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Merck
CN

F3542

纤连蛋白片段III1-C 人

recombinant, expressed in E. coli, lyophilized powder

别名:

FF III1-C

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关于此项目

UNSPSC Code:
12352202
NACRES:
NA.75
MDL number:
MFCD00283226
Form:
lyophilized powder
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
8-15 kDa

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biological source

human

recombinant

expressed in E. coli

form

lyophilized powder

quality

essentially salt free

mol wt

8-15 kDa

packaging

pkg of 0.5 mg

technique(s)

cell culture | mammalian: suitable

surface coverage

0.45 μg/cm2

solubility

Tris-buffered saline: soluble 1.00-1.10 mg/mL, clear, colorless

UniProt accession no.

P02751

shipped in

ambient

storage temp.

−20°C

Quality Level

200

Gene Information

human ... FN1(2335)

相关类别

General description

纤连蛋白由位于C末端的两个亚基通过二硫键连接而成。在细胞外基质原纤维中，纤连蛋白进一步被二硫键合成高分子量聚合物。不同组织和物种中的纤连蛋白亚基大小在约235至270 kD之间变化。每个亚基由三种类型的重复模块组成：I、II和III。I型重复有12个，长约45个氨基酸，分为三组，两个相邻的II型重复每个有60个氨基酸，而III型重复则有15-17个，每个长约90个氨基酸。I型和II型各自包含两个二硫键，而III型不含二硫键。在III型重复的每个亚基上含有两个游离的巯基。

最近一种新的区域，III1型重复从人胎盘cDNA中被克隆得到，据报道可参与到基质的形成。在一项利用抗体对基质组装所需的纤连蛋白结构域进行分析的实验中，在纤连蛋白的III1型和I型模块上发现了可通过成纤维细胞抑制标记的血浆纤连蛋白结合和不溶化的表位。这提示III1型和I型在纤连蛋白组装的调节中能够起到作用。来自纤连蛋白前两个III型重复的14 kDa片段能够对纤连蛋白基质组装进行抑制的能力进一步支持了这一发现。4 最近发现，以III1重复的C端三分之二为模型的重组片段III1-C可与纤连蛋白结合并诱导纤连蛋白分子自发性二硫键交联成类似于基质纤丝的多聚体

Application

上皮细胞、间充质细胞、神经元细胞、成纤维细胞、神经嵴细胞、内皮细胞

Biochem/physiol Actions

促进纤连蛋白交联形成基质原纤维样多聚体。

Packaging

包装尺寸基于蛋白质含量

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

法规信息

常规特殊物品
此项目有

历史批次信息供参考:

分析证书(COA)

Lot/Batch Number
11131016
123M4108V
042M4080V
11110734
040M4104

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D C Hocking et al.
The Journal of biological chemistry, 269(29), 19183-19187 (1994-07-22)
Cultured fibroblasts express binding sites for the amino-terminal region of fibronectin on their cell surface that mediate the assembly of soluble fibronectin into disulfide-stabilized fibrils. These binding sites have been termed matrix assembly sites and have been studied in binding
K C Ingham et al.
The Journal of biological chemistry, 272(3), 1718-1724 (1997-01-17)
The first type III module of fibronectin (Fn) contains a cryptic site that binds Fn and its N-terminal 29 kDa fragment and is thought to be important for fibril formation (Morla, A., Zhang, Z., and Ruoslahti, E. (1994) Nature 367
A Morla et al.
Nature, 367(6459), 193-196 (1994-01-13)
Fibronectin is an extracellular matrix protein that is important in development, wound healing and tumorigenesis. In the blood it is dimeric, but in tissues forms disulphide crosslinked fibrils. Here we show that a fragment from the first type-III repeat of
Fatemeh Khodabandehloo et al.
Journal of cellular and molecular medicine, 25(11), 5138-5149 (2021-05-04)
Multipotent human bone marrow-derived mesenchymal stem cells (hMSCs) are promising candidates for bone and cartilage regeneration. Toll-like receptor 4 (TLR4) is expressed by hMSCs and is a receptor for both exogenous and endogenous danger signals. TLRs have been shown to
Mitsutaka Nishida et al.
Bioscience, biotechnology, and biochemistry, 78(4), 635-643 (2014-07-19)
Although previous reports have suggested that pectin induces morphological changes of the small intestine in vivo, the molecular mechanisms have not been elucidated. As heparan sulfate plays important roles in development of the small intestine, to verify the involvement of

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