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SAB4200500

Sigma-Aldrich

Anti-Collagen IV antibody, Mouse monoclonal

clone J3-2, purified from hybridoma cell culture

Synonym(s):

Anti-COL4, Monoclonal Anti-Collagen IV antibody produced in mouse

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

J3-2, monoclonal

form

buffered aqueous solution

species reactivity

mouse, rat, dog, bovine, human, monkey

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: 2.0-4.0 μg/mL using human liver tissue sections.
western blot: 1.0-2.0 μg/mL using human placenta extracts.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... COL4A1(1282)

General description

Human collagen IV comprises six genes. The COL4A1-COL4A2 is mapped to chromosome 13. The COL4A3-COL4A4 and COL4A5-COL4A6 are localized on chromosome 2 and chromosome X, respectively. It belongs to the collagen superfamily and is associated with the basement membranes (BMs). The six α-chains namely α1(IV) to α6(IV) comprises an N-terminal cysteine and lysine domain, a typical Gly-X-Y triple repeats and a C-terminal noncollagenous (NC1) domain.

Immunogen

placenta preparation rich in basement membrane collagen.

Application

Monoclonal Anti-Collagen IV antibody produced in mouse has been used:
  • in the immunohistochemical staining
  • in the immunostaining
  • in the immunofluorescence detection
  • as a secondary antibody in the western blot analysis

Biochem/physiol Actions

Collagen IV plays a key role in basement membrane assembly. The six chains assemble as three different protomers namely, the α 1.α1.α2(IV), α3.α4.α5(IV) and α 5.α5.α6(IV). The trimers are formed in different combinations of the α-chains. High expression levels of α3, α4 and α5 is observed in specialized glomerular BM (GBM). Mutations in the COlA5 gene is associated with Alport syndrome and α3(IV) chain is associated pathogenesis of Goodpasture syndrome, an autoimmune disease. Mutation in the COlA5 is also implicated in Diffuse Esophageal Lewmyomatosis.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Type IV collagen: structure, gene organization, and role in human diseases. Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis.
Hudson BG, et al.
The Journal of Biological Chemistry, 268(35), 26033-26036 (1993)
Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
Poschl E, et al.
Development, 131(7), 1619-1628 (2004)
Monica S Schoenenberger et al.
The FEBS journal, 291(3), 477-488 (2023-11-21)
Basement membranes are among the most widespread, non-cellular functional materials in metazoan organisms. Despite this ubiquity, the links between their compositional and biophysical properties are often difficult to establish due to their thin and delicate nature. In this article, we
Lysyl hydroxylase inhibition by minoxidil blocks collagen deposition and prevents pulmonary fibrosis via TGF-beta1/Smad3 signaling pathway
Shao S, et al.
Medical Science Monitor : International Medical Journal of Experimental and Clinical Research, 24(2), 8592-8592 (2018)
Songjun Shao et al.
Medical science monitor : international medical journal of experimental and clinical research, 24, 8592-8601 (2018-11-28)
BACKGROUND Idiopathic pulmonary fibrosis (IPF) is a deadly disease characterized by excessive collagen in the extracellular matrix (ECM) of the lungs. Collagen is the primary protein component of the ECM. However, the exact mechanisms underlying the formation and deposition of

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