Recombinant Human Ras-Related Protein Rab-11A (RAB11A) Protein (His-SUMO)

Name: Recombinant Human Ras-Related Protein Rab-11A (RAB11A) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03332P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ras-Related Protein Rab-11A (RAB11A) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P62491
Target Symbol	RAB11A
Synonyms	MGC1490; Rab 11; Rab 11A; RAB 11A, member oncogene family; Rab-11; RAB11 A; RAB11; Rab11a; RAB11A member RAS oncogene family; Ras related protein Rab 11A; Ras related protein Rab11A; Ras-related protein Rab-11A; RB11A_HUMAN; YL 8; YL8
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	GTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIYRIVSQKQMSDRRENDMSPSNNVVPIHVPPTTENKPKVQCC
Expression Range	2-213aa
Protein Length	Full Length of Mature Protein
Mol. Weight	39.9kDa
Research Area	Cancer
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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11A regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, 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 participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes. May also play a role in melanosome transport and release from melanocytes.
Subcellular Location	Cell membrane; Lipid-anchor. Recycling endosome membrane; Lipid-anchor. Cleavage furrow. Cytoplasmic vesicle, phagosome. Cytoplasmic vesicle membrane.
Protein Families	Small GTPase superfamily, Rab family
Database References	HGNC: 9760 OMIM: 605570 KEGG: hsa:8766 STRING: 9606.ENSP00000261890 UniGene: PMID: 29123131 Study suggestes that Rab11a serves as an important oncoprotein and a regulator of YAP in human non-small cell lung cancer. PMID: 28468127 This review will focus on the structure and function of the novel Rab11-FIP3-Rabin8 dual effector complex and its implications for the targeting of sensory receptors to primary cilia, dysfunction of which causes cilia defects underlying human diseases and disorders know as ciliopathies. PMID: 26399276 Data suggest that membrane tethering mediated by endosomal RAB11A is drastically and selectively stimulated by its cognate Rab effectors, class V myosins (MYO5A and MYO5B), in a GTP-dependent manner. (RAB11A = ras-related GTPase Rab-11A; MYO5 = myosin class V) PMID: 28939769 these studies are not only the first to identify alpha4 helix of Rab11a as a protein binding domain on the GTPase but also reveal novel mechanistic insights into the intracellular trafficking of the hIP, and potentially of other members of the GPCR superfamily, involving Rab11-dependent mechanisms PMID: 28739266 transient expression of ATG16L1 not only inhibited autophagosome biogenesis, but also aberrantly targeted RAB11-positive recycling endosomes, resulting in recycling endosome aggregates. PMID: 27875067 The results from this analysis indicated that Rab11a, Rab11c(Rab25) and Rab14 were expressed in a wide range of cell lines, including the human placental trophoblastic BeWo cell line. PMID: 28922401 The results suggest that progressive assembly of vRNA segments may be cell type dependent and that vRNA may be transported through the cytoplasm without Rab11A-containing recycling endosomes in the absence of intact microtubules. PMID: 28724771 Rac1-Rab11-FIP3 regulatory hub coordinates vesicle traffic with actin remodeling and T-cell activation PMID: 27154205 In colorectal carcinoma, overexpression of Rab11 was found to promote collective cell migration through the increased distribution of E-cadherin, which enhanced cell-cell connections. PMID: 27696383 A novel tribasic Golgi export signal directs cargo protein interaction with activated Rab11 and AP-1-dependent Golgi-plasma membrane trafficking. PMID: 26941330 Analysis reveals novel aspects of the PI4KIIIb-Rab11 complex, specifically conformational changes induced in the switch regions of activated Rab11. PMID: 26756197 Substituted V20 of Rab11A was found to interfere with proper localization of the water molecule, which mediated GTP hydrolysis, resulting in GTP being locked in an active form of Rab11A S20V. PMID: 26879265 Data (including data from studies in knockout mice) suggest Munc13-4 binds to Rab11 and regulates trafficking of Rab11-containing vesicles; Munc13-4 appears to regulate final steps of Rab11-positive vesicle docking at plasma membrane in exocytosis. PMID: 26637356 Rab11A and Rab11B differentially regulate intracellular trafficking of PAR1 through distinct endosomal sorting mechanisms PMID: 26635365 Rab11a/Rab11 family-interacting protein 2-mediated VE-cadherin recycling is required for formation of adherens junctions and restoration of vascular endothelial barrier integrity. PMID: 26663395 Mumps Virus release from the apical surface of polarized epithelial cells is facilitated by a Rab11-mediated transport system. PMID: 26378159 Vaccinia virus traffics to early endosomes, where recycling endosome markers Rab11 and Rab22 are recruited to participate in subsequent virus trafficking prior to virus core uncoating in the cytoplasm. PMID: 26041286 Rab11a-knockdown cells displayed mislocalization of STX3 and the presentation of microvilli in the basolateral compartment PMID: 25673875 Rab11 co-localizes with alpha-synuclein in intracellular inclusions and modulates its aggregation, secretion and toxicity. PMID: 25092884 PI4KIIIbeta likely plays a role in breast oncogenesis and that cooperation between Rab11a and PI4KIIIbeta represents a novel Akt activation pathway. PMID: 24962317 Additionally, Rab11 recruitment is absent and Shigella-containing vacuolar rupture is delayed in the ipgD mutant that does not dephosphorylate PI(4,5)P2 into PI(5)P. PMID: 25299335 Data demonstrated that Rab11 regulated E-cadherin expression and promoted colon cancer cell transformation. PMID: 25117932 Rab11-dependent EGFR recycling has a role in synergistic cytotoxicity of afatinib and cetuximab against EGFR T790M PMID: 25446083 Microvilli establishment required interaction between RAB8A and MYO5B, while loss of the interaction between RAB11A and MYO5B induced microvillus inclusions. PMID: 24892806 Ubiquitylation and activation of RAB11a is promoted by a beta2 adrenergic receptor-HACE1 complex. PMID: 24190883 Rab11A controls BACE1 recycling to endosomes and thus affects beta-amyloid production. PMID: 24373285 these data provide a mechanism for how PI4KIIIbeta coordinates Rab11 and its effectors on PI4P-enriched membranes and also provide strategies for the design of specific inhibitors that could potentially target plasmodial PI4KIIIbeta to combat malaria. PMID: 24876499 Mitochondrial remodeling was associated with increased proximity between Rab11a and mitochondrial membranes, changes in fusion-fission dynamics, and mitochondrial relocalization of the Drp1, which was regulated by the Rab11a effector protein FIP1/RCP. PMID: 24302731 Data indicate that alpha2-macroglobulin (alpha2M*), through its receptor LRP1, induces cellular migration of Muller glial cells by a mechanism that involves MT1-MMP intracellular traffic to the plasma membrane by a Rab11-dependent recycling pathway. PMID: 23640058 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 These findings suggest that Rab11-FIP1 proteins participate in spatially and temporally distinct steps of the recycling process along a complex and dynamic tubular network in which Rab11-FIPs occupy discrete domains. PMID: 23283983 The potential roles of the Rab11 pathway in the trafficking, assembly and budding steps of negative-strand viruses. PMID: 23176490 Rab11 depletion gives rise to accumulation of recycling carriers containing endocytosed transferrin and transferrin receptor beneath the plasma membrane. PMID: 22685325 findings show 2 mother centriole appendage proteins, centriolin and cenexin/ODF2, regulate association of the endosome components Rab11, the Evi5, and the exocyst at the mother centriole PMID: 22981775 Rab11A/myosin Vb/Rab11-FIP2 complex frames two late recycling steps of langerin from the ERC to the plasma membrane PMID: 22420646 TBC1D14 binds activated Rab11 but is not a GAP for Rab11, and loss of Rab11 prevents TBC1D14-induced tubulation of recycling endosomes. PMID: 22613832 Our data suggest a selective role of PICK1 in clustering and reducing the recycling rates of PDZ domain binding partners sorted to the Rab11-dependent recycling pathway. PMID: 22303009 Recycling was accompanied by dephosphorylation of VEGFR-2 between Rab4 and Rab11 vesicles and quantitatively and qualitatively altered signal output. PMID: 21586748 Our results uncover a critical host factor with an essential contribution to influenza virus genome delivery and reveal a potential role for RAB11A in the transport of ribonucleoprotein cargo. PMID: 21525351 The authors propose that influenza virus ribonucleoproteins are routed from the nucleus to the pericentriolar recycling endosome (RE), where they access a Rab11-dependent vesicular transport pathway to the cell periphery. PMID: 21307188 Rabin8 and Rab11 are associated with the Bardet-Biedl syndrome. PMID: 21273506 Rab11a, but not Rab8a, is required for recycling of transferrin in nonpolarized cells. PMID: 21282656 Rab11a played a prominent role in recycling of the wild type ss1-adrenergic receptors because dominant negative rab11a inhibited. PMID: 20727405 Rab11a is an important regulator of TLR4 and Toll-receptor-associated molecule transport to E. coli phagosomes thereby controlling IRF3 activation from this compartment. PMID: 20933442 Mutant prion protein expression is associated with an alteration of the Rab GDP dissociation inhibitor alpha (GDI)/Rab11 pathway. PMID: 19996123 Results describe the involvement of two Rab GTPases, Rab9 and Rab11, in the trafficking of TRPC6. PMID: 20346379 Transmission electron microscopy of thin sections confirmed that Rab11 depletion resulted in significant numbers of abnormally formed virus particles that had failed to pinch off from the plasma membrane. PMID: 20357086 Rab11, in its GTP-bound form, interacts with Rabin8 and kinetically stimulates the guanine nucleotide-exchange activity of Rabin8 toward Rab8. PMID: 20308558 mutation impairs a specific subset of Rab11 interactions, possibly those involved in cytoskeleton-based movements driving the slow recycling pathway PMID: 14699104

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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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