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Key Documents

M9434

Sigma-Aldrich

Monoclonal Anti-Myelin Basic Protein (MBP) (36-50) antibody produced in rat

clone 14, tissue culture supernatant

Synonyme(s) :

Anti-MBP

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rat

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

tissue culture supernatant

Type de produit anticorps

primary antibodies

Clone

14, monoclonal

Contient

0.09% sodium azide

Espèces réactives

horse, chicken, human

Technique(s)

ELISA: suitable
immunofluorescence: suitable
immunohistochemistry: suitable

Isotype

IgG

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MBP(4155)

Description générale

Myelin basic protein (MBP) is part of the myelin sheath and is a calcium-dependent protein. It has six isoforms and the gene encoding it is localized on human chromosome 18q23.

Spécificité

Recognizes amino acids 36-50 of myelin basic protein.

Immunogène

bovine myelin basic protein.

Actions biochimiques/physiologiques

Myelin basic protein (MBP) associates with calmodulin and has been identified as an auto-antigen in multiple sclerosis (MS). It also inhibits the assembly of amyloid-β protein.

Notes préparatoires

Generated by somatic cell hybridization of NS0 myeloma cells with spleen cells from an outbred rat immunized with bovine myelin basic protein.

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


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Alexey Belogurov et al.
The Journal of biological chemistry, 289(25), 17758-17766 (2014-04-18)
The vast majority of cellular proteins are degraded by the 26S proteasome after their ubiquitination. Here, we report that the major component of the myelin multilayered membrane sheath, myelin basic protein (MBP), is hydrolyzed by the 26S proteasome in a
Neha Soni et al.
Frontiers in neurology, 11, 153-153 (2020-03-27)
Early loss of white matter microstructure integrity is a significant cause of long-term neurological disorders following traumatic brain injury (TBI). White matter abnormalities typically involve axonal loss and demyelination. In-vivo imaging tools to detect and differentiate such microstructural changes are
Frank Rattay et al.
PloS one, 8(11), e79256-e79256 (2013-11-22)
Our knowledge about the neural code in the auditory nerve is based to a large extent on experiments on cats. Several anatomical differences between auditory neurons in human and cat are expected to lead to functional differences in speed and
H K Palliser et al.
Neuroendocrinology, 96(1), 60-67 (2012-04-18)
Intra-uterine growth restriction (IUGR) is a significant in utero complication that can have profound effects on brain development including reduced myelination and deficits that can continue into adulthood. Progesterone increases oligodendrocyte proliferation and myelin expression, an action that may depend
Ekaterina Kuzina et al.
BioMed research international, 2014, 926394-926394 (2014-10-03)
We recently showed that myelin basic protein (MBP) is hydrolyzed by 26S proteasome without ubiquitination. The previously suggested concept of charge-mediated interaction between MBP and the proteasome led us to attempt to compensate or mimic its positive charge to inhibit

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