Recombinant Human Ras-Related Protein Rab-4A (RAB4A) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-09284P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Ras-Related Protein Rab-4A (RAB4A) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-09284P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description Recombinant Human Ras-Related Protein Rab-4A (RAB4A) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P20338
Target Symbol RAB4A
Synonyms HRES 1 / RAB4; Oncogene RAB4; Rab 4; RAB 4A; RAB4 member RAS oncogene family; Rab4a; RAB4A member RAS oncogene family; RAB4A_HUMAN; Ras related protein Rab 4A; Ras related protein Rab4A; Ras-related protein Rab-4A
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MSQTAMSETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFVQCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRRAQAPNAQECGC
Expression Range 1-218aa
Protein Length Full Length
Mol. Weight 51.4kDa
Research Area Tags & Cell Markers
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Involved in protein transport. Plays a role in vesicular traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2 signaling. Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets.
Subcellular Location Membrane; Peripheral membrane protein. Cytoplasm. Early endosome membrane; Peripheral membrane protein. Recycling endosome membrane; Peripheral membrane protein.
Protein Families Small GTPase superfamily, Rab family
Database References

Gene Functions References

  1. These findings bring attention to the effects of C-terminal carboxylmethylation on RAB GTPases and provide a rationale for targeting ICMT in the treatment of metastatic cancer PMID: 28604748
  2. The results contradict the model of feedback activation of Rab5 and instead indicate that Rbpt5 is recruited by both Rabex5 recognizing ubiquitylated cargo and by Rab4 to activate Rab5 in a feed-forward manner. PMID: 26430212
  3. Rab4 expression is up-regulated by laminar shear stress, which contributed to improved vascular endothelial cell autophagy and function. PMID: 26716952
  4. Together the findings indicate that Arl1 links Rab4-dependent formation of endosomal sorting domains with downstream assembly of adaptor protein complexes that constitute the endosomal sorting machinery. PMID: 24835460
  5. HRES-1/Rab4 regulates autophagy through promoting the formation of LC3(+) autophagosomes and the preservation of mitochondria. PMID: 24404161
  6. Data indicate that Rab4 regulates ether-a-go-go-related gene (hERG) channel density via neural precursor cell-expressed developmentally down-regulated protein 4-2 (Nedd4-2). PMID: 23792956
  7. our findings suggest an evolutionarily conserved function of HDPTP-Rab4 in the regulation of endocytic trafficking, cell adhesion and migration. PMID: 22825871
  8. TBC1D16 is a GTPase activating protein for Rab4A that regulates transferrin receptor recycling and EGFR trafficking and signaling. PMID: 23019362
  9. Upregulated expression of rab4, rab5, rab7 and rab27 correlates with antemortem measures of cognitive decline in individuals with mild cognitive impairment and Alzheimer disease. PMID: 21669283
  10. Thus down- or up-regulation of Rab4A expression or Rab4A function triggered inhibition or increase of procathepsin L secretion respectively. PMID: 21501115
  11. Overexpression of Rab4 regulates angiotensin II type I receptor phosphorylation and sensitization. PMID: 20943774
  12. Findings substantiate the notion that modulation of the temporal and spatial distribution of P-gp in cancer cells may be a valid therapeutic strategy to alleviate the MDR phenotype, and signal to Rab4 as a potential target. PMID: 20209493
  13. These findings suggest that Rab14 and Rab4 act sequentially, together with RUFY1. PMID: 20534812
  14. NDRG1 specifically interacts with constitutively active Rab4aQ67L mutant protein and not with GDP-bound Rab4aS22N mutant proving NDRG1 as a novel Rab4a effector PMID: 17786215
  15. Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein PMID: 11786538
  16. Data suggest that abnormal membrane recycling in Niemann-Pick type A and C lipid storage disease fibroblasts results from specific inhibition of rab4 function by excess cholesterol in early endosomes. PMID: 15292453
  17. In contrast to Rab11, Rab4 is not involved in exocytosis PMID: 15689494
  18. Rab4 specific residue His39 modulates the nucleotide binding pocket giving rise to a reduced rate for nucleotide hydrolysis and exchange PMID: 15907487
  19. critical element that regulates epithelial sodium channel (ENaC) function by GTP-GDP recycling and concomitant changes in ENaC expression at the cell surface and in intracellular pool PMID: 16389071
  20. The study suggests that Rab4 regulates the channel through multiple mechanisms that include protein-protein interaction, GTP/GDP exchange, and channel protein trafficking. PMID: 16413502
  21. CT229 of Chlamydia trachomatis interacts with and recruits Rab4A to the inclusion membrane and therefore may play a role in regulating the intracellular trafficking or fusogenicity of the chlamydial inclusion. PMID: 16926431
  22. Regulation of CD4 expression via recycling by HRES-1/RAB4 controls susceptibility to HIV infection PMID: 16935861
  23. elevated [5HT](ex)"paralyzes" the translocation of SERT from intracellular locations to the plasma membrane by controlling transamidation and Rab4-GTP formation PMID: 18227069
  24. Both phosphorylated and nonphosphorylated MOR internalize via Rab5-dependent pathway after agonist stimulation, and the phosphorylated and nonphosphorylated MORs recycle through distinct vesicular trafficking pathways mediated by Rab4 and Rab11. PMID: 18550774
  25. Cyclic AMP-mediated phosphoinositide-3-kinase-independent activation of Rab4 facilitates Ntcp translocation in a hepatoma cell line. PMID: 18688880
  26. oxytocin receptors localize in vesicles containing the Rab5 and Rab4 small GTPases PMID: 19126785
  27. activation of mTOR causes the loss of TCRzeta in lupus T cells through HRES-1/Rab4-dependent lysosomal degradation. PMID: 19201859
  28. conclude that a recycling pathway regulated by Rab4A is a critical effector of VEGFR1 during branching morphogenesis of the vasculature PMID: 19302266
  29. Data show that within several minutes after initiating rapid endocytosis of B2ARs by the isoproterenol, bright "puffs" of locally increased surface fluorescence intensity representing discrete Rab4-dependent recycling events. PMID: 19369423
  30. D-AKAP2 promotes accumulation of recycling proteins in the Rab4/Rab11-positive endocytic recycling compartment PMID: 19797056

FAQs

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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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