Ras Related GTP Binding B (RRAGB) Antibody

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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
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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