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Key Documents

AV48247

Sigma-Aldrich

Anti-SEP15 antibody produced in rabbit

affinity isolated antibody

Synonyme(s) :

Anti-Selenoprotein 15 kDa

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

15 kDa

Espèces réactives

mouse, rat, pig, human

Concentration

0.5 mg - 1 mg/mL

Technique(s)

western blot: suitable

Numéro d'accès NCBI

Numéro d'accès UniProt

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... SEP15(9403)

Catégories apparentées

Description générale

SEP15 is a selenoprotein that regulates the unfolded protein response. It is modulated by ER stresses. SEP15 variations have been linked to the risk of lung cancer.
Rabbit Anti-SEP15 antibody recognizes bovine, zebrafish, pig, human, mouse, rat, and canine SEP15.

Immunogène

Synthetic peptide directed towards the middle region of human SEP15

Application

Rabbit Anti-SEP15 antibody is suitable for western blot applications at a concentration of 1μg/ml.

Actions biochimiques/physiologiques

SEP15 is a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding. The gene that encodes the protein is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3′ UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Studies in mouse suggest that this selenoprotein may have redox function and may be involved in the quality control of protein folding. This gene is localized on chromosome 1p31, a genetic locus commonly mutated or deleted in human cancers. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.

Séquence

Synthetic peptide located within the following region: SDKPKLFRGLQIKYVRGSDPVLKLLDDNGNIAEELSILKWNTDSVEEFLS

Forme physique

Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.

Clause de non-responsabilité

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.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Vyacheslav M Labunskyy et al.
Biochemistry, 48(35), 8458-8465 (2009-08-05)
The accumulation of misfolded proteins in the endoplasmic reticulum (ER) results in activation of signaling pathways collectively known as the unfolded protein response (UPR). The UPR promotes adaptation of cells to ER stress by transient inhibition of protein translation and
Ewa Jablonska et al.
European journal of nutrition, 47(1), 47-54 (2008-02-02)
Selenium (Se) is a trace element suggested to act chemopreventive in lung cancer. The mechanism by which Se suppresses tumour development may be associated with some of the functions of selenoproteins, including 15 kDa selenoprotein (Sep15). This protein exhibits antioxidant
Mengdi Li et al.
Placenta, 55, 81-89 (2017-06-19)
Selenocysteine insertion binding protein 2 (SECISBP2) plays a vital role in selenocysteine incorporation into selenoprotein in many creatures. However, the impact of SECISBP2 in development of trophoblast cells remains unclear. The aim of this study was to investigate the roles

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