The Rab-6.1 antibody is a research tool designed to detect Rab-6.1, a member of the Rab GTPase family involved in regulating intracellular vesicular trafficking. Rab-6.1 (also referred to as Rab6A in humans) localizes to Golgi apparatus and trans-Golgi network (TGN) membranes, where it facilitates retrograde transport between the Golgi and endoplasmic reticulum (ER) and modulates post-Golgi secretory pathways . This antibody is critical for studying Rab-6.1's role in cellular processes such as protein sorting, mitotic regulation, and cell migration .
Rab-6.1 antibodies are validated for multiple applications, including:
Western Blot (WB): Detects Rab-6.1 at ~24 kDa in human, mouse, rat, and zebrafish samples .
Immunofluorescence (IF)/Immunocytochemistry (ICC): Localizes Rab-6.1 to Golgi and endosomal compartments .
Immunohistochemistry (IHC): Used in tissue sections to map Rab-6.1 expression .
| Antibody Clone | Host | Applications Validated | Species Reactivity | Citation Count |
|---|---|---|---|---|
| ab95954 (Polyclonal) | Rabbit | WB, IHC-P, ICC/IF | Human, Mouse, Rat | 6+ publications |
| ab308377 [HL1047] | Rabbit | WB, IHC-P, ICC/IF, IP | Human, Mouse, Rat, Drosophila | Not specified |
IP = Immunoprecipitation; WB = Western Blot; IF = Immunofluorescence.
Rab-6.1 governs COPI-independent retrograde transport from the Golgi to the ER, ensuring proper delivery of proteins like β1 integrins .
Overexpression of GTP-bound Rab-6.1 redistributes Golgi enzymes (e.g., β-1,4-galactosyltransferase) into the ER, mimicking Brefeldin A effects .
Depletion of Rab-6.1 disrupts metaphase and cytokinesis, highlighting its role in mitotic membrane dynamics .
In intestinal epithelial cells, Rab-6.1 knockout impairs β1 integrin trafficking, slowing cell migration and compromising tissue integrity .
Rab-6.1 autoantibodies are identified in cancer-associated retinopathy (CAR), where they target retinal ganglion cells .
Dysregulated Rab-6.1 correlates with defective secretory pathways in herpes simplex virus (HSV-1) egress, impacting viral spread .
Human Rab6A (Rab-6.1) and Rab6A′ (a splice variant) exhibit distinct effector binding due to a critical residue (Thr87 vs. Ala87) .
Rab-6.1’s Thr87 enables interaction with Rabkinesin-6, essential for Golgi-ER retrograde transport .
In C. elegans, Rab-6.1 and Rab-6.2 jointly regulate retrograde transport in neurons and non-neuronal tissues .
Saccharomyces cerevisiae Ypt6 shares functional homology with Rab-6.1, underscoring evolutionary conservation .
Specificity Controls: Rab-6.1 antibodies show no cross-reactivity in knockout cell lines (e.g., Rab6A KO HeLa) .
Buffer Optimization: Use 12% SDS-PAGE for WB and citrate-based antigen retrieval for IHC .
Ethical Compliance: Rab-6.1 antibodies are for research only, excluding diagnostic/therapeutic use .
Rab GTPases are essential regulators of intracellular membrane trafficking, governing processes from vesicle formation to membrane fusion. They cycle between inactive GDP-bound and active GTP-bound states. The GTP-bound form recruits effector proteins mediating vesicle formation, movement, tethering, and fusion. RAB-6.1, in its active GTP-bound state, functions redundantly with RAB-6.2 to facilitate retrograde transport of cargo from endosomes to the Golgi apparatus. Specifically, it's crucial for the retrograde trafficking of GLR-1 (an AMPA-type glutamate receptor subunit) from early endosomes to the Golgi in neurons. In conjunction with RAB-6.2, it promotes the retrograde transport of MIG-14 from endosomes to the Golgi in intestinal cells. Furthermore, in oocytes, the active GTP-bound form of RAB-6.1 is involved in the membrane fusion and exocytosis of cortical granules, contributing to post-fertilization embryo surface remodeling. It recruits SEP-1 to cortical granules for exocytosis during the oocyte-to-embryo transition. RAB-6.1 is also required for seam cell division, alae formation, and promotes spontaneous reversals in locomotion.
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