RAC2, Recombinant Protein

Gx; EN-7; HSPC022

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 22; NC_000022.10 (37621301..37640339, complement). Location: 22q13.1

E Coli

50mM sodium phosphate, pH 7.0, 300mM NaCl, 150mM imidazole, 0.1mM PMSF, 0.25mM DTT, 25% glycerol.

Store product at -70 degree C. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.

Small volumes of RAC2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Recombinant full-length human RAC2 was expressed in E. coli cells using an N-terminal His tag

Scientific Background: RAC2 is a GTPase which belongs to the RAS superfamily of small GTP-binding proteins and is involved in a diverse array of cellular events, including the control of cell growth, cytoskeletal reorganization and the activation of protein kinases. Knockdown of the gene for both RAC1 and RAC2 completely blocks B-cell development indicating that both GTPases are required to transduce B-cell receptor (BCR) signals leading to proliferation, survival, and the upregulation of BAFF receptor (1). Furthermore, RAC2 is required for the transfer of electrons from NADPH to cytochrome b-associated FAD, then to cytochrome b heme, and finally to oxygen (2).

G-Proteins; Signaling Proteins - G-Proteins

Western Blot (WB)

~ 22 kDa

ras-related C3 botulinum toxin substrate 2 (rho family, small GTP binding protein Rac2)

ras-related C3 botulinum toxin substrate 2; small G protein; Ras-related C3 botulinum toxin substrate 3 (rho family, small GTP-binding protein Rac2)

Ras-related C3 botulinum toxin substrate 2

RAC2_HUMAN

This gene encodes a member of the Ras superfamily of small guanosine triphosphate (GTP)-metabolizing proteins. The encoded protein localizes to the plasma membrane, where it regulates diverse processes, such as secretion, phagocytosis, and cell polarization. Activity of this protein is also involved in the generation of reactive oxygen species. Mutations in this gene are associated with neutrophil immunodeficiency syndrome. There is a pseudogene for this gene on chromosome 6. [provided by RefSeq, Jul 2013]

Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase. Ref.8

Enzyme regulation: Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase.

Subunit structure: Interacts with DOCK2, which may activate it. Interacts with S100A8 and calprotectin (S100A8/9). Ref.12 Ref.13

Subcellular location: Cytoplasm. Note: Membrane-associated when activated.

Tissue specificity: Hematopoietic specific.

Involvement in disease: Neutrophil immunodeficiency syndrome (NEUID) [MIM:608203]: An immunodeficiency syndrome due to defective neutrophils. Affected individuals present with leukocytosis, neutrophilia, severe recurrent bacterial infections and poor wound healing.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

Sequence similarities: Belongs to the small GTPase superfamily. Rho family.

1.Walmsley, M. J. et al: Critical roles for Rac1 and Rac2 GTPases in B cell development and signaling. Science 302: 459-462, 2003.
2.Diebold, B. A. et al: Molecular basis for Rac2 regulation of phogocyte NADPH oxidase. Nature Immun. 2: 211-215, 2001.

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