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Merck
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HPA021004

Sigma-Aldrich

Anti-MYBPC1 antibody produced in rabbit

enhanced validation

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Szinonimák:

Anti-C-protein, skeletal muscle slow isoform, Anti-Myosin-binding protein C, slow-type, Anti-Slow MyBP-C

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
Human Protein Atlas-szám:
NACRES:
NA.41
konjugátum:
unconjugated
application:
IHC
klón:
polyclonal
faj reaktivitás:
human
citations:
7
technika/technikák:
immunohistochemistry: 1:50- 1:200

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

termékcsalád

Prestige Antibodies® Powered by Atlas Antibodies

Forma

buffered aqueous glycerol solution

faj reaktivitás

human

fejlettebb validálás

independent
orthogonal RNAseq
Learn more about Antibody Enhanced Validation

technika/technikák

immunohistochemistry: 1:50- 1:200

immunogén szekvencia

DWTLVETPPGEEQAKQNANSQLSILFIEKPQGGTVKVGEDITFIAKVKAEDLLRKPTIKWFKGKWMDLASKAGKHLQLKETFERHSRVYTFEMQIIKAKDNFAGNYRCEVTYKDKFDSCSFDLEVHESTGTTPN

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... MYBPC1(4604)

Általános leírás

The gene MYBPC1 (myosin-binding protein C, slow type) is mapped to human chromosome 12q23.2.

Immunogén

Myosin-binding protein C, slow-type recombinant protein epitope signature tag (PrEST)

Alkalmazás

Anti-MYBPC1 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige. In addition, the antibody has been used for immunocytochemistry.

Biokémiai/fiziológiai hatások

MYBPC1 (myosin-binding protein C, slow type) is a proteasomal substrate. It associates with myosin and titin, and is suggested to stabilize sarcomere structure. In addition, MYBPC1 interaction with myosin-S2 might be crucial for regulation of muscle contraction. In muscles, MTBPC1 association with myosin and MM-CK (muscle-type creatine kinase) controls energy homoeostasis. It is associated with distal arthrogryposis type I (DA1) and lethal congenital contractural syndrome type 4 (LCCS4). Mutation in MYBPC1 is cause of hypertrophic cardiomyopathy, linked with left ventricular dysfunction and dilation.

Tulajdonságok és előnyök

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Kapcsolódás

Corresponding Antigen APREST72729

Fizikai forma

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Jogi információk

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Jogi nyilatkozat

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Dokumentumtár megtekintése

Gabriele Tonni et al.
Congenital anomalies, 53(3), 137-140 (2013-01-30)
An early second-trimester prenatal ultrasound diagnosis of an arthrogryposis multiplex congenita-like syndrome associated with median clefts is reported. A molecular biological work-up was performed to search for a potentially overlapping syndrome and dysostosis. Autopsy and postmortem radiogram were performed to
Zhe Chen et al.
The Biochemical journal, 436(2), 437-445 (2011-03-24)
Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In
Christina A Gurnett et al.
Human molecular genetics, 19(7), 1165-1173 (2010-01-05)
Distal arthrogryposis type I (DA1) is a disorder characterized by congenital contractures of the hands and feet for which few genes have been identified. Here we describe a five-generation family with DA1 segregating as an autosomal dominant disorder with complete
Tetsuo Konno et al.
Journal of the American College of Cardiology, 41(5), 781-786 (2003-03-12)
We studied the clinical features of hypertrophic cardiomyopathy (HCM) caused by a novel mutation in the myosin binding protein-C (MyBP-C) gene in patients and family members of Japanese descent. Previous reports have demonstrated that the clinical features of HCM associated
Barak Markus et al.
Human mutation, 33(10), 1435-1438 (2012-05-23)
Autosomal recessive lethal congenital contractural syndrome (LCCS) is a severe form of neuromuscular arthrogryposis. We previously showed that this phenotype is caused in two unrelated inbred Bedouin tribes by different defects in the phosphatidylinositol pathway. However, the molecular basis of

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