Recombinant Human Proteasomal Ubiquitin Receptor Adrm1 (ADRM1) Protein (His-SUMO)

Name: Recombinant Human Proteasomal Ubiquitin Receptor Adrm1 (ADRM1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09365P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Proteasomal Ubiquitin Receptor Adrm1 (ADRM1) 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	Q16186
Target Symbol	ADRM1
Synonyms	110 kDa cell membrane glycoprotein; adhesion regulating molecule 1; Adhesion-regulating molecule 1; ADRM 1; Adrm1; ADRM1_HUMAN; ARM 1; ARM-1; ARM1; Gp110; hRpn13; M(r) 110,000 surface antigen; Proteasomal ubiquitin receptor ADRM1; proteasome regulatory particle non ATPase 13; Proteasome regulatory particle non-ATPase 13; Regulatory particle non ATPase 13; Rpn13; Rpn13 homolog
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	TTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCWKDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHCRKVNEYLNNPPMPGALGASGSSGHELSALGGEGGLQSLLGNMSHSQLMQLIGPAGLGGLGGLGALTGPGLASLLGSSGPPGSSSSSSSRSQSAAVTPSSTTSSTRATPAPSAPAAASATSPSPAPSSGNGASTAASPTQPIQLSDLQSILATMNVPAGPAGGQQVDLASVLTPEIMAPILANADVQERLLPYLPSGESLPQTADEIQNTLTSPQFQQALGMFSAALASGQLGPLMCQFGLPAEAVEAANKGDVEAFAKAMQNNAKPEQKEGDTKDKKDEEEDMSLD
Expression Range	2-407aa
Protein Length	Full Length of Mature Protein
Mol. Weight	58.0kDa
Research Area	Signal Transduction
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	Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. Within the complex, functions as a proteasomal ubiquitin receptor. Engages and activates 19S-associated deubiquitinases UCHL5 and PSMD14 during protein degradation. UCHL5 reversibly associate with the 19S regulatory particle whereas PSMD14 is an intrinsic subunit of the proteasome lid subcomplex.
Subcellular Location	Cytoplasm. Nucleus.
Protein Families	ADRM1 family
Database References	HGNC: 15759 OMIM: 610650 KEGG: hsa:11047 STRING: 9606.ENSP00000253003 UniGene: Hs.90107

Gene Functions References

Rpn13-Rpn2 complex structural analysis shows that RA190 targets hRpn13 and Uch37 through parallel mechanisms and at proteasomes, RA190-inactivated Uch37 cannot disassemble hRpn13-bound ubiquitin chains PMID: 28598414
findings indicate that up-regulated ADRM1 was involved in intrahepatic cholangiocarcinoma (ICC) progression and suggest the potential clinical application of ADRM1 inhibitors (e.g., RA190 and KDT-11) for ICC treatment. PMID: 29913454
We show that ADRM1 mRNA overexpression is an early event in high grade serous carcinoma of the ovary. This is associated with TP53 mutation and increased burden of misfolded proteins in carcinomas that likely renders the cancer cells particularly sensitive to RPN13 inhibitors. PMID: 28784174
evidence that the interaction can mediate the association of Rpn13 and SGTA in a cellular context. PMID: 27827410
The structures of proteasome substrate receptor complexes with the shuttle factors that deliver ubiquitinated proteins to proteasomes have been solved, namely human Rpn13 complexed with PLIC2 and Saccharomyces cerevisiae Rpn1 with Rad23. PMID: 27396824
RPN13 binds ubiquitin with an affinity similar to that of other proteasome-associated ubiquitin receptors and that RPN2, ubiquitin, and the deubiquitylase UCH37 bind to RPN13 with independent energetics. PMID: 28442575
regulation of NY-ESO-1 processing by the ubiquitin receptors Rpn10 and Rpn13 as a well as by the standard and immunoproteasome is governed by non-canonical ubiquitination on non-lysine sites. PMID: 26903513
this work implicates hRpn13 and Uch37 in cell cycle progression, providing a rationale for their function in cellular proliferation and for the apoptotic effect of the hRpn13-targeting molecule RA190. PMID: 26907685
the binding of SGTA to Rpn13 enables specific polypeptides to escape proteasomal degradation and/or selectively modulates substrate degradation. PMID: 26169395
Data suggest that ADRM1 is involved in proliferation of acute leukemia cells; expression of ADRM1 is up-regulated in leukemia; knockdown of ADRM1 inhibits cell proliferation at G0/G1 phase of cell cycle but does not affect apoptosis/cell migration. PMID: 25896055
findings implicate Rpn13 in linking parkin to the 26 S proteasome and regulating the clearance of mitochondrial proteins during mitophagy PMID: 25666615
Data show that DEUBAD domain in RPN13 (ADRM1) activates ubiquitin thioesterase L5 (UCH-L5), and the related DEUBAD domain in INO80G (NFRKB) inhibits UCH-L5. PMID: 25702870
Together, our findings suggest that the interaction of Psmd1 with Adrm1 is controlled by SUMOylation in a manner that may alter proteasome composition and function. PMID: 24910440
ADRM1 is a candidate target gene in the chromosome 20q13.33 amplicon that may possibly be linked to development of gastric cancer PMID: 24968865
Autoubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates. PMID: 24811749
Inherent asymmetry in the 26S proteasome is defined by the ubiquitin receptor RPN13. PMID: 24429290
mRNA and protein levels of ADRM1 were increased in hepatocellular carcinoma tissues and was parallel to the metastatic potential PMID: 22576803
hRpn13 modulates the influence of osteoblasts on osteoclasts by controlling the stability of regulatory proteins in osteoblasts. PMID: 22057889
this study provides a possible mechanism of action in ovarian cancer for amplification and overexpression of ADRM1 PMID: 21432940
In tumor cells non-phosphorylated DeltaNp63alpha failed to form protein complexes with Rpn13, allowing the latter to bind and target LKB1 into a proteasome-dependent degradation pathway, modulating cisplatin-induced autophagy. PMID: 21191146
Phosphorylated TP63 induces transcription of RPN13, leading to NOS2 protein degradation PMID: 20959455
Silencing of Adrm1 by RNA interference can significantly suppress proliferation of colorectal cancer cells through inducing apoptosis and arresting the cell cycle. PMID: 20137344
show that Rpn13 is involved in inducible nitric oxide synthase degradation and is required for iNOS interaction with the deubiquitination protein UCH37. PMID: 20634424
results suggest that there is different substrate specificity between S5a and hRpn13 at the level of delivery and S5a may be the major docking site for ERAD substrates. PMID: 20417181
Rpn13 binding to the proteasome scaffolding protein hRpn2/S1 abrogates its interdomain interactions, thus activating hRpn13 for ubiquitin binding. PMID: 20471946
ARM-1 is a cytosolic protein associated with the plasma membrane. However, no cell surface expression of the protein was observed. These results suggest an indirect role of ARM-1 in adhesion rather than a direct role as an adhesion molecule itself.[ARM-1] PMID: 15819879
Adrm1 has a specialised role in proteasome function. Identified Adrm1 as a novel component of the regulatory ATPase complex of the 26 S proteasome PMID: 16815440
Neither Uch37 alone nor the Uch37-Adrm1 or Uch37-Adrm1-S1 complexes can hydrolyse di-ubiquitin efficiently; rather, incorporation into the 19S complex is required to enable processing of polyubiquitin chains. PMID: 16906146
These results indicate that hRpn13 (Adrm1) is essential for the activity of UCH37. PMID: 16990800
In human 26S proteasomes, hRpn13 appears to be important for the binding of UCH37 to the 19S complex and for efficient proteolysis. PMID: 17139257
identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome PMID: 18497817
ADRM1 overexpression was the most highly correlated with amplification and is associated with ovarian cancer. PMID: 18615678
Adrm1 is potentially oncogenic and may play an important role in colon tumorigenesis PMID: 19148532
these data suggest that Adrm1, a new Atp6v0d2-interacting protein, plays an important role in osteoclast differentiation, and in particular the fusion of preosteoclasts. PMID: 19818731

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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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