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MAB1944

Sigma-Aldrich

Anti-Collagen Type VI Antibody, clone 3C4

ascites fluid, clone 3C4, Chemicon®

Synonym(s):

Collagen alpha-3(VI) chain, Collagen VI alpha-3 polypeptide

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About This Item

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

biological source

mouse

Quality Level

antibody form

ascites fluid

antibody product type

primary antibodies

clone

3C4, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

electron microscopy: suitable
flow cytometry: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... COL6A3(1293)

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).

Specificity

Clone 3C4 targets the non-helical region of alpha-3(VI) chain.
Other species not tested.

Immunogen

Epitope: Non-helical region.
Purified human collagen VI

Application

Flow Cytometry Analysis: A representative lot detected intracellular type VI collagen retention by flow cytometry using permeabilized and non-permeabilized fibroblasts isolated from both healthy individuals, as well as Ullrich congenital muscular dystrophy (UCMD) and Bethlem myopathy (BM) patients (Kim, J., et al. (2012). Neuromuscul. Disord. 22(2):139-148).
Immunocytochemistry Analysis: Representative lots detected extracellular type VI collagen immunoreactivity in cultured fibroblasts isolated from Ullrich congenital muscular dystrophy (UCMD) and Bethlem myopathy (BM) patients by fluorescent immunocytochemistry (Kim, J., et al. (2012). Neuromuscul. Disord. 22(2):139-148; Allamand, V., et al. (2011). Skelet Muscle. 1:30; Briñas, L., et al. (2010). Ann. Neurol. 68(4):511-520; Jimenez-Mallebrera, C., et al. (2006). Neuromuscul. Disord. 16(9-10):571-582; Tétreault, M., et al. (2004). Brain. 129(Pt 8):2077-2084; Zhang, R.Z., et al. (2002). J. Biol. Chem. 277(46):43557-43564).
Immunocytochemistry Analysis: A representative lot detected exogenously expressed wild-type α3(VI) chain, as well as α3(VI) chain with G49A or G301V mutation in SaOS-2 transfectants by fluorescent immunocytochemistry (Lamandé, S.R., et al. (2002). J. Biol. Chem. 277(3):1949-1956).
Immunocytochemistry Analysis: Representative lots immunostained extracellular type VI collagen fibrils in human MG63 osteosarcoma cells and primary foreskin fibroblasts cultures (Bruns, R.R., et al. (1986). J. Cell Biol. 103(2):393-404; Engvall, E., et al. (1986). J. Cell Biol. 102(3):703-710).
Immunohistochemistry Analysis: A representative lot detected human type VI collagen immunoreactivity in frozen muscle tissue sections from mice grafted with human synovial stem cells (hSSCs) by fluorescent immunohistochemistry (Meng, J., et al. (2010). Neuromuscul. Disord. 20(1):6-15).
Immunohistochemistry Analysis: Representative lots detected type VI collagen immunoreactivity in muscle and skin samples from congenital muscular dystrophy (CMD) and Ullrich congenital muscular dystrophy (UCMD) patients by fluorescent immunohistochemistry using frozen tissue sections (Peat, R.A., et al. (2008). Neurology. 71(5):312-321; Jimenez-Mallebrera, C., et al. (2006). Neuromuscul. Disord. 16(9-10):571-582).
Immunoprecipitation Analysis: A representative lot co-immunoprecipitated type VI collagen α1(VI) and α2(VI) chains with wild-type α3(VI) chain, as well as α3(VI) chain with G16S or G49A mutation. Impaired α1(VI) and α2(VI) co-IP was observed with α3(VI) G301V mutant (Lamandé, S.R., et al. (2002). J. Biol. Chem. 277(3):1949-1956).
Immunoprecipitation Analysis: A representative lot immunoprecipitated type VI collagen alpha chains from Triton X-100 extracts of MRC-5 human lung fibroblasts (Engvall, E., et al. (1986). J. Cell Biol. 102(3):703-710).
Electron Microscopy Analysis: A representative lot detected reduced extracellular type VI collagen immunoreactivity in cultured fibroblasts isolated from an Ullrich congenital muscular dystrophy (UCMD) patient (Zhang, R.Z., et al. (2002). J. Biol. Chem. 277(46):43557-43564).
Electron Microscopy Analysis: A representative lot immunostained extracellular filaments and fibrils by binding to the band (non-helical) region of the type VI collagen fibrils using cultured human foreskin fibroblasts (Bruns, R.R., et al. (1986). J. Cell Biol. 103(2):393-404).
Dot Blot Analysis: A representative lot detected exogenously expressed wild-type α3(VI) chain, as well as α3(VI) chain with G49A or G301V mutation in the medium of cultured SaOS-2 transfectants (Lamandé, S.R., et al. (2002). J. Biol. Chem. 277(3):1949-1956).
Research Category
Cell Structure
Research Sub Category
ECM Proteins
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.

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

Physical form

Liquid
Unpurified.

Storage and Stability

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

Legal Information

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

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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Arístides López-Márquez et al.
International journal of molecular sciences, 23(8) (2022-04-24)
Collagen VI-related disorders are the second most common congenital muscular dystrophies for which no treatments are presently available. They are mostly caused by dominant-negative pathogenic variants in the genes encoding α chains of collagen VI, a heteromeric network forming collagen;
Adele D'Amico et al.
European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society, 21(6), 873-883 (2017-08-02)
Collagen VI-related disorders (COL6-RD) are a group of heterogenous muscular diseases due to mutations in the COL6A1, COL6A2 and COL6A3 genes, encoding for collagen VI, a critical component of the extracellular matrix. Ullrich congenital muscle disorder and Bethlem myopathy represent
Jong Hee Chae et al.
Journal of medical genetics, 52(3), 208-216 (2015-01-31)
Neuromuscular disorders are a clinically, pathologically, and genetically heterogeneous group. Even for the experienced clinician, an accurate diagnosis is often challenging due to the complexity of these disorders. Here, we investigated the utility of next generation sequencing (NGS) in early
Identification of a deep intronic mutation in the COL6A2 gene by a novel custom oligonucleotide CGH array designed to explore allelic and genetic heterogeneity in collagen VI-related myopathies.
Bovolenta, M; Neri, M; Martoni, E; Urciuolo, A; Sabatelli, P; Fabris, M; Grumati et al.
BMC Medical Genetics null
Sara Aguti et al.
Methods in molecular biology (Clifton, N.J.), 2176, 221-230 (2020-09-01)
Allele-specific gene silencing by antisense oligonucleotide (ASO) or small interference RNA (siRNA) has been used as a therapeutic approach for conditions caused by dominant gain-of-function mutations. We here present an antisense approach using gapmer ASO to diminish the dominant-negative effect

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