HU COLLAGEN VI; MS X-100UL

Code: MAB1944 D2-231

Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

This Anti-Collagen Type VI Antibody, clone 3C4 is validated for use in Dot Blot, Electron Microscopy, Flow Cytometry, Immunofluorescence, Immunohistochemistry (Pa...


 En savoir plus

Votre prix
$550.60 EACH

Non disponible en dehors du Royaume-Uni et de l'Irlande

Application

This Anti-Collagen Type VI Antibody, clone 3C4 is validated for use in Dot Blot, Electron Microscopy, Flow Cytometry, Immunofluorescence, Immunohistochemistry (Paraffin), and Immunoprecipitation for the detection of collagen VI alpha-3 chain.

Research CategoryCell Structure

Research Sub CategoryECM Proteins

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.

General description

Collagen alpha-3(VI) chain (UniProt P12111; also known as Collagen VI alpha-3 polypeptide) is encoded by the COL6A3 gene (Gene ID 1293) in human. Type VI collagen is an extracellular matrix (ECM) component present in virtually all connective tissues, including cartilage, bone, tendon, muscles and cornea, where it forms microfibrils in close association with basement membranes. In addition to anchoring the basement membrane to the pericellular matrix in muscle, research also indicates a role for collagen VI in cell signaling and cell migration. The basic structural unit of collagen VI is a heterotrimer composed of the alpha-1(VI), alpha-2(VI), and alpha-3(VI) chains (encoded by the COL6A1, COL6A2, and COL6A3 genes, respectively). The α1(VI) and α2(VI) chains are similar in size and domain structure, they contain a 335- or 336-amino acid triple helix region that is characteristic of all collagens. Flanking the triple helix are domains homologous to the A-type domains found in von Willebrand factor (VWA domains). α1(VI) and α2(VI) contain one VWA domain N-terminal to the triple helix (N1) and two VWA domains C-terminal of the helix (C1 and C2). The α3(VI) chain, on the other hand, is much larger with 10 N-terminal (N1–N10) and two C-terminal VWA domains (C1 and C2), and several other types of identifiable domains in the C terminal region (C3–C5). Mutations in the COL6A1, COL6A2, and COL6A3 genes are known causes of Ullrich congenital muscular dystrophy (UCMD) and Bethlem myopathy (BM). Three additional type VI collagen chains have been reported in 2008 (α4(VI), α5(VI) and α6(VI) chains encoded by COL6A4, COL6A5, and COL6A6, respectively).

Immunogen

Purified human collagen VI

Epitope: Non-helical region.

Legal Information

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

Physical form

Unpurified.

Liquid

Specificity

Clone 3C4 targets the non-helical region of alpha-3(VI) chain.

Other species not tested.

Storage and Stability

Maintain frozen at -20°C. Avoid repeated freeze/thaw cycles.

Target description

343.7/321.4/113.2/278.2/134.7 kDa (isoform 1/2/3/4/5 pro-form) and 340.8/318.5/110.4/275.3/131.8 kDa (isoform 1/2/3/4/5 mature form) calculated

antibody formascites fluid
antibody product typeprimary antibodies
biological sourcemouse
clone3C4, monoclonal
Gene Informationhuman ... COL6A3(1293)
isotypeIgG1κ
manufacturer/tradenameChemicon®
NCBI accession no.NP_004360
Quality Level100
shipped indry ice
species reactivityhuman
technique(s)immunocytochemistry: suitable, immunohistochemistry: suitable (paraffin), electron microscopy: suitable, flow cytometry: suitable, immunoprecipitation (IP): suitable
UniProt accession no.P12111
Ce produit répond aux critères suivants pour être admissible aux récompenses suivantes :



HAVE AN ACCOUNT? LOGIN

GUEST CHECKOUT

Proceed as a guest. You will have the option to register to access exclusive pricing and stock availability features after checkout.