Recombinant Human Comm Domain-Containing Protein 1 (COMMD1) Protein (GST)

Name: Recombinant Human Comm Domain-Containing Protein 1 (COMMD1) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08792P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Comm Domain-Containing Protein 1 (COMMD1) 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	Q8N668
Target Symbol	COMMD1
Synonyms	C2orf5; COMD1; COMD1_HUMAN; COMM domain-containing protein 1; COMMD1; Copper metabolism (Murr1) domain containing 1; Copper metabolism domain containing 1; Copper metabolism gene MURR1; Copper metabolism MURR1 domain-containing protein 1; MGC27155; MURR1; Protein Murr1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	AAGELEGGKPLSGLLNALAQDTFHGYPGITEELLRSQLYPEVPPEEFRPFLAKMRGILKSIASADMDFNQLEAFLTAQTKKQGGITSDQAAVISKFWKSHKTKIRESLMNQSRWNSGLRGLSWRVDGKSQSRHSAQIHTPVAIIELELGKYGQESEFLCLEFDEVKVNQILKTLSEVEESISTLISQPN
Expression Range	1-190aa
Protein Length	Full Length
Mol. Weight	48.0kDa
Research Area	Epigenetics And Nuclear Signaling
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	Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1; in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription; competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner.
Subcellular Location	Nucleus. Cytoplasm. Endosome membrane. Cytoplasmic vesicle. Early endosome. Recycling endosome. Note=Shuttles between nucleus and cytosol. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins.
Database References	HGNC: 23024 OMIM: 607238 KEGG: hsa:150684 STRING: 9606.ENSP00000308236 UniGene: PMID: 29336469 This study has thus revealed a novel nuclear complex of F-actin, DRR1 and COMMD1 that is involved in NF-kappaB degradation and cell cycle suppression in neuroblastoma cells. PMID: 28604741 these results identify COMMD1 and an E2F-metabolic pathway as key regulators of osteoclastogenic responses under pathological inflammatory conditions PMID: 28723554 The COMMD1 downregulation by miR-205 promotes tumor development by modulating a positive feedback loop that amplifies inflammatory- and stemness-associated properties of cancer cells. PMID: 26586569 COMMD1 plays a critical role in the termination of NF-kappaB activity and the control of pro-inflammatory and pro-labor mediators. PMID: 26733542 COMMD1 expression is associated with poor prognosis in diffuse large B-cell lymphoma PMID: 24625556 COMMD1 is identified as a novel regulator of misfolded protein aggregation. PMID: 24691167 COMMD1 is directly linked to early endosomes through its interaction with a protein complex containing CCDC22, CCDC93, and C16orf62. PMID: 25355947 COMMD1 is acetylated by p300 and that acetylation protects COMMD1 from XIAP-mediated proteosomal degradation PMID: 25074812 IkappaB-alpha protein was stabilized by COMMD1, which attenuated NF-kappaB signaling during Toll-like receptor ligand and tumor necrosis factor alpha treatment and enhanced HIV-1 latency in latently HIV-1-infected cells. PMID: 25520503 These data demonstrate the anti-inflammatory properties of COMMD1 in bronchial epithelial cells and open new therapeutic avenues in cystic fibrosis. PMID: 23892095 Placental COMMD1 expression is increased in women with severe preeclampsia compared to that found in women with normal pregnancies. PMID: 23364987 The role of COMMD1 in copper metabolism and it structure and function are discussed. PMID: 23677795 The results indicate a role for COMMD1 in the regulation of NKCC1 membrane expression and ubiquitination. PMID: 23515529 No major role can be attributed to Atox1 and COMMD in the pathophysiology or clinical variation of Wilson disease. PMID: 22677543 Clusterin and COMMD1 independently regulate degradation of the mammalian copper ATPases ATP7A and ATP7B. PMID: 22130675 These results suggest that COMMD1 downregulates deltaENaC activity by reducing deltaENaC surface expression through promoting internalization of surface deltaENaC to an intracellular recycling pool, possibly via enhanced ubiquitination. PMID: 21741370 Data show that COMMD1 interacts with CFTR. This interaction promotes CFTR cell surface expression as assessed by biotinylation experiments in heterologously expressing cells through regulation of CFTR ubiquitination. PMID: 21483833 We argue that COMMD1 participates in the normal disposition of copper within the hepatocyte and we speculate about that role. PMID: 21275100 COMMD1 as a novel protein regulating SOD1 activation and associate COMMD1 function with the production of free radicals. PMID: 20595380 report a single novel, putative mutation in COMMD1 in one Wilson disease (WD) patient with atypical features; absence of any other prospective mutations among 108 patients suggests that COMMD1 variants are not major contributors towards WD phenotypes PMID: 20550661 Elevated levels of sCLU promote prostate cancer cell survival by facilitating degradation of COMMD1 and I-kappaB, thereby activating the canonical NF-kappaB pathway. PMID: 20068069 COMMD1 has a role in conjunction with HSP90beta/HSP70 in the ubiquitin and O(2)-independent regulation of HIF-1alpha PMID: 19802386 These data identify a new role for COMMD1 in regulating the nuclear/nucleolar distribution of RelA PMID: 20048074 No mutations in the MURR1 gene, including the intron-exon boundaries, were identified in a total of 23 patients with non-Wilsonian hepatic copper toxicosis PMID: 12547404 findings reveal involvement of Murr1 in the defined pathway of hepatic biliary copper excretion, suggest a mechanism for Murr1 function in this process, and provide evidence in support of the proposed role of the MURR1 gene in hepatic copper toxicosis PMID: 12968035 MURR1 was detected in different tissues and cell lines; in cell lines it was found both in cytosol and membrane preparations; in some cells MURR1 was associated with a vesicular compartment diffusely localized throughout the cell PMID: 14568250 Murr1 is a novel regulator of delta ENaC PMID: 14645214 Murr1, a gene product known previously for its involvement in copper regulation, inhibits HIV-1 growth in unstimulated CD4+ T cells PMID: 14685242 XIAP functions through MUUR1 to regulate copper homeostasis. PMID: 14685266 3 intronic base pair changes, 1 new sequence variation & 2 known polymorphisms were detected, including the GAT/GAC heterozygous state at Asn 164 in 24% of the patients. GAT/GAC heterozygosity at Asn 164 is associated with earlier onset of Wilson disease. PMID: 15205742 MURR1/COMMD1 functions in the nucleus by affecting the association of NF-kappaB with chromatin PMID: 15799966 COMMD1 is not a significant contributor to Wilson-like copper storage disorders in humans. PMID: 16283886 These data support the significance of COMMD protein-protein interactions and provide new mechanistic insight into the function of this protein family in NF-kappaB signalling. PMID: 16573520 The solution structure of the N-terminal domain of COMMD1 (N-COMMD1, residues 1-108), is presented. PMID: 17097678 COMMD1 accelerates the ubiquitination and degradation of NF-kappaB subunits through its interaction with a multimeric ubiquitin ligase containing Elongins B and C, Cul2 and SOCS1 (ECS(SOCS1)). PMID: 17183367 COMMD1 specifically binds copper as Cu(II) in 1:1 stoichiometry & does not bind other divalent metals. Fluorescence studies of single point mutants of the full-length protein revealed the involvement of M110 in addition to H134 in direct Cu(II) binding. PMID: 17309234 Implicate COMMD1 in the pathogenesis of Wilson's disease and indicate that COMMD1 exerts its regulatory role in copper homeostasis through the regulation of ATP7B stability. PMID: 17919502 the ability to promote Lys(63)-mediated polyubiquitination of COMMD1 is a novel property of ARF independent of p53 PMID: 18305112 COMMD1 expression is controlled primarily by protein ubiquitination PMID: 18795889 COMMD1 is a scaffold protein in a distinct sub-compartment of endocytic pathway and offer first clues to its role as a regulator of structurally unrelated membrane transporters. PMID: 18940794 Data suggest that translocation of ATP7B takes place independently of Rab7-regulated endosomal traffic, and that Murr1 plays a role in a later step of the copper excretion pathway but is not involved in the translocation of the Wilson disease protein. PMID: 18974300

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.