RAB35 | RAY Rabbit pAb, APC conj. (标记一抗) | Bioss

bs-7765R-APC

RAB35 | RAY Rabbit pAb, APC conj.

APC标记的RAS相关蛋白癌基因Rab35抗体

GTP binding protein RAY; GTP-binding protein RAY; H ray; RAB1C; Rab35; RAB35 member RAS oncogene family; RAB35, member RAS oncogene family; RAB35_HUMAN; Ras related protein rab 1c(GTP binding protein ray); Ras related protein Rab 1C; Ras related protein Rab35; Ras-related protein Rab-1C; Ras-related protein Rab-35; RAY.

APC
Excitation spectrum: 650nm
Emission spectrum: 660nm

Rabbit

KLH conjugated synthetic peptide derived from human RAB35: 131-201/201

IgG

affinity purified by Protein A

Polyclonal

22 kDa

1mg/ml

0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Shipped at 4℃. Store at -20℃ for one year. Avoid repeated freeze/thaw cycles.

This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

RAB35

Ras-related protein Rab-35

Interacts with DENND1A and DENND1B in a nucleotide-dependent manner. The low binding to DENND1C is nucleotide-independent. All 3 DENND1 act as GEFs for RAB35 and thus activate the protein.

Cell membrane; Lipid-anchor; Cytoplasmic side (Potential). Membrane, clathrin-coated pit. Cytoplasmic vesicle, clathrin-coated vesicle. Endosome. Melanosome.

AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB35 constitutively active.
Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP-bound forms can be phosphocholinated. Phosphocholination inhibits the GEF activity of DENND1A.

Belongs to the small GTPase superfamily. Rab family.

In the process of endocytosis, essential rate-limiting regulator of a fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge.