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Key Documents

R5530

Sigma-Aldrich

Anti-Rab8 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-Mel transforming oncogene (RAB8 homolog), Anti-Mel transforming oncogene (derived from cell line NK14), Anti-RAB8 homolog, Anti-RAB8A, Anti-Ras-associated protein RAB8

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About This Item

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

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~24 kDa

Espèces réactives

mouse, human, rat

Technique(s)

indirect immunofluorescence: 1:100-1:200 using mouse 3T3 and rat NRK cells
western blot: 1:250-1:500 using whole extract of human Jurkat cells

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 ... RAB8A(4218)
mouse ... Rab8a(17274)
rat ... Rab8a(117103)

Description générale

Rab proteins contain conserved regions involved in guanine-nucleotide binding and hypervariable COOH-terminal domains with a cysteine motif. Rab8 localizes to the trans-Golgi network (TGN), recycling endosomes, tubular structures in the cytosol, membrane protrusions and plasma membrane.

Application

Anti-Rab8 antibody produced in rabbit has been used in immunoblotting and immunofluorescence staining.

Actions biochimiques/physiologiques

Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a subcellular compartment. Through their effector proteins, Rab guanosine triphosphate (GTPases) regulate vesicle formation, actin- and tubulin-dependent vesicle movement and membrane fusion. The guanine-nucleotide binding and hypervariable COOH-terminal domains are implicated in subcellular targeting. Each Rab shows a characteristic subcellular distribution. Therefore, antibodies to Rab proteins may serve as useful tools for studying subcellular localization and membrane organization.
Rab8 (Ras-related protein Rab-8A) controls polarized trafficking, that helps in the formation of protrusion, ciliogenesis or intestinal epithelial. It may involve in the malignant development of EC (endometrial cancer). In human, Rab8 also participates in the dengue virus infection. It controls the translocation of in muscle 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

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions
Yamamura R, et al.
Molecular Biology of the Cell, 19(3), 971-983 (2008)
Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers
Trask B, et al.
Genomics, 15(1), 133-145 (1993)
RAB8A a new biomarker for endometrial cancer?
Bie Y and Zhang Z
World Journal of Surgical Oncology, 12 (2014)
TI-VAMP/VAMP7-SNARE-Rab-GTPase interaction network within a ciliary membrane targeting complex
Kandachar V, et al.
Journal of Cell Science, jcs-222034 (2018)
Endocytic turnover of Rab8 controls cell polarization
Vidal-Quadras M, et al.
Journal of Cell Science, 130(6), 1147-1157 (2017)

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