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Merck
Összes fotó(3)

Fontos dokumentumok

C2456

Sigma-Aldrich

Monoclonal Anti-Collagen, Type I antibody produced in mouse

clone COL-1, ascites fluid

Szinonimák:

Collagen Type 1 Antibody, Collagen Type 1 Antibody - Monoclonal Anti-Collagen, Type I antibody produced in mouse, Collagen Type I Antibody, Type 1 Collagen Antibody

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
DB
ELISA (i)
IHC (f)
klón:
COL-1, monoclonal
faj reaktivitás:
bovine, human, pig, rat, rabbit, deer
citations:
204
technika/technikák:
dot blot: suitable
immunohistochemistry (frozen sections): 1:2000 using human or other mammalian frozen sections
indirect ELISA: suitable

biológiai forrás

mouse

Minőségi szint

konjugátum

unconjugated

antitest forma

ascites fluid

antitest terméktípus

primary antibodies

klón

COL-1, monoclonal

tartalmaz

15 mM sodium azide

faj reaktivitás

bovine, human, pig, rat, rabbit, deer

technika/technikák

dot blot: suitable
immunohistochemistry (frozen sections): 1:2000 using human or other mammalian frozen sections
indirect ELISA: suitable

izotípus

IgG1

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

Általános leírás

Collagen type I contributes maximum to the fibrous protein content in mammals. It is also present in arteries and extracellular matrix. The protein has an elongated cylindrical structure with tapering ends. It possess a left-handed helix with three polyproline II-type polypeptide strands.
Type I collagen [1α(I)]2α2 is distributed throughout the body. This fibrillar collagen is found in dermis, bone, tendon, ligament, dentin, fasciae, sclera, cornea, organ capsules and fibrous cartilage. It appears in tissues as the classically designated collagen fibers which are formed from densely-packed thin striated fibrils with marked variation in diameter. Collagen I is synthesized mainly by fibroblasts, osteoblasts, odontoblasts and chondroblasts.Collagen type Iα1 (COL1A1) is encoded by the gene mapped to human chromosome 17q21.33. It is the most abundant extracellular matrix (ECM) protein in humans. Type 1 collagen is the major structural protein of bone, tendon, skin and cornea. The encoded protein is a heterotrimer consisting of two α1-chains and one α2-chain.

Egyediség

The antibody is reactive with the native (helical) form of collagen type I in ELISA and dot blot. The product is not reactive when tested on thermally denatured molecules. In immunohistochemical staining of acetone-fixed and unfixed frozen sections, a strong staining of connective tissue fibers is seen. Using the dot blot and ELISA techniques, the antibody shows no cross-reactivity with collagen types, II, III, IV, V, VI, VII, IX, X and XI. The epitope recognized by the antibody is sensitive to routine formalin fixation and paraffin embedding.

Immunogén

Bovine skin collagen type I

Alkalmazás

Monoclonal Anti-Collagen Type I may be used for the localization of type I collagen using various immunochemical assays including ELISA, dot blot and immunohistochemistry. A minimum working dilution of 1:2,000 is determined by indirect immunofluorescent staining of human or other mammalian frozen sections.
Monoclonal Anti-Collagen, Type I antibody produced in mouse has been used in:
  • immunohistochemistry
  • dot blot technique
  • indirect immunofluorescence staining

Biokémiai/fiziológiai hatások

Collagen type I is responsible for mechanical stability, elasticity, strength and toughness, observed in tendons, ligaments, skin, cornea, bone, dentin and many other tissues.
Type 1 collagen serves a structural role in the extracellular matrix by providing mechanical support and resistance to tension. Some of the more important genetic diseases, directly or indirectly involving this collagen type include the majority cases of osteogenesis imperfecta and certain types of Ehlers Danlos syndrome. The development of antibodies against collagens has provided a powerful method for examining the distribution of these connective tissue proteins and for investigation of epithelial-mesenchymal interactions, tumorigenesis and basement membrane biology in ontogeny and epithelial differentiation.

Fizikai forma

Liquid

Tárolás és stabilitás

Store at 2-8 °C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use.

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

nwg

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Pan Yeung et al.
PloS one, 10(12), e0144139-e0144139 (2015-12-15)
There is a growing trend for researchers to use in vitro 3D models in cancer studies, as they can better recapitulate the complex in vivo situation. And the fact that the progression and development of tumor are closely associated to
Collagen: structure and mechanics, an introduction
Fratzl P.
Collagen: Structure and Mechanics, 1-13 (2008)
Gene expressions of small leucine-rich repeat proteoglycans and fibulin-5 are decreased in pelvic organ prolapse
Soderberg M W, et al.
Molecular Human Reproduction, 15(4), 251-257 (2009)
Gemma Pascual et al.
PloS one, 8(11), e80647-e80647 (2013-11-16)
Composite biomaterials designed for the repair of abdominal wall defects are composed of a mesh component and a laminar barrier in contact with the visceral peritoneum. This study assesses the behaviour of a new composite mesh by comparing it with
Cellulose-based scaffold materials for cartilage tissue engineering.
Muller F A, et al.
Biomaterials, 27(21), 3955-3963 (2006)

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