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Merck

R5530

Sigma-Aldrich

Anti-Rab8 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~24 kDa

species reactivity

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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.

Biochem/physiol Actions

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.

Physical form

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

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.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation in muscle cells
Sun Y, et al.
Proceedings of the National Academy of Sciences of the USA, 107(46), 19909-19914 (2010)
Rab8, a vesicular traffic regulator, is involved in dengue virus infection in HepG2 cells
Xu XF, et al.
Intervirology, 51(3), 182-188 (2008)
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)
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)

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