISA, IH for the detection of Endorphin.
Key Applications
ELISA
Immunohistochemistry
Application Notes
ELISA Immunohistochemistry
Optimal working dilutions must be determined by end user.
Biological Information
Immunogen
Synthetic human beta-endorphin coupled with poly-lysine or thyroglobulin (Gramsch et al., 1983; Meo et al., 1983) (H-Tyr-Gly-Gly-Phe sequence).
Clone
3-E7
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
Host
Mouse
Specificity
The antibody reacts with the amino terminal H-Tyr-Gly-Gly-Phe sequence of human O-endorphin. Therefore, a high cross-reactivity with homologues of identical sequence, such as [Met]-enkephalin and [Leu]-enkephalin and a number of opioid peptides, occurs; the antibody also reacts with swine and camel O-endorphin. However, the antibody does not recognize human beta-lipotropin and N-acetyl-beta-endorphin (Gramsch et al., 1983; Meo et al., 1983; Herz et al., 1982).
This gene encodes a polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. There are eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. The encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary where four cleavage sites are used; adrenocorticotrophin, essential for normal steroidogenesis and the maintenance of normal adrenal weight, and lipotropin beta are the major end products. In other tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and beta-lipotropin peptides. Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described.
FUNCTION: SwissProt: P01189 # Beta-endorphin and Met-enkephalin are endogenous opiates. SIZE: 267 amino acids; 29424 Da TISSUE SPECIFICITY: ACTH and MSH are produced by the pituitary gland. PTM: Specific enzymatic cleavages at paired basic residues yield the different active peptides. & O-glycosylated; reducing sugar is probably N- acetylgalactosamine. DISEASE: SwissProt: P01189 # Defects in POMC may be associated with susceptibility to obesity [MIM:601665]. & Defects in POMC are the cause of pro-opiomelanocortinin deficiency [MIM:609734]. Affected individuals present early-onset obesity, adrenal insufficiency and red hair. SIMILARITY: SwissProt: P01189 ## Belongs to the POMC family.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Maintain at 2-8°C in undiluted aliquots for up to 6 months.
Binding characteristics of a monoclonal beta-endorphin antibody recognizing the N-terminus of opioid peptides. Gramsch, C, et al. J. Neurochem., 40: 1220-6 (1983)
1982
The present paper describes the isolation and characterization of a clone of hybrid myelomas (3-E7) secreting a mouse monoclonal antibody to beta-endorphin. An examination of its specificity against a series of human beta-lipotropin fragments and other opioid peptides revealed that the N-terminus portion of beta-endorphin is the determinant. Complete or almost complete cross-reactivity was obtained to methionine- and leucine-enkephalin, beta-lipotropin 60-65, and BAM 22; partial cross-reactivity was seen to dynorphin1-13 and alpha-neo-endorphin, whereas beta-lipotropin, alpha-N-acetyl-beta-endorphin, Des-Tyr1-beta-endorphin, in addition to a series of synthetic enkephalin derivatives, completely lacked cross-reactivity. The use of the monoclonal antibody in radioimmunoassay (RIA) for beta-endorphin resulted in a lower sensitivity related to respective polyclonal antibodies. An increase of 100% in tracer binding could, however, be obtained by use of beta-endorphin iodinated with its N-terminal tyrosine protected by coupling to an antibody. A solid-phase RIA was developed involving the internally 3H-labeled monoclonal antibody, which resulted in a 10-fold increase in sensitivity as compared with the homogenous RIA. These data indicate that for the binding to this antibody a tyrosine residue in position 61 is essential, and it thus recognizes a site that is of functional significance for many naturally occurring opioid peptides.
Monoclonal antibody to the message sequence Tyr-Gly-Gly-Phe of opioid peptides exhibits the specificity requirements of mammalian opioid receptors. Meo, T, et al. Proc. Natl. Acad. Sci. U.S.A., 80: 4084-8 (1983)
1982
Six myeloma cell hybrids producing antibodies to human beta-endorphin were isolated from a single mouse spleen. The monoclonal antibodies displayed different binding patterns with the antigen. We report the characterization of one antibody which recognizes the tetrapeptide Tyr-Gly-Gly-Phe representing the message sequence found at the NH2 terminus of all naturally occurring mammalian opioid peptides. Competition experiments in radioimmunoassay and immunohistochemistry show that the antibody fails to bind the beta-endorphin precursor beta-lipotrophin, does not discriminate among opioid peptides that share the same message sequence but have different COOH-terminal extensions, and does not react with pharmacologically inactive derivatives of beta-endorphin. The antibody recognition of the message sequence of natural opioid peptides is sensitive to those molecular changes that affect their receptor binding competence.
Opioid peptide-like immunoreactivity localized in GABAErgic neurons of rat neostriatum and central amygdaloid nucleus. Oertel, W H, et al. Life Sci., 33 Suppl 1: 73-6 (1983)
1982
Opioid peptide-like (OPL)-immunoreactivity and (the GABA-biosynthetic enzyme) glutamic acid decarboxylase-like (GAD)-immunoreactivity were localized in rat neostriatum and central amygdaloid nucleus (ACE) using a polyclonal sheep antiserum to rat brain GAD and a monoclonal mouse antibody to the N-terminus of beta-endorphin (3-E7) as primary antisera. PAP-immunohistochemistry revealed GAD-immunoreactivity in the majority of neurons in neostriatum and ACE. OPL-immunoreactivity was observed in numerous neurons in ACE, but only in few neostriatal nerve cells. In double immunofluorescence in the same section OPL- and GAD-immunoreactivity colocalized in few medium size cells in the neostriatum, but in numerous neurons in ACE. The existence of opioid peptide containing GABAergic neurons in ACE and neostriatum is demonstrated.
Characteristics of a monoclonal beta-endorphin antibody recognizing the N-terminus of opioid peptides. Herz, A, et al. Life Sci., 31: 1721-4 (1982)
1981
The properties of a mouse monoclonal antibody to beta-endorphin secreted by a clone of hybrid myelomas (3-E7) are described. The antibody displays virtually complete cross-reactivity to met-enkephalin and leu-enkephalin, but no cross-reactivity to beta-lipotropin, alpha-N-acetyl-beta-endorphin and des-Tyr1-beta-endorphin. Substantial cross-reactivity is seen with some other naturally occurring opioid peptides bearing the enkephalin sequence, such as dynorphin, alpha-neo-endorphin and BAM 22, but cross-reactivity is lacking in the case of certain synthetic enkephalin derivatives possessing a D-amino acid in position 2. The data indicate that for the binding of an antigen to the antibody the N-terminal tyrosine moiety is essential. The antibody recognizes, thus, a site which is of functional significance for the interaction of many naturally occurring opioid peptides with the opiate receptor.
