Ras Related GTP Binding B (RRAGB) Antibody

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292.5€ (80 µl)

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935106861
info@markelab.com
name
Ras Related GTP Binding B (RRAGB) Antibody
category
Primary Antibodies
provider
Abbexa
reference
abx030652
tested applications
ELISA, WB

Description

Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. [provided by RefSeq].

Documents del producto

Instrucciones
Data sheet
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Product specifications

Category
Primary Antibodies
Immunogen Target
Ras Related GTP Binding B (RRAGB)
Host
Rabbit
Reactivity
Human
Recommended Dilution
WB: 1/1000. Optimal dilutions/concentrations should be determined by the end user.
Clonality
Polyclonal
Conjugation
Unconjugated
Isotype
IgG
Purification
Purified through a protein A column, followed by peptide affinity purification.
Size 1
80 µl
Size 2
400 µl
Form
Liquid
Tested Applications
ELISA, WB
Buffer
PBS containing 0.09% sodium azide.
Availability
Shipped within 5-10 working days.
Storage
Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
Q5VZM2
Background
Antibody anti-RRAGB
Status
RUO

Descripción

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Ras Related GTP Binding B (RRAGB) Antibody

Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. [provided by RefSeq].

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