Recombinant Human Replication Factor C Subunit 1 (RFC1) Protein (His&Myc)

Name: Recombinant Human Replication Factor C Subunit 1 (RFC1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-09255P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Human Replication Factor C Subunit 1 (RFC1) 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	P35251
Target Symbol	RFC1
Synonyms	A1 140 kDa subunit; A1; A1 P145 Activator 1 large subunit; Activator 1 140 kDa subunit; Activator 1 large subunit; Activator 1 subunit 1; DNA binding Protein PO GA; DNA-binding protein PO-GA; MHC binding factor beta; MHCBFB; PO GA; RECC1; Replication factor C (activator 1) 1, 145kDa; Replication factor C 140 kDa subunit; Replication factor C; Replication factor C large subunit; Replication factor C subunit 1; Replication factor C1; RF-C 140 kDa subunit; RFC; RFC1; RFC1_HUMAN; RFC140; RFC140 Replication Factor C 140 kDa subunit
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIRTMPGKKSKYEIA
Expression Range	402-492aa
Protein Length	Partial
Mol. Weight	14.8 kDa
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	The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Could play a role in DNA transcription regulation as well as DNA replication and/or repair. Can bind single- or double-stranded DNA.; Interacts with C-terminus of PCNA. 5' phosphate residue is required for binding of the N-terminal DNA-binding domain to duplex DNA, suggesting a role in recognition of non-primer template DNA structures during replication and/or repair.
Subcellular Location	Nucleus.
Protein Families	Activator 1 large subunit family
Database References	HGNC: 9969 OMIM: 102579 KEGG: hsa:5981 STRING: 9606.ENSP00000371321 UniGene: Hs.507475
Tissue Specificity	Wide tissue distribution. Undetectable in placental tissue.

Gene Functions References

Human CTF18-RFC clamp-loader complexed with non-synthesising POLE efficiently loads the PCNA sliding clamp. PMID: 28199690
RFC depletion had a negative impact on LANA's ability to replicate and maintain viral DNA in cells containing artificial KSHV episomes or in infected cells, leading to loss of virus. PMID: 25071216
phosphorylation of serine 51 on hLigI plays a critical role in regulating the interaction between hLigI and RFC, which is required for efficient DNA replication and repair. PMID: 22952233
report that the large subunit (RFC1) of replication factor C is cleaved in Hutchinson-Gilford progeria syndrome cells, leading to the production of a truncated RFC1 of ~ 75 kDa PMID: 22168243
We identified a variant in each of 3 genes (RFC1, SCN1A, ANPEP) potentially implicated in susceptibility to severe neurological complications in West Nile Virus disease. PMID: 21881118
Small interfering RNA-mediated knockdown of RFC1 impairs upstream removal of UV lesions and abrogates the downstream recruitment of DNA polymerase delta. PMID: 20713449
analysis of the DNA-bound BRCA1 C-terminal region structure from human replication factor C p140 and model of the protein-DNA complex PMID: 20081198
interaction with histone deacetylase HDAC1 PMID: 12045192
RFC (p140) has an important role as a regulator of transcription and NF-kappaB activity PMID: 12509469
destabilization of the RF-C complex by CDKs may inactivate the RF-C complex at the end of S phase PMID: 12947101
NMR resonance assignments of the BRCT region of the large subunit PMID: 15772763
Ctf18-RFC interacts physically with pol eta, which allows DNA replication forks to overcome interference by various template structures, including damaged DNA and DNA-protein complexes that maintain chromosome cohesion PMID: 17545166
Data show that replication factor C (RFC), via several stimulatory motifs per molecule, potently activates flap endonuclease 1 (FEN1), making RFC a critical partner with FEN1 for the processing of eukaryotic Okazaki fragments. PMID: 19208620
a mutant version of hLigI, which mimics the hyperphosphorylated M-phase form of hLigI, does not interact with and is not inhibited by RFC, demonstrating that inhibition of ligation is dependent upon the interaction between hLigI and RFC PMID: 19223468

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.