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Merck

L8271

Sigma-Aldrich

Anti-Laminin-1 A&B chains Antibody

mouse monoclonal, LAM-89

Synonym(e):

Anti-Laminin Antibody

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Produktbezeichnung

Monoclonal Anti-Laminin antibody produced in mouse, clone LAM-89, ascites fluid

Biologische Quelle

mouse

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

ascites fluid

Antikörper-Produkttyp

primary antibodies

Klon

LAM-89, monoclonal

Enthält

15 mM sodium azide

Speziesreaktivität

feline, human, pig

Darf nicht reagieren mit

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

Methode(n)

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

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Allgemeine Beschreibung

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.

Anwendung

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.

Biochem./physiol. Wirkung

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.

Haftungsausschluss

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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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

nwg

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


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Holmberg J, et al.
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Verbeke S, et al.
Journal of Clinical Pathology, 55(6), 440-445 (2002)
Enhanced expression of matrilysin, collagenase, and stromelysin-1 in gastrointestinal ulcers.
Saarialho-Kere UK, et al.
The American Journal of Pathology, 148(2), 519-519 (1996)

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