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Merck

MAB3392

Anti-Collagen Type III (COL3A1) Antibody

mouse monoclonal, 1E7-D7

別名:

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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この商品について

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Clone:
1E7-D7, monoclonal
Species reactivity:
rat
Application:
ELISA, IHC, WB
Citations:
11
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製品名

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

biological source

mouse

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

1E7-D7, monoclonal

species reactivity

rat

species reactivity (predicted by homology)

human (based on 100% sequence homology)

technique(s)

ELISA: suitable, immunohistochemistry: suitable, western blot: suitable

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Quality Level

Gene Information

human ... COL3A1(1281)

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General description

138 kDa calculated
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.

Immunogen

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

Application

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.

Biochem/physiol Actions

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.

Physical form

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.

Preparation Note

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

Analysis Note

Control
Rat knee joint tissue
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.

Other Notes

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.

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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保管分類

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

MAB3392:

jan


試験成績書(COA)

製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。

以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

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
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
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
Characterization of type I, III and V collagens in high-density cultured tenocytes by triple-immunofluorescence technique.
Gungormus, C; Kolankaya, D
Cytotechnology null

グローバルトレードアイテム番号

カタログ番号GTIN
MAB339204053252463983

ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.

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