Recombinant human RAB9B protein; Source: E. coli derived, PGEX-4T; Tag: GST; Domain: 1-201 aa of BC093756
Conjugate
Unconjugated
Applications
Application Notes
WB: 1:500-1:1000 IF/ICC: 1:10-1:100
General Notes
This product (Catalog No. CABT-BL5488) is a rabbit-derived polyclonal antibody raised against human RAB9B, targeting the amino acid region 1–201 of the protein. This antibody exhibits cross-reactivity with Human RAB9B from mouse and rat. It has been affinity purified by Protein A. This gene encodes a member of a subfamily of RAS small guanosine triphosphate (GTP)-binding proteins that regulate membrane trafficking. The encoded protein may be involved in endosome-to-Golgi transport. CABT-BL5488 is suitable for use in Western blot (WB) (1:500–1:1,000), IF/ICC (1:10–1:100) applications. CABT-BL5488 is supplied as a liquid formulation in PBS with 0.02% sodium azide and 50% glycerol, pH 7.3. For long-term storage, keep at −20 °C. For short-term use, store at 2–8 °C. Avoid repeated freeze–thaw cycles to maintain antibody integrity and performance.
Target
Alternative Names
Rab 9 like protein; Rab 9L; RAB9B; RAB9L; Ras related protein Rab 9B
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References
Crystal Structure of the Rab9A-RUTBC2 RBD Complex Reveals the Molecular Basis for the Binding Specificity of Rab9A with RUTBC2
Rab9 plays a vital role in regulating the transport of mannose 6-phosphate receptors from late endosomes to the trans-Golgi network through interactions with various effectors. Here, we report the crystal structure of GTP-bound Rab9A in complex with the Rab-binding domain (RBD) of the effector RUTBC2. RUTBC2 RBD assumes a pleckstrin homology domain fold that uses a binding site consisting of mainly b1 and the h1 insertion to interact with the switch and interswitch regions of Rab9A. The C-terminal hypervariable region of Rab9A is disordered and thus not required for RUTBC2 binding. The conformational plasticity of the switch and interswitch regions of Rab9A primarily determines the specificity for RUTBC2. Our biochemical and biological data confirm these findings and further show that Rab9B can bind to RUTBC2 probably in a similar manner as Rab9A. These results together reveal the molecular basis for the binding specificity of Rab9A with RUTBC2.
COA
Publication 
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