Recombinant Human Rb1-Inducible Coiled-Coil Protein 1 (RB1CC1) Protein (His&Myc)

Name: Recombinant Human Rb1-Inducible Coiled-Coil Protein 1 (RB1CC1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-11239P
Availability: InStock

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) RB1CC1.

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Product Overview

Description	Recombinant Human Rb1-Inducible Coiled-Coil Protein 1 (RB1CC1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q8TDY2
Target Symbol	RB1CC1
Synonyms	FAK family kinase-interacting protein of 200 kDa; FIP200; RB1-inducible coiled-coil protein 1; RB1CC1; RBCC1_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	AIQTALKEFKLEREVVEKELLEKVKHLENQIAKSPAIDSTRGDSSSLVAELQEKLQEEKAKFLEQLEEQEKRKNEEMQNVRTSLIAEQQTNFNTVLTREKMRKENIINDLSDKLKSTMQQQERDKDLIESLSEDRARLLEEKKKLEEEVSKLRSSSFVPSPYVATAPELYGACAPELPGESDRSAVETADEGRVDSAMETSMMSVQENIHMLSEEKQRIMLLERTLQLKEEENKRLNQRLMSQSMSSVSSRHSEKIAIRDFQVGDLVLIILDERHDNYVLFTVSPTLYFLHSESLPALDLKPGEGASGASRRPWVLGKVMEKEYCQAKKAQNRFKVPLGTKFYRVKAVSWNKKV
Expression Range	1241-1594aa
Protein Length	Partial
Mol. Weight	47.7 kDa
Research Area	Others
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	Involved in autophagy. Regulates early events but also late events of autophagosome formation through direct interaction with Atg16L1. Required for the formation of the autophagosome-like double-membrane structure that surrounds the Salmonella-containing vacuole (SCV) during S.typhimurium infection and subsequent xenophagy. Involved in repair of DNA damage caused by ionizing radiation, which subsequently improves cell survival by decreasing apoptosis. Inhibits PTK2/FAK1 and PTK2B/PYK2 kinase activity, affecting their downstream signaling pathways. Plays a role as a modulator of TGF-beta-signaling by restricting substrate specificity of RNF111. Functions as a DNA-binding transcription factor. Is a potent regulator of the RB1 pathway through induction of RB1 expression. Plays a crucial role in muscular differentiation. Plays an indispensable role in fetal hematopoiesis and in the regulation of neuronal homeostasis.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasm, cytosol. Preautophagosomal structure. Lysosome.
Protein Families	ATG17 family
Database References	HGNC: 15574 OMIM: 606837 KEGG: hsa:9821 STRING: 9606.ENSP00000025008 UniGene: PMID: 30075197 These findings suggested that PHF8 played an oncogenic role in facilitating FIP200-dependent autophagic degradation of E-cadherin, EMT and metastasis in hepatocellular carcinoma (HCC). PHF8 might be a promising target for prevention, treatment and prognostic prediction of HCC. PMID: 30180906 miR-224-3p regulates autophagy in hrHPV-induced cervical cancer cells through targeting FIP200 expression. PMID: 27615604 Data suggest that, in patients with diabetic kidney disease, urinary excretion of mRNAs for MAP1LC3A, WIPI2, and RB1CC1 is down-regulated as compared to healthy control subjects; these transcripts may serve as urinary autophagy biomarkers. (MAP1LC3A = microtubule associated protein 1 light chain 3; WIPI2 = WD repeat domain phosphoinositide-interacting protein 2; RB1CC1 = RB1 inducible coiled-coil 1) PMID: 28760651 This is the first report demonstrating that polymorphisms in the autophagy-related FIP200 gene may predict hypertension in patients with mCRC treated with FOLFIRI and bevacizumab. PMID: 28347919 MiR-20a and miR-20b negatively regulate autophagy by targeting RB1CC1/FIP200 in breast cancer cells PMID: 26829385 RB1CC1 has been implicated in cell cycle progression, cell growth, cell proliferation, cell survival, cell spreading/migration and neurodegeneration. PMID: 26151896 miR-133b targeted and downregulated RB1CC1 in prostate cancer cells. PMID: 24610824 RB1CC1 knockdown in PC3 cells enhances clonal growth in vitro and tumor growth in vivo. PMID: 24732589 Liver-specific deficiency of FIP200 leads to chronic liver injury associated with fibrosis and inflammation. PMID: 23960084 The APC-independent beta-catenin degradation by FIP200 suggests a role for FIP200 in tumor suppression in the presence of APC dysfunction. PMID: 22751121 Interaction between FIP200 and ATG16L1 distinguishes ULK1 complex-dependent and -independent autophagy. PMID: 23262492 Nuclear expression of RB1CC1 predicts a better clinical outcome and is useful in the follow-up of salivary gland cancers. PMID: 21717524 analysis of preparation of the monoclonal antibody for RB1CC1 PMID: 22396748 RB1CC1 protein suppresses type II collagen synthesis in chondrocytes and causes dwarfism PMID: 22049074 p53 regulates autophagy through a direct molecular interaction with RB1CC1/FIP200, a protein that is essential for the very apical step of autophagy initiation. PMID: 21775823 RB1CC1 activates the expression of p16 (also called INK4a/CDKN2a) through the activation of its promoter. RB1CC1 essentially requires binding with hSNF5 to activate the p16 promoter. PMID: 21637919 RB1CC1 thus appears to play a unique role as a modulator of TGF-beta signaling by restricting substrate specificity of Arkadia. PMID: 21795712 downregulation of FIP200 protein in glioblastoma tumor cells, astrocytes, and brain microvessel endothelial cells promotes apoptosis, most likely due to the removal of a direct interaction of FIP200 with Pyk2 that inhibits Pyk2 activation PMID: 21602932 RB1CC1, RB1 and p53 have prognostic roles in breast cancer in Japanese patients PMID: 21203526 present study indicates that RB1CC1 together with hSNF5 and/or p53 enhances the RB1 pathway through transcriptional activation of RB1, p16 and p21 PMID: 20614030 the 3'-untranslated region of RB1-inducible coiled-coil 1 gene is mutated in colon tumors PMID: 19888451 RB1CC1 is frequently mutated in breast cancer and shows characteristics of a classical tumor-suppressor gene. PMID: 12068296 RB1CC1 gene preferentially expressed and contributed to the maturation of human embryonic musculoskeletal cells, and may regulate the proliferative activity and maturation of tumor cells derived from these tissues. PMID: 12163359 RB1CC1 induces the expression of RB1, especially of underphosphorylated forms, then suppresses cell cycle progression in human neoplastic cells PMID: 14533007 expression and promoter activities of RB1CC1 in developing murine and human tissues; RB1CC1 expression is controlled more stringently by modification at intron 1 in humans than in mice PMID: 15375585 FIP200 regulates of cell size by interaction with the TSC1-TSC2 complex. PMID: 16043512 FIP200 increases p21 protein levels via stabilization of its upstream regulator p53 and decreases cyclin D1 protein. Both effects are critical for FIP200-induced G1 arrest and may contribute to the antitumor activities of FIP200 in breast cancer. PMID: 16061648 RB1CC1 insufficiency causes neuronal atrophy through mTOR signaling alteration and involved in the pathology of Alzheimer's diseases. PMID: 17706618 RB1CC1 and PACE4 genes might be the DNA targets of sodium arsenite treatment in human lymphoblastoid cells. PMID: 17707572 Cellular functions of FIP200 and its interacting proteins, and the emerging roles of FIP200 in embryogenesis and cancer development. Review. PMID: 18036779 provide the first evidence for the existence of a close-spatially controlled-mode of regulation of FIP200 and PIASy nucleocytoplasmic functions PMID: 18285457 These results suggest that FIP200 is a novel mammalian autophagy factor that functions together with ULKs. PMID: 18443221 Nuclear RB1CC1 directly activates the RB1 promoter to enhance RB1 expression associated with breast cancer. PMID: 19437535 Nuclear RB1CC1 directly activates the RB1 promoter to enhance RB1 expression in cancer cells. PMID: 19437535 Rb1cc1 expression is a prerequisite for the induction of RB1 and myosin heavy chain. Rb1cc1 plays a crucial role in muscular differentiation and function. PMID: 15968549

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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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