Recombinant Human ARL2BP Protein

Name: Recombinant Human ARL2BP Protein
Brand: Beta LifeScience
SKU: BLA-12222P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	Q9Y2Y0
Synonym	ADP ribosylation factor like 2 binding protein ADP-ribosylation factor-like protein 2-binding protein AR2BP_HUMAN Arf like 2 binding protein BART1 ARF-like 2-binding protein ARL2 binding protein Arl2bp ARL2BP protein BART BART1 Binder of ARF2 protein 1 Binder of Arl Two Binder of Arl2 Retinitis pigmentosa 66 (autosomal recessive) RP66
Description	Recombinant Human ARL2BP Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMDALEGESFALSFSSASDAEFDAVVGYLED IIMDDEFQLLQRNFMDKYYLEFEDTEENKLIYTPIFNEYISLVEKYIEEQ LLQRIPEFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRA EKEGRGLDLSSGLVVTSLCKSSSLPASQNNLRH
Molecular Weight	21 kDa including tags
Purity	Greater than 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	Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2.
Subcellular Location	Cytoplasm. Mitochondrion intermembrane space. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, cilium basal body.
Protein Families	ARL2BP family
Database References	HGNC: 17146 OMIM: 615407 KEGG: hsa:23568 STRING: 9606.ENSP00000219204 UniGene: Hs.632873
Associated Diseases	Retinitis pigmentosa with or without situs inversus (RPSI)
Tissue Specificity	Expressed in retina pigment epithelial cells (at protein level). Widely expressed.

Gene Functions References

This study identified two homozygous variants in ARL2BP as a rare cause of autosomal recessive retinitis pigmentosa. Further studies are required to define the underlying disease mechanism causing retinal degeneration as a result of mutations in ARL2BP and any phenotype-genotype correlation associated with residual levels of the wild-type transcript. PMID: 30210231
Subsequent analysis of 844 index cases did not reveal further pathogenic chances in ARL2BP indicating that mutations in ARL2B are a rare cause of arRCD (about 0.1%) in a large cohort of French patients. PMID: 27790702
Alteration of EBV encoded miR-BART1 expression results in an increase in migration and invasion of nasopharyngeal carcinoma in vitro and causes metastasis in vivo. EBV-miR-BART1 directly targets the cellular tumour suppressor PTEN. PMID: 26135619
EBV also downregulates two immediate early genes by miR-BART20-5p. PMID: 24899173
Mutations in ARL2BP cause autosomal-recessive retinitis pigmentosa. PMID: 23849777
EBV-miR-BART1 could influence the expression of metabolism-associated genes and might be involved in cancer metabolism in nasopharyngeal carcinoma PMID: 23685147
Our results imply that BART regulates actin-cytoskeleton rearrangements at membrane ruffles through modulation of the activity of Rac1, which, in turn, inhibits pancreatic cancer cell invasion. PMID: 22745590
These results imply that BART contributes to regulating PKCalpha activity through binding to ANX7, thereby affecting the invasiveness of pancreatic cancer cells. PMID: 22532868
We identify a subset of BART miRNAs that are restricted to Latency III in normal infection but are up regulated in tumors that express Latency I and II. PMID: 21901094
Our results imply that BART increases active RhoA by inhibiting ARL2 function, which in turn inhibits invasiveness of cancer cells. PMID: 21833473
Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector. PMID: 19368893

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.