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Merck
Összes fotó(3)

Fontos dokumentumok

HPA017861

Sigma-Aldrich

Anti-UNC45B antibody produced in rabbit

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

Szinonimák:

Anti-SMUNC45, Anti-UNC-45B, Anti-UNC45 homolog B

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352203
Human Protein Atlas-szám:
NACRES:
NA.41
konjugátum:
unconjugated
application:
IF
IHC
klón:
polyclonal
faj reaktivitás:
human
citations:
4
technika/technikák:
immunofluorescence: 0.25-2 μg/mL
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

technika/technikák

immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:50-1:200

immunogén szekvencia

GEDDDKVQNAAAGALAMLTAAHKKLCLKMTQVTTQWLEILQRLCLHDQLSVQHRGLVIAYNLLAADAELAKKLVESELLEILTVVGKQEPDEKKAEVVQTARECLIKCMDYGFI

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... UNC45B(146862)

Általános leírás

Unc-45 myosin chaperone B (UNC45B) is a muscle-specific chaperone which is expressed in the heart and skeletal muscles. It has an amino terminus which contains three tetratricopeptide repeat (TPR) motifs, a central region and a carboxyl terminal with a Unc-45, Cro1 and She4 (UCS) domain.

Immunogén

UNC45 homolog B recombinant protein epitope signature tag (PrEST)

Alkalmazás

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biokémiai/fiziológiai hatások

Unc-45 myosin chaperone B (UNC45B) takes part in the organization of the sarcomere and in myoblast fusion. It is trafficked to the A-band of sarcomeres under conditions of thermal stress and plays a role in myosin folding. Along with the general heat shock protein HSP90, UNC45B functions in myosin assembly.

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 APREST72666

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

Egyéni védőeszköz

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Paul J Bujalowski et al.
FEBS letters, 589(1), 123-130 (2014-12-02)
Molecular chaperones are commonly identified by their ability to suppress heat-induced protein aggregation. The muscle-specific molecular chaperone UNC-45B is known to be involved in myosin folding and is trafficked to the sarcomeres A-band during thermal stress. Here, we identify temperature-dependent
Doris Hellerschmied et al.
Nature communications, 9(1), 484-484 (2018-02-06)
Muscle development requires the coordinated activities of specific protein folding and degradation factors. UFD-2, a U-box ubiquitin ligase, has been reported to play a central role in this orchestra regulating the myosin chaperone UNC-45. Here, we apply an integrative in
Lars Hansen et al.
European journal of human genetics : EJHG, 22(11), 1290-1297 (2014-02-20)
Genome-wide linkage analysis, followed by targeted deep sequencing, in a Danish multigeneration family with juvenile cataract revealed a region of chromosome 17 co-segregating with the disease trait. Affected individuals were heterozygous for two potentially protein-disrupting alleles in this region, in
Jaakko I Lehtimäki et al.
The Journal of cell biology, 216(12), 4053-4072 (2017-10-22)
Contractile actomyosin bundles, stress fibers, are crucial for adhesion, morphogenesis, and mechanosensing in nonmuscle cells. However, the mechanisms by which nonmuscle myosin II (NM-II) is recruited to those structures and assembled into functional bipolar filaments have remained elusive. We report

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