C4361
Collagen Type I−FITC Conjugate from bovine skin
~1 mg/mL, solution
동의어(들):
Collagen from bovine skin
biological source
bovine skin
form
solution
concentration
~1 mg/mL
shipped in
wet ice
storage temp.
−20°C
Quality Level
Gene Information
cow ... COL1A1(282187), COL1A2(282188)
human ... MMP1 (includes EG:4312)
mouse ... MMP1 (includes EG:4312)
rat ... MMP1 (includes EG:4312)
General description
Type I collagen is the major collagen of tendon and bone, but it is widely distributed in other tissues, such as skin, cornea, tooth dentin, heart valve, lung, liver, fascia and scar tissue.
Application
Collagen Type I-FITC Conjugate from bovine skin has been used in collagen I gel deformation analysis. It has also been used to coat silicone elastic membranes for seeding cells for various experimental studies. It can also be used as a substrate for assaying mammalian collagenase activity in cell culture.
Biochem/physiol Actions
Collagen type I offers mechanical stability, strength and toughness to a range of tissues from tendons and ligaments, to skin, cornea, bone and dentin.
Physical form
Supplied in 0.01 M acetic acid.
저장 등급
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Faceshields, Gloves, Goggles
Processing of collagen-based biomaterials and the resulting materials properties
Meyer M, et al.
BioMedical Engineering OnLine, 18 (2019)
ROCK-and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo
Wyckoff JB, et al.
Current Biology, 16(15), 1515-1523 (2006)
Collagen: structure and mechanics, an introduction
Collagen, 1-13 (2008)
Ayodele Olaolu Oladejo et al.
Journal of inflammation research, 15, 807-825 (2022-02-18)
Endometritis is a female reproductive disease that affects the cattle industries development and microRNAs (miRNAs) play a pivotal role and critical regulators of the innate immune response in varieties of diseases. The present study intends to investigate the regulatory role
F Nelson et al.
The Journal of clinical investigation, 102(12), 2115-2125 (1998-12-17)
There is evidence to suggest that the synthesis of type II collagen is increased in osteoarthritis (OA). Using an immunoassay, we show that the content of the C-propeptide of type II procollagen (CPII), released extracellularly from the newly synthesized molecule
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