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Key Documents

G2404

Sigma-Aldrich

Anti-Golgi FTCD antibody, clone 58k-9, Mouse monoclonal

ascites fluid

Synonyme(s) :

Anti-LCHC1

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

ascites fluid

Type de produit anticorps

primary antibodies

Poids mol.

antigen 58 kDa

Contient

15 mM sodium azide

Espèces réactives

human, bovine, mouse, pig, canine, kangaroo rat, hamster, monkey, rat

Technique(s)

electron microscopy: suitable
indirect immunofluorescence: 1:50 using cultured CHO cells
western blot: 1:5,000 using whole rat liver extract

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... FTCD(10841)
mouse ... Ftcd(14317)
rat ... Ftcd(89833)

Description générale

FTCD is a homooctamer with its subunits arranged in a planar ring. It is predominantly expressed in the liver. Apart from being associated with the Golgi apparatus, it is detectable in the supernatant cytosolic fraction, and may also be localized to cytoplasmic vesicles.
Monoclonal Anti-Golgi 58K Protein/formiminotransferase cyclodeaminase (FTCD) (mouse IgG1 isotype) is derived from the 58K-9 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from a mouse immunized with FTCD/Golgi 58K protein purified from rat liver.

Spécificité

The antibody recognizes an epitope located on the microtubule-binding peripheral Golgi membrane 58 kDa protein. It is also useful for studies on the effect of microtubule-perturbing agents on the Golgi apparatus.

Immunogène

Golgi 58K protein from rat liver.

Application

Anti-Golgi FTCD antibody, clone 58k-9, Mouse monoclonal has been used in western blot analysis and dual immunofluorescence staining.
Anti-Golgi FTCD antibody, clone 58k-9, Mouse monoclonal is suitable for electron microscopy, indirect immunofluorescence at a working dilution of 1:50 using cultured CHO cells and indirect immunoblotting at 1:5000 working dilution using whole rat liver extract. It is also useful for the localization of Golgi 58K protein using immunoblotting, dot blot, electron microscopy, and immunocytochemistry.
The antibody was used:


  • for the analysis of distribution of the 58K9 protein exclusively localized in the Golgi
  • as a primary antibody in the immunofluorescence analysis in studies related to functioning of nuclear envelope protein TMEM209 in lung carcinoma cells, tracking TG2 (Transglutaminase Type 2) transport in renal tubular epithelial cells, binding of TRADD (TNFR-associated death domain protein) to TNF-R1 at the plasma membrane and localization of Wilson disease protein in the Golgi apparatus
  • in immunoprecipitation studies
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Western Blotting (1 paper)

Actions biochimiques/physiologiques

FTCD/58K protein of the Golgi apparatus used in conjunction with other antibodies to Golgi proteins (e.g., the Golgi β-COP protein) may be used for studies on the role and relationships of this protein in the cell. It is also useful for localization studies following subcellular fractionation procedures.
Golgi 58K protein is associated with the Golgi apparatus peripherally and has been identified as a version of FTCD (Formiminotransferase Cyclodeaminase). It is a bifunctional metabolic enzyme involved in conversion of histidine to glutamic acid. It acts as a channel for the transport of one-carbon units from formiminoglutamate to the folate pool. It also interacts with vimentin subunits and with polymerized vimentin filaments. Autosomal recessive disorder glutamate formiminotransferase deficiency is caused by defects in FTCD.

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

nwg

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Human Cathepsin W, a Cysteine Protease Predominantly Expressed in NK Cells, Is Mainly Localized in the Endoplasmic Reticulum
Wex T, et al.
Journal of Immunology, 167(4), 2172-2178 (2001)
Holger M Rohde et al.
The Journal of biological chemistry, 278(52), 52689-52699 (2003-10-07)
The Saccharomyces cerevisiae SAC1 gene encodes an integral membrane protein of the endoplasmic reticulum (ER) and the Golgi apparatus. Yeast SAC1 mutants display a wide array of phenotypes including inositol auxotrophy, cold sensitivity, secretory defects, disturbed ATP transport into the
X L Yang et al.
The Biochemical journal, 326 ( Pt 3), 897-902 (1997-10-23)
Copper is an essential trace element in prokaryotes and eukaryotes and is strictly regulated by biological mechanisms. Menkes and Wilson diseases are human disorders that arise from disruption of the normal process of copper export from the cytosol to the
Ahmad Massarweh et al.
Journal of lipid research, 57(8), 1477-1491 (2016-06-10)
We reported an oligosaccharide diphosphodolichol (DLO) diphosphatase (DLODP) that generates dolichyl-phosphate and oligosaccharyl phosphates (OSPs) from DLO in vitro. This enzyme could underlie cytoplasmic OSP generation and promote dolichyl-phosphate recycling from truncated endoplasmic reticulum (ER)-generated DLO intermediates. However, during subcellular
Y Gao et al.
The Journal of cell biology, 152(5), 877-894 (2001-03-10)
The integration of the vimentin intermediate filament (IF) cytoskeleton and cellular organelles in vivo is an incompletely understood process, and the identities of proteins participating in such events are largely unknown. Here, we show that the Golgi complex interacts with

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