05-429
Anti-phospho-MBP Antibody, clone P12
clone P12, Upstate®, from mouse
Synonyma:
Anti-C76307, Anti-R75289, Anti-golli-mbp, Anti-jve, Anti-mld, Anti-shi
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Doporučené produkty
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
P12, monoclonal
species reactivity
vertebrates
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable
western blot: suitable
isotype
IgG
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
phosphorylation (pThr98)
Gene Information
human ... MBP(4155)
General description
Myelin basic protein (MBP) is the major extrinsic membrane protein of central nervous system and has a molecular mass of 21.5 kDa. MBP is believed to be important in the process of myelination of nerves in the central nervous system (CNS). MBP was initially sequenced in 1979 after isolation from myelin membranes. Since that time, knockout mice deficient in MBP have been developed which showed decreased amounts of CNS myelination and a progressive disorder characterized by tremors, seizures, and early death. The gene for MBP is on chromosome 18; the protein localizes to the CNS and to various cells of the hematopoietic system.
The pool of MBP in the central nervous system is very diverse, with several splice variants being expressed and a large number of post-translational modifications on the protein, which include phosphorylation, methylation, deamidation and citrullination. MBP phosphorylation at Threonine 125 is a complex regulatory process that modulates the contribution of MBP to the stability of the Myelin sheath.
Interest in MBP has centered on its role in demyelinating diseases, particularly multiple sclerosis (MS). Several studies have shown a role for antibodies against MBP in the pathogenesis of MS. Some studies have linked a genetic predisposition to MS to the MBP gene, though a majority have not.
The pool of MBP in the central nervous system is very diverse, with several splice variants being expressed and a large number of post-translational modifications on the protein, which include phosphorylation, methylation, deamidation and citrullination. MBP phosphorylation at Threonine 125 is a complex regulatory process that modulates the contribution of MBP to the stability of the Myelin sheath.
Interest in MBP has centered on its role in demyelinating diseases, particularly multiple sclerosis (MS). Several studies have shown a role for antibodies against MBP in the pathogenesis of MS. Some studies have linked a genetic predisposition to MS to the MBP gene, though a majority have not.
Specificity
Recognizes MBP phosphorylated at Threonine 98; Some preparations of MBP contain basal levels of phosphorylated MBP, which are detected by the pMBP antibody.
Immunogen
Synthetic peptide corresponding to the human myelin basic protein sequence phosphorylated at Thr98 and coupled to tuberculin
Application
Detect phospho-MBP using this Anti-phospho-MBP Antibody, clone P12 validated for use in EA & WB.
Research Category
Signaling
Signaling
Research Sub Category
MAP Kinases
MAP Kinases
Quality
routinely evaluated by immunoblot on MBP phosphorylated by MAP Kinase 2/Erk2, active (Catalog #14-173)
Target description
33 kDa
Physical form
Format: Purified
Protein A purified
Protein G Purified immunoglobulin in Protein A Purified immunoglobulin in 30% glycerol, PBS, and 0.09% sodium azide as a preservative.
Storage and Stability
Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Analysis Note
Control
Mouse brain extract or rat brain extract
Mouse brain extract or rat brain extract
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
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.
Ještě jste nenalezli správný produkt?
Vyzkoušejte náš produkt Nástroj pro výběr produktů.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Osvědčení o analýze (COA)
Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.
Již tento produkt vlastníte?
Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.
Romina Giacometti et al.
Pest management science, 72(8), 1585-1594 (2015-11-26)
Southern green stink bugs (Nezara viridula L.) invade field-grown soybean crops, where they feed on developing seeds and inject phytotoxic saliva, which causes yield reduction. Although leaf responses to herbivory are well studied, no information is available about the regulation
Cefan Zhou et al.
Cell communication and signaling : CCS, 17(1), 105-105 (2019-08-24)
Breast cancer is a life-threatening disease in females and the leading cause of mortality among the female population, presenting huge challenges for prognosis and treatment. ITM2A is a member of the BRICHOS superfamily, which are thought to have a chaperone
Identification of a mitogen-activated protein kinase site in human myelin basic protein in situ.
Yon, M, et al.
Journal of Neuroimmunology, 65, 55-59 (1996)
J W Mandell et al.
Analytical biochemistry, 293(2), 264-268 (2001-06-12)
We describe a versatile intracellular reporter of ERK/MAP kinase activity: a cDNA construct, pGFP.MBP, encoding amino acids 85-144 of the human myelin basic protein fused to the C-terminus of an enhanced green fluorescent protein (GFP). The fused fragment of myelin
Lingfeng Liu et al.
Genes & cancer, 3(1), 23-36 (2012-08-16)
Regulation of Myc protein abundance is critical for normal cell growth as evidenced by the fact that deregulated Myc expression is a hallmark of many cancers. One of several important mechanisms that control Myc levels involves its phosphorylation-dependent proteolysis. Previous
Náš tým vědeckých pracovníků má zkušenosti ve všech oblastech výzkumu, včetně přírodních věd, materiálových věd, chemické syntézy, chromatografie, analytiky a mnoha dalších..
Obraťte se na technický servis.