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MAB3392

Sigma-Aldrich

Anti-Collagen Type III Antibody, clone IE7-D7

clone 1E7-D7, from mouse

Sinônimo(s):

collagen, type III, alpha 1, collagen, fetal, Ehlers-Danlos syndrome type IV, autosomal dominant, alpha1 (III) collagen, collagen alpha-1(III) chain

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About This Item

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

fonte biológica

mouse

Nível de qualidade

forma do anticorpo

purified immunoglobulin

tipo de produto de anticorpo

primary antibodies

clone

1E7-D7, monoclonal

reatividade de espécies

rat

reatividade da espécie (prevista por homologia)

human (based on 100% sequence homology)

técnica(s)

ELISA: suitable
immunohistochemistry: suitable
western blot: suitable

Isotipo

IgG1κ

nº de adesão NCBI

nº de adesão UniProt

Condições de expedição

wet ice

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... COL3A1(1281)

Descrição geral

Type III collagen (also known as COL3A1), which adds structure and strength to connective tissues, is found in many places in the body, especially skin, lung, intestinal walls, and the walls of blood vessels. Collagen type III is initially produced as pro-collagen, a protein consisting of three pro-alpha1(III) chains that form the triple-stranded, rope-like molecule. After being synthesized, the pro-collagen molecule is modified by the cell. Enzymes modify the amino acids lysine and proline in the protein strands by adding chemical groups that are necessary for the strands to form a stable molecule and then later to crosslink to other molecules outside the cell. Other enzymes add sugars to the protein. The type III pro-collagen molecules are released from the cell and are processed by enzymes that clip small segments off either end of the molecules to form mature collagen. The mature collagen molecules assemble into fibrils. Cross-linking between molecules produces a very stable fibril, contributing to collagen′s tissue strengthening function.

Especificidade

This antibody detects collagen type III. There is no evidence for cross reactivity with Collagen Types I, V and VI or connective tissue proteins (Elastin, Fibronectin and Laminin) at suggested working concentrations.

Imunogênio

Epitope: N-terminus
Human type III collagen (Werkmeister, J.A., et al. 1990).

Aplicação

ELISA Analysis: A previous lot of this antibody was used in ELISA (Werkmeister, J.A., et al., 1991).

Western Blot Analysis: A previous lot of this antibody was used to detect collagen type III in western blot under non-reduced conditions (Werkmeister J.A., et al., 1988; Ramshaw, J.S., et al., 1988).
Some Collagen samples can be contaminated with other Collagen Types. When purified Collagen is used in an application the purity of the Collagen sample should be verified by SDS-page to minimize the risk of false positives.

Immunohistochemistry Analysis: A previous lot of this antibody was used to detect collagen type III in immunohistochemistry (Werkmeister J.A., et al., 1989; Werkmeister J.A., et al., 1989; Werkmeister J.A., et al., 1988).
Research Category
Cell Structure
Research Sub Category
ECM Proteins
This Anti-Collagen Type III Antibody, clone IE7-D7 is validated for use in ELISA, WB, IH for the detection of Collagen Type III.

Qualidade

Evaluated by Immunohistochemistry in rat knee joint tissue.

Immunohistochemistry Analysis: A 1:600 dilution of this antibody detected Collagen Type III in rat knee joint tissue.

Descrição-alvo

138 kDa calculated

forma física

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Armazenamento e estabilidade

Stable for 1 year at 2-8°C from date of receipt.

Nota de análise

Control
Rat knee joint tissue

Outras notas

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
This clone displays a high affinity for human, dog, rat, kangaroo and porcine Type III Collagens.

Exoneração de responsabilidade

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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Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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Mark R Buckley et al.
Connective tissue research, 54(6), 374-379 (2013-10-04)
The mechanical properties of the human supraspinatus tendon (SST) are highly heterogeneous and may reflect an important adaptive response to its complex, multiaxial loading environment. However, these functional properties are associated with a location-dependent structure and composition that have not
Mingyu Cheng et al.
Tissue engineering. Part A, 16(5), 1479-1489 (2009-12-05)
Collagen-platelet (PL)-rich plasma composites have shown in vivo potential to stimulate anterior cruciate ligament (ACL) healing at early time points in large animal models. However, little is known about the cellular mechanisms by which the plasma component of these composites
Yvette M Coulson-Thomas et al.
Forensic science international, 251, 186-194 (2015-04-29)
Morphological and ultrastructural data from archaeological human bones are scarce, particularly data that have been correlated with information on the preservation of molecules such as DNA. Here we examine the bone structure of macroscopically well-preserved medieval human skeletons by transmission
Sophie Cardin et al.
Circulation research, 100(3), 425-433 (2007-01-20)
Gene-expression changes in atrial fibrillation patients reflect both underlying heart-disease substrates and changes because of atrial fibrillation-induced atrial-tachycardia remodeling. These are difficult to separate in clinical investigations. This study assessed time-dependent mRNA expression-changes in canine models of atrial-tachycardia remodeling and
Hacer Sahin et al.
Journal of orthopaedic research : official publication of the Orthopaedic Research Society, 30(12), 1952-1957 (2012-05-23)
Recent studies reveal an important role of vascular endothelial growth factor (VEGF)-induced angiogenesis in degenerative tendon diseases. The way how VEGF influences mechanical properties of the tendons is not well understood yet. We here hypothesized that tendinopathy results in a

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