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MAB3392

Sigma-Aldrich

Anti-Collagen Type III (COL3A1) Antibody

mouse monoclonal, 1E7-D7

Synonim(y):

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

Zaloguj sięWyświetlanie cen organizacyjnych i kontraktowych


About This Item

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

Nazwa produktu

Anti-Collagen Type III Antibody, clone IE7-D7, clone 1E7-D7, from mouse

pochodzenie biologiczne

mouse

Poziom jakości

forma przeciwciała

purified immunoglobulin

rodzaj przeciwciała

primary antibodies

klon

1E7-D7, monoclonal

reaktywność gatunkowa

rat

reaktywność gatunkowa (przewidywana na podstawie homologii)

human (based on 100% sequence homology)

metody

ELISA: suitable
immunohistochemistry: suitable
western blot: suitable

izotyp

IgG1κ

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

wet ice

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... COL3A1(1281)

Opis ogólny

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.

Specyficzność

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.

Immunogen

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

Zastosowanie

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.

Jakość

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.

Opis wartości docelowych

138 kDa calculated

Postać fizyczna

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.

Przechowywanie i stabilność

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

Komentarz do analizy

Control
Rat knee joint tissue

Inne uwagi

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.

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
Characterization of type I, III and V collagens in high-density cultured tenocytes by triple-immunofluorescence technique.
Gungormus, C; Kolankaya, D
Cytotechnology null
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
Lei Wang et al.
The Journal of biological chemistry, 289(2), 921-929 (2013-11-23)
Corneal stroma contains an extracellular matrix of orthogonal lamellae formed by parallel and equidistant fibrils with a homogeneous diameter of ~35 nm. This is indispensable for corneal transparency and mechanical functions. However, the mechanisms controlling corneal fibrillogenesis are incompletely understood
Michaela Leyh et al.
Stem cell research & therapy, 5(3), 77-77 (2014-06-12)
In the present study, we established a novel in vitro coculture model to evaluate the influence of osteoarthritis (OA) cartilage explants on the composition of newly produced matrix and chondrogenic differentiation of human bone marrow-derived mesenchymal stem cells (BMSCs) and

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