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Merck

SAB4200710

Sigma-Aldrich

Anti-Calponin antibody, Mouse monoclonal

clone hCP, purified from hybridoma cell culture

Synonym(e):

Anti-CNN-1, Anti-CNN-2

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100 μL
CHF 436.00

CHF 436.00


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100 μL
CHF 436.00

About This Item

UNSPSC-Code:
12352203
NACRES:
NA.41

CHF 436.00


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Antikörperform

purified from hybridoma cell culture

Qualitätsniveau

Antikörper-Produkttyp

primary antibodies

Klon

hCP, monoclonal

Form

buffered aqueous solution

Mol-Gew.

antigen ~34 kDa

Speziesreaktivität

bovine, monkey, human, rabbit, ferret, mouse, hamster, rat, canine, pig

Konzentration

~1 mg/mL

Methode(n)

immunoblotting: suitable
immunohistochemistry: 10-20 μg/mL using heat-retrieved formalin-fixed, paraffin-embedded human tonsil sections
immunoprecipitation (IP): suitable

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... CNN1(1264)

Allgemeine Beschreibung

Anti-Calponin antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the hCP hybridoma (also cites as CALP), produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mouse. Calponin (CNN) exists in three isoforms CNN1, CNN2 and CNN3. CNN2 gene is mapped to human chromosome 19p13.3. All three isoforms are expressed in smooth muscle. While CNN1 expression is confined only to smooth muscle, CNN2 and CNN3 are expressed in other cells including the neuronal tissue, fibroblast, myoblast and B lymphocyte. The three isoforms differ in the C-terminal region and comprise conserved actin-binding middle domain and a N-terminal calponin homology (CH) domain.

Spezifität

Monoclonal Anti-Calponin specifically recognizes smooth muscle Calponin.

Immunogen

human uterus smooth muscle extract

Anwendung

Anti-Calponin antibody, Mouse monoclonal may be used in:
  • immunoblotting
  • immunoprecipitation
  • immunohistochemistry

Biochem./physiol. Wirkung

Calponin is an F-actin, calmodulin, and tropomyosin binding protein that presents in both the cytoskeleton and contractile machinery of smooth muscle (SM) cells. The interaction of Calponin with actin is shown to inhibit myosin Mg-ATPase activity. The binding strength of calponin to tropomyosin is weakened in the presence of Ca2+. Calponin is involved in a variety of cellular processes including smooth muscle contraction, cell movement, shape change, angiogenesis, exocytosis and endocytosis. Monoclonal anti-Calponin can be used for the identification and localization of calponin in SM elements. Calponin levels may serve as a prognostic factor in hepatocellular carcinoma, renal cell carcinoma, osteosarcoma and melanoma.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Lagerung und Haltbarkeit

For continuous use, store at 2-8°C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Calponin isoforms CNN1, CNN2 and CNN3: regulators for actin cytoskeleton functions in smooth muscle and non-muscle cells
Liu R and Jin JP
Gene, 585(1), 143-153 (2016)
Calcium-dependent regulation of smooth muscle calponin by S100
Fujii T, et al.
Journal of Biochemistry, 116(1), 121-127 (1994)

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