Skip to Content
Merck
All Photos(1)

Key Documents

F6136

Sigma-Aldrich

Anti-Horse Spleen Ferritin antibody produced in rabbit

affinity isolated antibody, lyophilized powder

Synonym(s):

Ferritin Antibody

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

horse

technique(s)

immunoelectrophoresis: suitable
immunoelectrophoresis: suitable
indirect ELISA: 1:10,000

storage temp.

2-8°C

target post-translational modification

unmodified

Gene Information

horse ... Ftl(100051593)

Looking for similar products? Visit Product Comparison Guide

General description

Ferritin consists of homogenous protein segment called as apoprotein and an iron segment which binds to the apoprotein. It is composed of heavy (H) and light (L) chains.
Ferritin is the storage form of iron in mammals, found mainly in liver, bone marrow and spleen. It is also present in small intestine, placenta, kidney and heart. Horse spleen ferritin is made up of 24 identical subunits. Ferritin of different organs is distinct with different electrophoretic mobility and possible functional differences.
.

Specificity

The antibody specifically recognizes ferritin from horse spleen.

Immunogen

Purified horse spleen ferritin

Application

Anti-Horse Spleen Ferritin antibody was used for immunocytochemistry of rat brain sections at a working antibody dilution of 1:2000 and in mouse brain sections at 1:1000. The antibody was used for immunoblotting using cell lysates of mouse primary erythroblasts and human ovarian carcinoma cells and human bronchial epithelial cells at a working dilution of 1:1000. The antibody is suitable for immunoelectrophoresis.
Horse Spleen Ferritin antibody has been used:
  • immunofluorescence
  • in western blotting
  • in immunohistochemistry

Biochem/physiol Actions

Ferritin iron is oxidized from Fe(II) to Fe(III) in the presence of the enzyme ferroxidase.

Physical form

Lyophilized from 0.01 M sodium phosphate, 0.015 M sodium chloride, pH 7.2

Reconstitution

Reconstitute with 0.135 M sodium chloride.

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

11 - Combustible Solids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Transferrin ensures survival of ovarian carcinoma cells when apoptosis is induced by TNF$\alpha$, FasL, TRAIL, or Myc
Fassl S, et al.
Oncogene, 22(51), 8343-8343 (2003)
Jan A Gorter et al.
Epilepsia, 46(9), 1371-1379 (2005-09-09)
Iron accumulation in the brain has been associated with neurodegenerative disorders, including epilepsy. In our previous SAGE study, we showed that ferritin, an iron-storage protein, was one of the genes (Ferritin-H) that showed overexpression before the chronic epileptic phase. In
New functions for an iron storage protein: the role of ferritin in immunity and autoimmunity
Recalcati S, et al.
Journal of Autoimmunity, 30(1-2), 84-89 (2008)
Microglial pathology in Down syndrome
Xue Q S and Streit W J
Acta Neuropathologica, 122(4), 455-455 (2011)
Structure and physiological functions of ferritin
Granick, S
Physiological Reviews, 31(4), 489-511 (1951)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service