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AB7821

Sigma-Aldrich

Anti-Collagen Type VI Antibody

serum, Chemicon®

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About This Item

UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Antikörperform

serum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Speziesreaktivität

human

Hersteller/Markenname

Chemicon®

Methode(n)

ELISA: suitable
immunohistochemistry: suitable

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... COL6A1(1291)

Spezifität

Human collagen type I <0.5%

Human collagen type II <0.5%

Human collagen type III <0.5%

Human collagen type IV <0.5%

Human collagen type V 5%

Human collagen type VI 100%

Human fibronectin <0.5%

Human albumin <0.5%

Human immunoglobulin <0.5%

Immunogen

Human placental collagen type VI

Anwendung

Anti-Collagen Type VI Antibody is an antibody against Collagen Type VI for use in ELISA, IH.
Immunohistochemistry: 1:10-1:40 dilution of reconstitute for indirect immunofluorescent staining of frozen tissue sections.

ELISA: 1:10,000 dilution of reconstitute for ELISA on human collagen type VI.

Optimal working dilutions must be determined by the end user.

Physikalische Form

Pooled antisera was cross-absorbed against immobilized human serum proteins and collagen types IV and V. The IgG fraction was then precipitated with ammonium sulfate and subsequently dialyzed. Lyophilized from 500μL of 10mM Na-phosphate, 150mM NaCl, pH 7.5 with 0.1% mannitol.

Lagerung und Haltbarkeit

Maintain lyophilized at -20°C for up to 12 months. Reconstitute with 500uL of distilled water or saline. Store reconstitute between 2 and 8°C for up to two months. Remove any insoluble material by microcentrifugation before use.

Rechtliche Hinweise

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Lagerklassenschlüssel

11 - Combustible Solids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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S San Martin et al.
Journal of tissue engineering and regenerative medicine, 7(1), 10-19 (2011-11-05)
Several studies have developed efficient oral mucosa constructs using different types of scaffold. However, the changes in the morphology and gene and protein expression profile that could occur in these artificial constructs remain unknown. This study compared the histology and
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PLoS neglected tropical diseases, 10(4), e0004599-e0004599 (2016-04-02)
The time-course of the pathological effects induced by the venom of the snake Bothrops asper in muscle tissue was investigated by a combination of histology, proteomic analysis of exudates collected in the vicinity of damaged muscle, and immunodetection of extracellular
Valentina Emmanuele et al.
Human molecular genetics, 24(3), 714-726 (2014-10-03)
A member of the four-and-a-half-LIM (FHL) domain protein family, FHL1, is highly expressed in human adult skeletal and cardiac muscle. Mutations in FHL1 have been associated with diverse X-linked muscle diseases: scapuloperoneal (SP) myopathy, reducing body myopathy, X-linked myopathy with
Xin Xu et al.
Developmental biology, 418(2), 242-247 (2016-09-01)
The pericellular matrix (PCM) is a component of the extracellular matrix that is found immediately surrounding individual chondrocytes in developing and adult cartilage, and is rich in the proteoglycan perlecan. Mutations in perlecan are the basis of several developmental disorders
Tyler Novak et al.
Advanced functional materials, 26(16), 2617-2628 (2016-06-28)
Biological tissues and biomaterials are often defined by unique spatial gradients in physical properties that impart specialized function over hierarchical scales. The structure and organization of these materials forms continuous transitional gradients and discrete local microenvironments between adjacent (or within)

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