Recombinant Human Ras-Related Protein Rab-1A (RAB1A) Protein (GST)

Name: Recombinant Human Ras-Related Protein Rab-1A (RAB1A) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-02359P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Ras-Related Protein Rab-1A (RAB1A) 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	P62820
Target Symbol	RAB1A
Synonyms	GTP binding protein RAB 1A; mKIAA3012; RAB 1; Rab 1A; RAB1; RAB1, member RAS oncogene family; Rab1A; RAB1A member RAS oncogene family; RAB1A_HUMAN; Ras related protein Rab 1A; Ras-associated protein RAB1; Ras-related protein Rab-1A; YPT1; YPT1 related protein; YPT1-related protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	SSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC
Expression Range	2-205aa
Protein Length	Full Length of Mature Protein
Mol. Weight	49.5kDa
Research Area	Transport
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. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport.
Subcellular Location	Golgi apparatus. Endoplasmic reticulum. Early endosome. Cytoplasm, cytosol. Membrane. Melanosome.
Protein Families	Small GTPase superfamily, Rab family
Database References	HGNC: 9758 OMIM: 179508 KEGG: hsa:5861 STRING: 9606.ENSP00000387286 UniGene: Hs.310645

Gene Functions References

he present study demonstrated that DANCR/miR-634/RAB1A axis plays crucial roles in the progression of glioma, and DANCR might potentially serve as a therapeutic target for the treatment of glioma patients. PMID: 29301870
Rab1 is regulated by the host in a similar fashion, and that the innate immunity kinase TAK1 and Legionella effectors compete to regulate Rab1 by switch II modifications during infection. PMID: 27482120
Rab1A may be involved in the pathogenesis of human lung cancer in an mTOR- and MAPK-independent manner. PMID: 27902464
In clinical samples, the expression of Rab1A or DHX33 was reversely correlated with miR-634. Re-expression of Rab1A or DHX33 abrogated the miR-634-mediated inhibition of cell proliferation and migration. Collectively, our data suggest a tumor suppressor role of miR-634 in hepatocellular carcinoma. PMID: 27693040
New Rab1 binding sites have been discovered using an ensemble of clustering methods. PMID: 28120477
Leucine-rich repeat kinase 2 (LRRK2) can interact with several Rab proteins, and such ractions may serve to recruit LRRK2 to distinct subcellular organelles to phosphorylate select substrate proteins involved in membrane trafficking events. PMID: 28202668
As a Rab1a effector, C9orf72 controls initiation of autophagy by regulating the Rab1a-dependent trafficking of the ULK1 autophagy initiation complex to the phagophore. PMID: 27334615
our data indicate that miR-1202 suppresses proliferation and induces endoplasmic reticulum stress and apoptosis through targeting and inhibiting Rab1A in glioma cells. These results suggest miR-1202 as a potential therapeutic target for the treatment of glioma patients. PMID: 28443461
Upregulation of RAB1A is associated with triple-negative breast cancer. PMID: 28184936
For RAB1A, a high accuracy for the discrimination of human hepatocellular carcinoma and nontumorous liver tissue was observed. PMID: 27467182
The ability of Rab1 to regulate WHAMM and the Arp2/3 complex represents a distinct strategy for membrane remodeling in which a Rab G-protein recruits the actin nucleation machinery but dampens its activity. PMID: 26823012
Rab1A isoform 3 shows enhanced basal activity and is not controlled by accessory proteins PMID: 26953259
Results demonstrate that ALS-mutant forms of TDP-43, FUS, and SOD1 all perturb protein transport in the early secretory pathway between ER and Golgi compartments, and imply that restoring Rab1-mediated ER-Golgi transport is a novel ALS therapeutic target PMID: 26298469
Rab1A-dependent activation of mTORC1 has as role in amino acid signaling promotes growth and metastasis of hepatocellular carcinomas PMID: 26308575
Overexpression of RAB1A is associated with hepatocellular carcinoma. PMID: 26023735
Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP PMID: 25649263
Rab1A knockdown induced cell death by inhibition of autophagosome formation. PMID: 24801886
Vaccinia virus can be added to the growing list of viruses which require RAB1A for optimal replication, highlighting this protein as a broadly proviral host factor. PMID: 25462347
hyperactive amino acid signaling through Rab1A overexpression drives oncogenesis and renders cancer cells prone to mTORC1-targeted therapy. PMID: 25446900
A major biological consequence of upregulation of miR-221 is reprogramming of androgen receptor signaling via downregulation of HECTD2 and RAB1A. PMID: 23770851
Rab1A can rescue the Golgi fragmentation caused by the overabundance of alpha-synuclein in nigral dopaminergic neurons, improving the ability of the surviving neurons to control motor function in hemiparkinsonian animals. PMID: 23939344
These data indicate that Rab1a is an important regulator of early endosome sorting for multiple cargo species. PMID: 24407591
evidence for a remarkable adaptation of SidD to its host cell target Rab1 which explains how this effector confers specificity to the reaction it catalyses. PMID: 23696742
The transition state mimetic structure of the Legionella pneumophila GAP LepB in complex with Rab1, is reported. PMID: 23821544
Rab1a and Rab5a preferentially bind to binary lipid compositions with higher stored curvature elastic energy. PMID: 23815289
Findings show that Ypt1/Rab1 infindings show that Ypt1/Rab1 interacts with Atg1/Ulk1 in yeast and mammalian cells. PMID: 23716696
analysis of APPL1 and APPL2 proteins and their interaction with Rab PMID: 23055524
the potential interaction of Rab1 and its effect on export from the endoplasmic reticulum PMID: 22628317
The NS5A interaction with TBC1D20 and Rab1 is essential for the viral life cycle. PMID: 22491470
When bound to Rab1, LidA interfered with the covalent modification of Rab1 by phosphocholination or AMPylation, and it also blocked de-AMPylation of Rab1 by SidD and dephosphocholination by Lem3. PMID: 22228731
Rab1a/b and Rab43, are important for herpes simplex virus 1 virion assembly PMID: 21680502
Antibacterial autophagy occurs at omegasomes and reveal that the Rab1 GTPase plays a crucial role in mammalian autophagy. PMID: 20980813
Results suggest a novel function for Rab1a in the regulation of cell migration through controlling integrin beta1 recycling and localization to lipid rafts via a specific downstream effector pathway. PMID: 20639577
Studies determined the crystal structures of Legionella pneumophila SidM alone (residues 317-647) and SidM (residues 193-550) in complex with nucleotide-free WT Rab1. PMID: 20176951
Results indicate that Rab1 and Rab43 are key Rabs required for the biogenesis and maintenance of a functional Golgi structure, and suggest that other Rabs acting at the Golgi complex are likely to be functionally redundant. PMID: 17684057
TBC1D20 was found to be the first known GAP for Rab1, which is implicated in the regulation of anterograde traffic between the endoplasmic reticulum and the Golgi complex PMID: 17901050
depletion of GM130 by RNA interference slows the rate of ER to Golgi trafficking in vivo; interactions of GM130 with syntaxin 5 and Rab1 are regulated by mitotic phosphorylation PMID: 18167358
Results suggest a model where protein trafficking and neuronal differentiation are directly linked by the interaction of Rab1 and its regulator GTRAP3-18. PMID: 18363836
Rab 1 S25N mutants efficiently blocked the plasma membrane trafficking of the Kir3.1/Kir3.4 complex however they did not block the Gbeta1gamma2/Kir3.1 interaction. PMID: 19135528
Rab1 GTPase and dimerization modulate export traffic from the emndoplasmic reticulum to the cell surface of newly synthesized angiotensin II type 2 receptor. PMID: 19357319

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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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