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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About This Item
UNSPSCコード:
12352203
eCl@ss:
32160702
NACRES:
NA.41
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製品名
Anti-Collagen Type III Antibody, clone IE7-D7, clone 1E7-D7, from mouse
由来生物
mouse
品質水準
抗体製品の状態
purified immunoglobulin
抗体製品タイプ
primary antibodies
クローン
1E7-D7, monoclonal
交差性
rat
交差性（ホモロジーによる予測）
human (based on 100% sequence homology)
テクニック
ELISA: suitable
immunohistochemistry: suitable
western blot: suitable
アイソタイプ
IgG1κ
NCBIアクセッション番号
UniProtアクセッション番号
輸送温度
wet ice
ターゲットの翻訳後修飾
unmodified
遺伝子情報
human ... COL3A1(1281)
詳細
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.
特異性
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.
免疫原
Epitope: N-terminus
Human type III collagen (Werkmeister, J.A., et al. 1990).
アプリケーション
Research Category
細胞骨格
細胞骨格
Research Sub Category
ECMタンパク質
ECMタンパク質
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).
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).
This Anti-Collagen Type III Antibody, clone IE7-D7 is validated for use in ELISA, WB, IH for the detection of Collagen Type III.
品質
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.
Immunohistochemistry Analysis: A 1:600 dilution of this antibody detected Collagen Type III in rat knee joint tissue.
ターゲットの説明
138 kDa calculated
物理的形状
Protein G Purified
Format: Purified
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
保管および安定性
Stable for 1 year at 2-8°C from date of receipt.
アナリシスノート
Control
Rat knee joint tissue
Rat knee joint tissue
その他情報
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.
免責事項
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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保管分類コード
12 - Non Combustible Liquids
WGK
WGK 1
引火点(°F)
Not applicable
引火点(℃)
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。
Jan Code
MAB3392:
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。
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
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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