Recombinant Human Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP) Protein (His)

Name: Recombinant Human Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06880P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Gamma-Aminobutyric Acid Receptor-Associated Protein (GABARAP) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O95166
Target Symbol	GABARAP
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	C-6His
Target Protein Sequence	MKFVYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGQLYQEHHEEDFFLYIAYSDESVYG
Expression Range	1-116aa
Protein Length	Full Length of Mature Protein
Mol. Weight	15.3 kDa
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	Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. Also required for the local activition of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction. Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation. Involved in apoptosis.
Subcellular Location	Endomembrane system. Cytoplasm, cytoskeleton. Golgi apparatus membrane. Cytoplasmic vesicle, autophagosome. Cytoplasmic vesicle.
Protein Families	ATG8 family
Database References	HGNC: 4067 OMIM: 605125 KEGG: hsa:11337 STRING: 9606.ENSP00000306866 UniGene: Hs.647421
Tissue Specificity	Heart, brain, placenta, liver, skeletal muscle, kidney and pancreas.

Gene Functions References

The centrosome and centriolar satellites regulate autophagosome formation by delivery of an ATG8-family member, GABARAP, to the forming autophagosome membrane, the phagophore. Its proposed that GABARAP regulates phagophore expansion by activating the ULK complex. [review] PMID: 28990689
GABAergic synapse is proposed as a focus of aging. (Review) PMID: 28497576
Cardiolipin interaction with various Atg8 human orthologs, namely LC3B, GABARAPL2 and GABARAP, was investigated. PMID: 27764541
Although neither GABARAPs nor LC3s are required for autophagosome biogenesis, loss of all Atg8s yields smaller autophagosomes and a slowed initial rate of autophagosome formation. PMID: 27864321
Development of LC3/GABARAP sensors containing a LIR and a hydrophobic domain to monitor autophagy. PMID: 28320742
GABRP plays an important role in placentation and this pathway may be a promising molecular target for the development of novel therapeutic strategies for preeclampsia. PMID: 27221053
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 by CUL3. PMID: 25684205
Data show that WAC directly binds to GM130 and that this binding is required for autophagosome formation through interacting with GABARAP regulating its subcellular localization. PMID: 26687599
The interaction of GABARAP with Mulan-Ube2E3 supports the role of Mulan as an important regulator of mitophagy. PMID: 25224329
The FLCN-GABARAP association is modulated by the presence of either folliculin-interacting protein (FNIP)-1 or FNIP2 and further regulated by ULK1. PMID: 25126726
A functional complementation of an lgg-1 null mutant with human GABARAP, its closer homolog showed that it localizes to autophagosomes and can rescue LGG-1 functions in the early embryo. PMID: 25126728
PLEKHM1 regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3/GABARAP proteins. PMID: 25498145
GABARBP dramatically inhibited VEGF-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 phosphorylation in vitro. PMID: 24686084
knockdown of LC3B but not GABARAPs resulted in significant accumulation of p62/Sqstm1, one of the selective substrates for autophagy PMID: 24582747
These results support the regulatory role of Bcl-2 in autophagy and define GABARAP as a novel interaction partner involved in this intricate connection. PMID: 24240096
Taken together, our results indicate that GABARBP can regulate the pro-apoptotic activity of cisplatin via the upregulation of p53 expression. PMID: 23545901
The level of GABARAPs is decreased in Lewy body disease. PMID: 21684337
Evidence suggests that changes in the expression and function of GABA(A) receptors are involved in the pathogenesis of epilepsy (review) PMID: 21376781
Used diffusion-ordered nuclear magnetic resonance spectroscopy to study the temperature and concentration dependence of the diffusion properties of GABARAP. PMID: 20665069
DLG4/PSD95 and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism. PMID: 20111057
analysis of human NSF possible binding mode to GABARAP and GATE-16 PMID: 19533740
Sequence-specific 1H, 13C and 15N resonance assignments of human GABA receptor associated protein. PMID: 11727985
Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABA(A) receptor associated protein (GABARAP). PMID: 11727986
We present the three-dimensional structure of GABARAP obtained by x-ray diffraction at 1.75 A resolution PMID: 11729197
Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p PMID: 11825910
Solution structure of human GABA(A) receptor-associated protein GABARAP: implications for biolgoical funcrion and its regulation PMID: 11875056
Gec1/GABARAPL1 was more expressed than GABARAP in the central nervous system (CNS), while GABARAP was more expressed in endocrine glands. PMID: 14625090
GABARAP mRNA expression and protein expression were significantly down-regulated in invasive ductal and invasive lobular carcinomas; GABARAP acts via a vesicle transport mechanism as a tumor suppressor in breast cancer. PMID: 15695379
GABARAP and DDX 47 are involved in the apoptotic process PMID: 15977068
Phosphatidylserine and phosphatidylethanolamine are targets of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16 PMID: 16303767
GABARAP does not alter receptor kinetics directly, but by facilitating surface expression of alphabetagamma receptors. PMID: 16339017
Results suggest that lysosomal turnover of GABARAP-PL is activated during the differentiation of C2C12 cells to myotubes without inactivation of the mTor kinase-signaling pathway. PMID: 16874098
GABARAP and DLG4 genes are involved in the etiology of nicotine dependence in European-American smokers. PMID: 17164261
The association of structurally altered GABARAP protein together with GABA(A) receptor downstream of Ca2+/calmodulin-dependent protein kinase II (CAMKII) activation is essential for long-term potentiation. PMID: 17581966
The X-ray structure of the soluble form of human GABA(A) receptor-associated protein complexed with a high-affinity synthetic peptide at 1.3 A resolution, is presented. PMID: 18638487
Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general. PMID: 19154346
The proapoptotic protein Nix/Bnip3L was found to be a potential GABARAP ligand. PMID: 19363302

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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.