Recombinant Human Ras-Related Protein Rab-8A (RAB8A) Protein (His-SUMO)

Name: Recombinant Human Ras-Related Protein Rab-8A (RAB8A) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-07910P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ras-Related Protein Rab-8A (RAB8A) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P61006
Target Symbol	RAB8A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	KTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKKLEGNSPQGSNQGVKITP
Expression Range	3-193aa
Protein Length	Partial
Mol. Weight	37.8 kDa
Research Area	Signal Transduction
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	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B and RAB11A participates in epithelial cell polarization. May be involved in ciliogenesis. Together with MICALL2, may also regulate adherens junction assembly. May play a role in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore play a role in glucose homeostasis. Involved in autophagy.
Subcellular Location	Cell membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus. Recycling endosome membrane. Cell projection, cilium. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle, phagosome membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Midbody. Cytoplasm. Cytoplasm, cytoskeleton, cilium axoneme.
Protein Families	Small GTPase superfamily, Rab family
Database References	HGNC: 7007 OMIM: 165040 KEGG: hsa:4218 STRING: 9606.ENSP00000300935 UniGene: PMID: 29357897 Rab8a is phosphorylated by LRRK2.Phosphorylation of Rab8a plays important role in the fusion and enlargement of lipid droplets. PMID: 29482628 C9ORF72 causes suboptimal autophagy PMID: 27494456 GRAF1-mediated removal of Rab8 from the cell surface restricts its activity during protrusion formation, thereby facilitating dynamic adjustment of the polarity axis. PMID: 28137756 Ectopic expression of an N-terminal-truncated ARHGEF10 mutant led to the generation of large vesicle-like structures containing both Rab6 and Rab8. PMID: 27550519 report the design of a bioavailable StRIP3 analogue that harbors two hydrophobic cross-links and exhibits increased binding affinity, combined with robust cellular uptake and extremely high proteolytic stability. Localization experiments reveal that this double-stapled peptide and its target protein Rab8a accumulate in the same cellular compartments PMID: 27336832 knockdown of another Parkinson's disease (PD) gene, LRRK2, which phosphorylates Rab8a, similarly impairs retromer trafficking, secretory autophagy and Golgi-derived vesicle secretion, thus demonstrating converging roles of two PD genes TMEM230 and LRRK2 on Rab8a function, and suggesting that retromer and secretory dysfunction play an important role in PD pathogenesis. PMID: 28115417 Rab8 can induce Rac1- and Tiam1-dependent cortical actin polymerization and focal adhesion disassembly through the proteases MT1-MMP and calpain, and Rho-GTPase-dependent mechanisms PMID: 26940916 Data demonstrate that EHBP1L1 links Rab8 and the Bin1-dynamin complex, which generates membrane curvature and excises the vesicle at the endocytic recycling compartment for apical transport. PMID: 26833786 Further exploration of the NINL-associated interactome identifies MICAL3, a protein known to interact with Rab8 and to play an important role in vesicle docking and fusion. PMID: 26485645 The small GTPase Rab8 interacts with VAMP-3 to regulate the delivery of recycling T-cell receptors to the immune synapse. PMID: 26034069 the role of Rabin8 (a mammalian ortholog of Sec2p) with Rab8-nucleotide-exchange factor activity in autophagy in mammalian cells, was examined. PMID: 25787272 DLC3 is recruited to Rab8-positive membrane tubules and is required for the integrity of the Rab8 and Golgi compartments. PMID: 25673874 Rab8A GTPase Ser(111) phosphorylation is not directly regulated by PINK1 in vitro and demonstrate in cells the time course of Ser(111) phosphorylation of Rab8A, 8B and 13 is markedly delayed compared to phosphorylation of Parkin at Ser(65). PMID: 26471730 Intercellular transfer of transferrin receptor by a contact-, Rab8-dependent mechanism involving tunneling nanotubes. PMID: 26220176 High expression of RAB8A is associated with endometrial cancer. PMID: 25477298 Study established a direct interaction between alpha-synclein and Rab8a and provided unique insights into the molecular mechanisms of alpha-synclein toxicity PMID: 24983211 Rab8a and Drebrin E act as key proteins in the regulation of apical trafficking in intestinal epithelial cells. PMID: 24399445 Microvilli establishment required interaction between RAB8A and MYO5B, while loss of the interaction between RAB11A and MYO5B induced microvillus inclusions. PMID: 24892806 TRIM required LAX for binding to Rab8 in a complex, a novel CTLA-4/TRIM/LAX/Rab8 effector complex in the transport of CTLA-4 to the surfaces of T cells PMID: 24515439 Intermediates in the guanine nucleotide exchange reaction of Rab8 protein catalyzed by guanine nucleotide exchange factors Rabin8 and GRAB. PMID: 24072714 Rab5a, Rab8a and Rab14 are major regulators of MT1-MMP trafficking and invasive migration of primary human macrophages. PMID: 23606746 Fuzzy appears to control subcellular localization of the core PCP protein Dishevelled, recruiting it to Rab8-positive vesicles and to the basal body and cilium. We show that loss of Fuzzy results in inhibition of PCP signaling PMID: 23303251 Slp4 and Rab8 are expressed and interact in human platelets, and might be involved in dense granule release. PMID: 23140275 Optineurin acts as an adaptor to bring together Rab8 and its GTPase-activating protein TBC1D17. PMID: 22854040 These findings show a role for Rab8a in the physiological function of hSVCT1 in intestinal epithelia. PMID: 23014846 NDR2-mediated Rabin8 phosphorylation is crucial for ciliogenesis by triggering the switch in binding specificity of Rabin8 from PS to Sec15. PMID: 23435566 This article reviewes biophysical and structural work and discuss possible functional implications of the finding that Rab8 binds with the highest affinity to OCRL1 among the Rab proteins tested.[review] PMID: 22790198 These experiments provide us with an understanding of the role Rab8 plays in coordinated regulation of mGluR1a and how this impacts mGluR1a signaling PMID: 23175844 Data suggest that the Rabin8-Rab8-Sec15 interaction may couple the activation of Rab8 to the recruitment of the Rab8 effector and is involved in the regulation of vesicular trafficking for primary cilium formation. PMID: 22433857 EPI64 regulates membrane trafficking both by stabilizing Arf6-GTP and by inhibiting the recycling of membrane through the tubular endosome by decreasing Rab8a-GTP levels. PMID: 22219378 This study demonistrated that Rabin8 regulates spine development. PMID: 22445341 DCDC5 colocalizes with Rab8 and links it to dynein during cytokinesis. PMID: 22159412 Rab8A function is not needed for budding or motility of exocytotic carriers but is required for their docking and fusion. PMID: 21596566 WNK1 promotes cell surface expression of glucose transporter GLUT1 by regulating a Tre-2/USP6-BUB2-Cdc16 domain family member 4 (TBC1D4)-Rab8A complex PMID: 20937822 RPGR modulates intracellular localization and function of RAB8A. PMID: 20631154 Data provide strong evidence indicating that Rab8 GTPase interacts with distinct motifs in the C termini of alpha(2B)-AR and beta(2)-AR and differentially modulates their traffic from the TGN to the cell surface. PMID: 20424170 Rab11, in its GTP-bound form, interacts with Rabin8 and kinetically stimulates the guanine nucleotide-exchange activity of Rabin8 toward Rab8. PMID: 20308558 These findings establish Rab8 as a key component of the regulatory machinery that leads to ATP-binding cassette transporter A1 (ABCA1)-dependent removal of cholesterol from endocytic circuits. PMID: 17050734 MT1-MMP delivery to invasive structures, and therefore its proinvasive activity, is regulated by Rab8 GTPase. PMID: 17332756 Rab8a and Myosin Vb colocalize to a tubular network containing EHD1 and EHD3, which does not contain Rab11a. PMID: 17507647 One microvillus inclusion disease patient who shows an identical phenotype to Rab8-deficient mice expresses a reduced amount of RAB8A PMID: 17597763 Data show that the Rab8a, -17, and -23, and their cognate GTPase-activating proteins (GAPs), XM_037557, TBC1D7, and EVI5like, are involved in primary cilia formation, and that Rab8a specifically interacts with cenexin/ODF2. PMID: 17646400 in response to cellular activation in T cells and B cells, a PTB-containing stability complex forms that contains binding sites for Rab8A and cyclin D(2) transcripts and increases their mRNA half-lifes PMID: 18714005 data suggest that the function of Rab8 is important for DV2 infection, and Rab8 may be involved in DV2 infection. PMID: 18724065 Both CEP290 and PCM-1 are required for ciliogenesis and are involved in the ciliary targeting of Rab8. PMID: 18772192 Rab8 regulates ABCA1 cell surface expression and facilitates cholesterol efflux in primary human macrophages. PMID: 19304576 These data suggest that Myo5c associated with Rab8 is involved in the release of dengue virus 2 from HepG2 cells. PMID: 19641326

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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.

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