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Merck

L8271

Sigma-Aldrich

Monoclonal Anti-Laminin antibody produced in mouse

clone LAM-89, ascites fluid

Synonim(y):

Anti-Laminin Antibody

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About This Item

Numer MDL:
Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

mouse

Poziom jakości

białko sprzężone

unconjugated

forma przeciwciała

ascites fluid

rodzaj przeciwciała

primary antibodies

klon

LAM-89, monoclonal

zawiera

15 mM sodium azide

reaktywność gatunkowa

feline, human, pig

spodziewany brak reakcji z

rabbit, lizard, sheep, carp, canine, chicken, rat, guinea pig, goat, frog, snake

metody

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:1,000 using enzyme-treated human tissue sections
indirect ELISA: suitable
western blot: suitable

izotyp

IgG1

numer dostępu UniProt

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

Opis ogólny

Laminin, a 900kD (approx.) complex extracellular glycoprotein, is the most abundant structural and biologically active component present in the basement membranes. It is a cell substrate adhesion protein and thus has a crucial role in promoting neurite regeneration and modulating cellular functions like differentiation, cell shape and cell movement. Monoclonal Anti-laminin antibody can be used in immunohistochemistry to classify various disease processes involving basement membranes, to mark blood vessel walls of different species and to determine the origin and classification of human tumours. It can also be used in dot blot assays. Mouse anti- laminin antibody reacts specifically with purified human laminin but not with collagen IV, fibronectin, vitronectin or chondroitin sulfate types A, B, and C.
Monoclonal Anti-Laminin (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Laminin, the most abundant structural and biologically active component in basement membranes, is a complex extracellular glycoprotein with an approximate molecular weight of 900 kDa. Laminin is composed of one A chain (400 kDa) one B1 chain (215 kDa) and one B2 chain (205 kDa) all held together by disulfide bonds. Laminin is only found in significant quantities in basement membranes, the thin extracellular matrices that surround epithelial tissue, nerve, fat cells and smooth, striated and cardiac muscle.

Immunogen

human laminin.

Zastosowanie

Monoclonal Anti-Laminin antibody produced in mouse has been used in:
  • immunohistochemistry to stain matrix proteins
  • double immunofluorescence staining
  • indirect immunofluorescence
  • immunogold labelling for electron microscopy

Monoclonal Anti-laminin antibody can be used in indirect immunostaining to determine the distribution of laminin. It may also be used for ELISA, Immunofluorescence and western blotting.

Działania biochem./fizjol.

Laminin is a cell substrate adhesion protein and thus has a crucial role in promoting neurite regeneration and modulating cellular functions like differentiation, cell shape and cell movement because it appears to be an important cell substrate adhesion protein. It plays an important role in many aspects of the cell biology. Variations in the expression of this protein have been observed in embryogenesis, organogenesis, post traumatic healing and cancer.

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

nwg

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


Certyfikaty analizy (CoA)

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Odwiedź Bibliotekę dokumentów

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Saarialho-Kere UK, et al.
The American Journal of Pathology, 148(2), 519-519 (1996)
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The Journal of physiology, 588(Pt 17), 3307-3320 (2010-07-14)
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Journal of biomedical materials research. Part A, 86(1), 170-181 (2007-10-25)
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The aim of this study was to adapt a proprietary decellularisation process for human dermis for use with porcine skin. Porcine skin was subject to: sodium chloride (1 M) to detach the epidermis, trypsin paste to remove hair follicles, peracetic acid

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