Recombinant Human RAB5A Protein

Beta LifeScience SKU/CAT #: BL-3487PS

Recombinant Human RAB5A Protein

Beta LifeScience SKU/CAT #: BL-3487PS
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Product Overview

Tag N/A
Host Species Human
Synonym Ras-related protein Rab-5A, RAB5A, RAB5.
Background RAB5A is a member of RAS oncogene family. The small GTPase, RAB5A is a crucial regulatory component of the endocytic pathway. Activation of RAB5A is mediated by GDP-GTP exchange factors (GEFs) that generate the Rab5-GTP complex). RAB5A is required for the fusion of plasma membranes and early endosomes.
Description RAB5A Human Recombinant expressed in E.Coli is a single, non-glycosylated polypeptide chain containing 215a.a. and having a molecular weight of 23kDa.
Source E.coli
Purity >95.0% as determined by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Formulation The protein solution contains 20mM Tris-HCl pH-8.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

Target Details

Target Function Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound form is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan. Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3.
Subcellular Location Cell membrane; Lipid-anchor; Cytoplasmic side. Early endosome membrane; Lipid-anchor. Melanosome. Cytoplasmic vesicle. Cell projection, ruffle. Membrane. Cytoplasm, cytosol. Cytoplasmic vesicle, phagosome membrane. Endosome membrane.
Protein Families Small GTPase superfamily, Rab family
Database References

Gene Functions References

  1. Low RAB5A expression is associated with polycystic ovary syndrome. PMID: 29626103
  2. The authors demonstrate that RABGEF1, the upstream factor of the endosomal Rab GTPase cascade, is recruited to damaged mitochondria via ubiquitin binding downstream of Parkin. RABGEF1 directs the downstream Rab proteins, RAB5 and RAB7A, to damaged mitochondria, whose associations are further regulated by mitochondrial Rab-GAPs. PMID: 29360040
  3. Low RAB5 expression is associated with glioma progression. PMID: 28575494
  4. The expression level of EMC-6 is significantly elevated in cervical cancer, without significant correlation with Beclin1 and Rab5a. PMID: 28742203
  5. Here the authors show that Rab5 is monoubiquitinated on K116, K140, and K165. Structural analysis combined with biochemical data revealed that interactions with downstream effectors were impeded in Rab5 monoubiquitinated at K140, whereas GDP release and GTP loading activities were altered in Rab5 monoubiquitinated at K165. PMID: 28968219
  6. Rab5a is overexpressed in oral cancer tissue samples and promotes the malignant phenotype through EMT and the ERK/MMP2 signaling pathway. PMID: 28849149
  7. Rab5 was found abundantly localized in macrophage rich areas of human atherosclerotic lesions.Rab5 plays an important role in modulating the intracellular cholesterol of macrophages and consequently mediating the formation of foam cells. PMID: 28899395
  8. The results were indicative that rabies virus N proficiently colocalized with Rab5/EEA1 and Rab7/LAMP1 in both cell lines at 24 and 48 h post-infection, while N titers significantly decreased in early infection of rabies virus. PMID: 28634871
  9. Membrane localization and dynamics of geranylgeranylated Rab5 hypervariable region has been reported. PMID: 28455099
  10. study elucidated a novel Malat1-miR-101-STMN1/RAB5A/ATG4D regulatory network that Malat1 activates autophagy and promotes cell proliferation by sponging miR-101 and upregulating STMN1, RAB5A and ATG4D expression in glioma cells PMID: 28834690
  11. In conclusion, mutant KRAS promotes endosomal degradation in PDAC cell lines, which is impaired by KRAS silencing. Moreover, KRAS silencing activates RAB5A upregulation and drives PDAC subtype-dependent modulation of endosome trafficking. PMID: 28867190
  12. siRNA knockdown of Rab5a or overexpression of miR-494 in human macrophages significantly inhibits the survival of the parasites PMID: 28650977
  13. our results show that Rab5a is overexpressed in pancreatic cancer and promotes aggressive biological behavior through regulation of the Wnt/beta-catenin signaling pathway. PMID: 28243729
  14. CMTM3 decreases EGFR expression, facilitates EGFR degradation, and inhibits the EGF-mediated tumorigenicity of gastric cancer cells by enhancing Rab5 activity. PMID: 27867015
  15. High RAS-associated protein RAB5 expression correlated with the presence of lymphatic invasion and venous invasion and low E-cadherin expression. PMID: 28103577
  16. downregulated Rab5a led to slowed cell growth, decreased numbers of migrated cells, decreased numbers of cells at the G0G1 phase and a higher apoptosis rate. However, PDGF significantly rescued these phenomena caused by siRNA against Rab5a PMID: 27666726
  17. results suggest a new mechanism in which Rab5 induces a change in flexibility of EEA1, generating an entropic collapse force that pulls the captured vesicle towards the target membrane to initiate docking and membrane fusion PMID: 27556945
  18. structural differences may provide an opportunity to selectively target one Rab5 state and lead to new approaches in the development of Rab5-specific therapies PMID: 28090783
  19. TTBK2 down-regulates GluK2 activity by decreasing the receptor protein abundance in the cell membrane via RAB5-dependent endocytosis. PMID: 27607061
  20. Results indicate that persistent rab5 overactivation through beta-cleaved carboxy-terminal fragment of APP-APPL1 interactions constitutes a novel APP-dependent pathogenic pathway in Alzheimer's disease PMID: 26194181
  21. Results demonstrate that DRG2 is an endosomal protein and a key regulator of Rab5 deactivation and Tfn recycling. PMID: 26582392
  22. Rab5a is involved in critical events not only at the beginning of the autophagy process with endosomal formation (initiation), but also later on, being important for autophagosome sealing and fusion with lysosomes through an interplay with Beclin 1. PMID: 27023526
  23. Findings indicate the role of CMTM7 protein in the regulation of epidermal growth factor receptor (EGFR)-AKT proto-oncogene protein signaling in tumor cells, and as a molecule related to Rab5 GTP-binding protein activation. PMID: 26528697
  24. Low expression of RAB5A is associated with metastasis in prostate cancer. PMID: 26473288
  25. PLD1 recovers the decrease in epidermal growth factor receptor (EGFR) endocytosis induced by HIF-1alpha independent of lipase activity via the Rab5-mediated endosome fusion pathway. PMID: 26680696
  26. Data show that Rab22a- and Rab5a-driven phagosomal uptake is a crucial step in the vesicular cascade that leads to elimination of spirochetes by macrophages. PMID: 26344766
  27. Higher expression of Rab5A was observed in colorectal cancer tissues and Rab5A may be identified as a useful predictor of metastasis and prognosis for CRC. PMID: 26261586
  28. Prelamin A/C was translocated to the nuclear membrane and formed a proper nuclear envelope. Rab5a was translocated to the early endosomes. The specific localizations of the prenylated proteins were dependent on intracellular oxygen concentration PMID: 26181205
  29. Rab5a is a key mediator of LPS-induced vascular hyperpermeability. PMID: 26112597
  30. findings suggest that Rab5 expression is required to maintain characteristics associated with cell transformation PMID: 26168723
  31. Membrane attack complexes activate noncanonical NF-kappaB by forming a novel Akt(+)NIK(+) signalosome on Rab5(+) endosomes. PMID: 26195760
  32. Rab5 activation as a tumor cell migration switch PMID: 25763873
  33. vacuolin-1 activates RAB5A to block autophagosome-lysosome fusion PMID: 25483964
  34. This process is inhibited in the presence of a Rab5 dominant-negative mutant. PMID: 25152371
  35. Bacteria controled the localization or function of host Rab5 and Rab7, and therefore modify the maturation from early to late phagosomes.[review] PMID: 25566515
  36. Recent studies have shown that the activation of Rab5 is a critical event for maintaining the dynamics of focal adhesions, which is fundamental in regulating not only cell migration but also tumor cell invasion PMID: 24727246
  37. activation, which is required for cell migration is promoted by Caveolin-1 PMID: 24659799
  38. In serum-deprivated HeLa cells with low endocytic activity there two types of EEA1-vesicles: the first one carries the both EEA1 and Rab5 at high levels; the second consists of weakly decorated EEA1-vesicles that can be both Rab5-positive and -negative. PMID: 25711083
  39. TNF-alpha augments invasion of Porphyromonas gingivalis in human gingival epithelial cells through increment of ICAM-1 and activation of Rab5. PMID: 25179218
  40. FGF21 has a role in promoting endothelial cell angiogenesis through a dynamin-2 and Rab5 dependent pathway PMID: 24848261
  41. Rab5 isoforms selectively oversee the multiple signaling and trafficking events associated with the endocytic network. PMID: 24587345
  42. Hepatitis B virus can downregulate miR-101-3p expression by inhibiting its promoter activity and that downregulation of miR-101-3p promotes hepatocellular carcinoma cell proliferation and migration by targeting Rab5a. PMID: 24788845
  43. vinculin binds to Rab5 and is required for Staphylococcus aureus uptake in cells. PMID: 24466349
  44. Overexpression of the GTPase RAB5A, a master regulator of endocytosis, is predictive of aggressive behavior and metastatic ability in human breast cancers. PMID: 25049275
  45. The predominant pathway mediated by Australian bat lyssavirus G envelope for internalization into HEK293T cells is clathrin-and actin-dependent also requiring Rab5. PMID: 24576301
  46. Rab5 activation is required to enhance cancer cell migration and invasion by promoting focal adhesion disassembly. PMID: 23813952
  47. Rab5a, Rab8a and Rab14 are major regulators of MT1-MMP trafficking and invasive migration of primary human macrophages. PMID: 23606746
  48. clathrin interacts with Rab5 and plays a fundamental role in the entry and intracellular survival of B. abortus via interaction with lipid rafts and actin rearrangement PMID: 23940042
  49. Data indicate that Rab5, Rab7 and Rab11 are involved in RGS4 traffics through plasma membrane recycling or endosome. PMID: 23733193
  50. Dominant negative (GDP-locked)-Rab5 and -Rab11 reproduced the effects of inhibitors of tubulin and actin, respectively, on the cycling of bradykinin B receptor. PMID: 23454239


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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