T2027
Anti-Transferrin antibody produced in goat
whole antiserum
Synonym(s):
Anti-HEL-S-71p, Anti-PRO1557, Anti-PRO2086, Anti-TFQTL1
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA (i), QPA
Species reactivity:
human
Citations:
12
Technique(s):
indirect ELISA: 1:50,000, quantitative precipitin assay: 3.2-4.8 mg/mL
Uniprot accession no.:
biological source
goat
conjugate
unconjugated
antibody form
whole antiserum
antibody product type
primary antibodies
clone
polyclonal
contains
15 mM sodium azide
species reactivity
human
packaging
antibody small pack of 25 μL
technique(s)
indirect ELISA: 1:50,000, quantitative precipitin assay: 3.2-4.8 mg/mL
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... TF(7018)
Application
Anti-Transferrin antibody has been used:
- in quantitative precipitin assay
- in enzyme linked immunosorbent assay (ELISA)
- in western blotting
- in immunoblotting
Anti-Transferrin antibody produced in goat was used in western blotting analysis of HEK293 cell extracts.
Biochem/physiol Actions
Transferrin is the major iron transporter protein that binds Fe(+3). The transferring-iron import system consists of a TonB dependent transporter (TbpA), and a lipoprotein co-receptor (TbpB) and both proteins work together in the transport of iron across the membrane.
Transferrin plays a major role in providing iron as a source for haemoglobin synthesis. It binds to the transferrin receptor 1(TfR1).
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.
General description
Transferrin is a bilobed glycoprotein. The polypeptide chain of transferrin is composed of two homologous lobes i.e N- and C- lobes. Each lobe is made of two domains N1, N2 and C1, C2 which are linked by a hinge. It has two specific sites for binding of Fe3+.
Preparation Note
treated to remove lipoproteins
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Yan Wang et al.
Journal of controlled release : official journal of the Controlled Release Society, 155(3), 386-392 (2011-07-16)
A proinsulin-transferrin (ProINS-Tf) recombinant fusion protein was designed and characterized for the sustained release of an active form of insulin (INS) by hepatoma cells. During incubation with H4IIE hepatoma cells, a gradual decline of ProINS-Tf concentration, with a concomitant generation
Receptor-mediated activation of a proinsulin-transferrin fusion protein in hepatoma cells.
Wang, Y., et al.
J. Controlled Release, 155, 386-392 (2011)
New iron acquisition system in Bacteroidetes
Manfredi P, et al.
Infection and Immunity, 83(1), 300-310 (2015)
Cole P Anderson et al.
Biochimica et biophysica acta, 1823(9), 1468-1483 (2012-05-23)
Cellular iron homeostasis is maintained by iron regulatory proteins 1 and 2 (IRP1 and IRP2). IRPs bind to iron-responsive elements (IREs) located in the untranslated regions of mRNAs encoding protein involved in iron uptake, storage, utilization and export. Over the
Nicholas Noinaj et al.
Molecular microbiology, 86(2), 246-257 (2012-09-11)
Two pathogenic species within the genus Neisseria cause the diseases gonorrhoea and meningitis. While vaccines are available to protect against four N. meningitidis serogroups, there is currently no commercial vaccine to protect against serogroup B or against N. gonorrhoeae. Moreover, the available
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