Recombinant Human RAB10 Protein (denatured)

Name: Recombinant Human RAB10 Protein (denatured)
Brand: Beta LifeScience
SKU: BLA-7521P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P61026
Synonym	GTP binding protein RAB10 Rab10 RAB10 member RAS oncogene family RAB10_HUMAN Ras related GTP binding protein Ras related GTP binding protein RAB10 Ras-related protein Rab-10
Description	Recombinant Human RAB10 Protein (denatured) was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHH SSGLVPRGSH MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT VELQGKKIKL QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI SKWLRNIDEH ANEDVERMLL GNKCDMDDKR VVPKGKGEQI AREHGIRFFE TSAKANINIE KAFLTLAEDI LRKTPVKEPN SENVDISSGG GVTGWKSKCC
Molecular Weight	25 kDa including tags
Purity	>90% SDS-PAGE.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

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. That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane. In epithelial cells, it regulates transport from the Golgi to the basolateral membrane. May play a role in the basolateral recycling pathway and in phagosome maturation. May play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion. Together with LRRK2, RAB8A, and RILPL1, it regulates ciliogenesis. When phosphorylated by LRRK2 on Thr-73, binds RILPL1 and inhibits ciliogenesis.; (Microbial infection) Upon Legionella pneumophila infection promotes endoplasmic reticulum recruitment and bacterial replication. Plays a role in remodeling the Legionella-containing vacuole (LCV) into an endoplasmic reticulum-like vacuole.
Subcellular Location	Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Golgi apparatus membrane. Golgi apparatus, trans-Golgi network membrane. Endosome membrane. Recycling endosome membrane. Cytoplasmic vesicle, phagosome membrane. Cytoplasm, cytoskeleton, cilium basal body. Endoplasmic reticulum membrane. Cytoplasm, perinuclear region.
Protein Families	Small GTPase superfamily, Rab family
Database References	HGNC: 9759 OMIM: 612672 KEGG: hsa:10890 STRING: 9606.ENSP00000264710 UniGene: Hs.467960
Tissue Specificity	Expressed in the hippocampus. Expressed in neutrophils (at protein level).

Gene Functions References

miR378a3p may act as a tumorsuppressor in Esophageal squamous cell carcinoma cells through negatively regulating Rab10. PMID: 29693138
Interrogating Parkinson's disease LRRK2 kinase pathway activity by assessing Rab10 phosphorylation in human neutrophils has been reported. PMID: 29127255
Our results suggest that RAB10 could be a promising therapeutic target for Alzheimer's Disease prevention PMID: 29183403
RAB10 regulates cell survival and proliferation through multiple oncogenic, cell stress and apoptosis pathways. More importantly, high RAB10 expression levels in HCC cells correlated with a poor prognosis in HCC patients. PMID: 28460436
miR-329 also suppresses wound-healing and migration ability of osteosarcoma cells and inhibits tumorigenicity in vivo. Rab10 was identified as a target of miR-329 in osteosarcoma and mediates its biofunction PMID: 27487475
Data suggest that MGCRABGAP is involved in mammalian spermiogenesis by modulating RAB10. PMID: 28067790
the target gene RAB10 regulated by miRNA-369-3p, miRNA-30e-5p, miRNA-30e-3p, and miRNA-655 may play key role in the progression and development of AD. PMID: 26082458
The Anaplasma phagocytophilum surface protein, uridine monophosphate kinase, was identified as a guanine nucleotide-independent, Rab10-specific ligand. PMID: 26289115
Rab10 is a target of the GTPase-activating protein AS160, which is inhibited after phosphorylation by the protein kinase Akt. PMID: 25103239
Rab10 silencing increased the plasma membrane residence of HAS3, resulting in a significant increase of hyaluronan secretion and an enlarged cell surface HA coat, whereas Rab10 overexpression suppressed hyaluronan synthesis. PMID: 24509846
Rab10 regulates endoplasmic reticulum dynamics/morphology. Suggest that these dynamics could be coupled to phospholipid synthesis. PMID: 23263280
Insulin-stimulated GLUT4 protein translocation in adipocytes requires the Rab10 guanine nucleotide exchange factor Dennd4C PMID: 21454697
Rab10 and Rab8A are new cytoplasmic factors implicated in WPB biogenesis that play a role in generating granules that can rapidly respond to secretagogue PMID: 21070595
Rab10, acting upstream of Rab5, plays a prominent role in phagolysosome formation and can modulate Mycobacterium-containing phagosomes maturation PMID: 20028485
Fibronectin 1 and RAB10 show elevated expression in uninvolved psoriatic epidermis. PMID: 15855153
a related Rab protein, Rab10, can interact with myosin Va, myosin Vb, and myosin Vc PMID: 19008234

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.