Recombinant Rat Retinoblastoma-Associated Protein (RB1) Protein (His)

Name: Recombinant Rat Retinoblastoma-Associated Protein (RB1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-08268P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Rat Retinoblastoma-Associated Protein (RB1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P33568
Target Symbol	RB1
Synonyms	Rb1; Rb-1; Retinoblastoma-associated protein; pRb; Rb; pp105
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	KDLPHAAQETFKRVLIREEEFDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFSSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGGNPPKPLKKLRFDIEGSDEADGSKHLPAESKFQQKLAEMTSTRTRMQKQKLNDSMEISNKEE
Expression Range	721-919aa
Protein Length	Partial
Mol. Weight	26.6kDa
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	Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle. The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes. Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription. Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase. RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex.
Subcellular Location	Nucleus.
Protein Families	Retinoblastoma protein (RB) family
Database References	KEGG: rno:24708 STRING: 10116.ENSRNOP00000021752 UniGene: PMID: 27056896 Inflammation disrupts LDLr feedback regulation through the activation of the mTOR pathway, increasing mTORC1 activity and up-regulating SREBP-2-mediated cholesterol uptake through Rb phosphorylation. PMID: 24068000 Phosphorylated retinoblastoma protein (p-Rb) is involved in neuronal apoptosis after traumatic brain injury in adult rats. PMID: 23371354 a role for Rb protein in directing oncogenic cell growth PMID: 22885065 Rb pathway may only be involved in early neuronal apoptosis and may be not an apoptotic signal in the late stages of transient cerebral ischemia. PMID: 19123049 Results indicate that HIV-infection in the brain is associated with site-specific hyperphosphorylation of pRb at serine795, and that this phosphorylation contributes to neuronal death in this disease. PMID: 21504794 Data show that proliferaton and nuclear expression of cyclin D1 and p-Rb coincide with the early phase of cyst growth, suggesting that there might be a therapeutic window in which cyclin-dependent kinase inhibitors are most effective in ARPKD. PMID: 20924203 proliferative lesions activate the cell cycle machinery following tumor promotion via a regulatory mechanism involving inactivation of GSK3beta and retinoblastoma protein PMID: 19505811 These data demonstrate how a new molecular network on ATM regulates the cell cycle through the control of pRb phosphorylation. PMID: 20213763 Expression of Rb is closely event-related to malignant transformation and conversion of the oral mucosa, and is a reliable biomarker linked to oral cancer pathogenesis. PMID: 20023236 employs both canonical cyclin-dependent kinase/cyclin regulation and metabolic regulation as a means to limit proliferation, underscoring its potency in tumor suppression PMID: 12221087 Rb is present in rat and human islets, and overexpression of cyclin D(1)/cdk-4 led to strikingly enhanced Rb phosphorylation. PMID: 14693709 Mitogen-induced rapid phosphorylation of serine 795 of the retinoblastoma gene product in vascular smooth muscle cells involves ERK activation PMID: 15069084 MyoD may function in myonuclei in response to denervation to protect against denervation-induced apoptosis via perhaps the activation of p21 and Rb PMID: 15084472 continued RB action is required for the maintenance of two kinetically and functionally distinct modes of replication inhibition PMID: 15169903 RB plays a role in the early neural differentiation of mysenchymal stem cells through histone deacetylases dependent pathways. PMID: 15459751 the derepression of Rb-E2F-regulated genes leads to apoptosis through inactivation of focal adhesion kinase and activation of caspase-8 PMID: 15640164 Caspase-9 antagonizes p53-induced apoptosis by generating a p76(Rb) truncated form of Rb PMID: 15735701 ERK1/2 mediates EGF-induced rapid Rb phosphorylation at Ser780 and Ser795 PMID: 16126730 deregulation of p16-cyclin D1/Cdk4-Rb pathway, but not oncogenic activation of ras, plays a crucial role in bladder tumorigenesis induced by bladder calculi PMID: 16896691 Results suggest that phosphorylation of the cell cycle regulator, Rb, contributes to death in oxygen-glucose deprivation in septal neurons but Cdk5 can have a protective role. PMID: 18351461 Results show that the Rb-E2F pathway functions as a bistable switch to convert graded serum inputs into all-or-none E2F responses. PMID: 18364697 Results suggest that proper CXCR4 stimulation by CXCL12 in the mature CNS can prevent impairment of the Rb-E2F pathway and support neuronal survival. PMID: 18583990 Ink4a/Cdk4/Rb1 pathway deregulation, more than Arf/Mdm2/Tp53 pathway, has a major role in the development of these tumors through p16(Ink4a) deregulation. PMID: 18656278 Cdk2 signaling pathways are critical regulators of cardiac I/R injury in vivo and support a cardioprotective role for Rb PMID: 18692063 These results indicate that cyclin D-cdk4/6-dependent phosphorylation of pRb and activation of E2F is necessary for hypertrophic growth in cardiomyocytes. PMID: 18700867

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.