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SAB4200341

Sigma-Aldrich

Anti-Golph3 (N-terminal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonyme(s) :

Anti-GOPP1, Anti-GPP34, Anti-Golgi peripheral membrane protein 1, 34 kDa, Anti-Golgi phosphoprotein 3 (coat-protein), Anti-Golgi-associated protein; Mitochondrial DNA absence factor, Anti-MIDAS

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~34 kDa

Espèces réactives

mouse, human

Concentration

~1.0 mg/mL

Technique(s)

immunoprecipitation (IP): 5-10 μg using lysates of human HeLa cells
indirect immunofluorescence: 2.5-5.0 μg/mL using mouse 3T3 cells
western blot: 1-2 μg/mL using whole extracts of human HeLa cells

Numéro d'accès UniProt

Q9H4A6

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... GOLPH3(64083)
mouse ... Golph3(66629)
rat ... Golph3(78961)

Description générale

Golph3 (Golgi phosphoprotein 3), also known as coat protein GPP34, is a peripheral membrane protein of the Golgi stack, that localizes to the trans-Golgi network. It is an oncogene that is commonly targeted for amplification in human cancer and in cancer cell lines.

Immunogène

peptide corresponding to the N-terminal region of human Golph3, conjugated to KLH. The corresponding sequence is identical in mouse, rat, monkey and bovine.

Application

Anti-Golph3 (N-terminal) antibody produced in rabbit has been used in:
  • immunoprecipitation
  • immunofluorescence
  • immunoblotting

Actions biochimiques/physiologiques

Golph3 (Golgi phosphoprotein 3) is important for Golgi trafficking and morphology by interacting with the unconventional myosin MYO18A, linking Golgi membranes to the actin cytoskeleton. It is a phosphatidylinositol-4-phosphate (PtdIns(4)P binding protein required for Golgi function. GOLPH3 overexpression is correlated with hyperactivation of mTOR signaling, in human cells.

Forme physique

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

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

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Juliati Rahajeng et al.
Developmental cell, 50(5), 573-585 (2019-06-25)
Vesicle budding for Golgi-to-plasma membrane trafficking is a key step in secretion. Proteins that induce curvature of the Golgi membrane are predicted to be required, by analogy to vesicle budding from other membranes. Here, we demonstrate that GOLPH3, upon binding
Kenneth L Scott et al.
Nature, 459(7250), 1085-1090 (2009-06-26)
Genome-wide copy number analyses of human cancers identified a frequent 5p13 amplification in several solid tumour types, including lung (56%), ovarian (38%), breast (32%), prostate (37%) and melanoma (32%). Here, using integrative analysis of a genomic profile of the region
Holly C Dippold et al.
Cell, 139(2), 337-351 (2009-10-20)
Golgi membranes, from yeast to humans, are uniquely enriched in phosphatidylinositol-4-phosphate (PtdIns(4)P), although the role of this lipid remains poorly understood. Using a proteomic lipid-binding screen, we identify the Golgi protein GOLPH3 (also called GPP34, GMx33, MIDAS, or yeast Vps74p)
Sara Ovejero et al.
The EMBO journal, 42(15), e112684-e112684 (2023-06-12)
Upon DNA damage, cells activate the DNA damage response (DDR) to coordinate proliferation and DNA repair. Dietary, metabolic, and environmental inputs are emerging as modulators of how DNA surveillance and repair take place. Lipids hold potential to convey these cues

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