Recombinant Human Squamous Cell Carcinoma Antigen Recognized By T-Cells 3 (SART3) Protein (His-SUMO)

Name: Recombinant Human Squamous Cell Carcinoma Antigen Recognized By T-Cells 3 (SART3) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10438P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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) SART3.

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Product Overview

Description	Recombinant Human Squamous Cell Carcinoma Antigen Recognized By T-Cells 3 (SART3) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q15020
Target Symbol	SART3
Synonyms	DSAP1; hSART 3; hSART-3; P100; P110; p110(nrb); RP11 13G14; SART 3; SART-3; SART3; SART3_HUMAN; Squamous cell carcinoma antigen recognized by T cells 3; Squamous cell carcinoma antigen recognized by T-cells 3; Tat interacting protein of 110 kDa; Tat-interacting protein of 110 kDa; Tip110
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QRKRARAEKKALKKKKKIRGPEKRGADEDDEKEWGDDEEEQPSKRRRVENSIPAAGETQNVEVAAGPAGKCAAVDVEPPSKQKEKAASLKRDMPKVLHDSSKDSITVFVSNLPYSMQEPDTKLRPLFEACGEVVQIRPIFSNRGDFRGYCYVEFKEEKSALQALEMDRKSVEGRPMFVSPCVDKSKNPDFKVFRYSTSLEKHKLFISGLPFSCTKEELEEICKAHGTVKDLRLVTNRAGKPKGLAYVEYENESQASQAVMKMDGMTIKENIIKVAISNPPQRKVPEKPETRKAPGGPMLLP
Expression Range	600-900aa
Protein Length	Partial
Mol. Weight	49.8kDa
Research Area	Cancer
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	U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation. Also binds U6atac snRNPs and may function as a recycling factor for U4atac/U6atac spliceosomal snRNP, an initial step in the assembly of U12-type spliceosomal complex. The U12-type spliceosomal complex plays a role in the splicing of introns with non-canonical splice sites. May also function as a substrate-targeting factor for deubiquitinases like USP4 and USP15. Recruits USP4 to ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex, promoting PRPF3 deubiquitination and thereby regulating the spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly. May also recruit the deubiquitinase USP15 to histone H2B and mediate histone deubiquitination, thereby regulating gene expression and/or DNA repair. May play a role in hematopoiesis probably through transcription regulation of specific genes including MYC.; Regulates Tat transactivation activity through direct interaction. May be a cellular factor for HIV-1 gene expression and viral replication.
Subcellular Location	Nucleus, nucleoplasm. Nucleus, Cajal body. Nucleus speckle. Cytoplasm.
Database References	HGNC: 16860 OMIM: 611684 KEGG: hsa:9733 STRING: 9606.ENSP00000228284 UniGene: PMID: 28878014 We show that PRP31, a component of U4 snRNP, is modified with K63-linked ubiquitin chains by the PRP19 complex and deubiquitinated by USP15 and its substrate targeting factor SART3. USP15SART3 makes a complex with USP4 and this ternary complex serves as a platform to deubiquitinate PRP31 and PRP3 PMID: 28088760 The complex structure of SART3 nuclear localization signal (NLS) and importin-alpha reveals bipartite binding, and removal of SART3 NLS prevents the entry of USP4 (and USP15) into the nucleus and abrogates the subsequent deubiquitinase activity of USP4. PMID: 27060135 crystal structures of SART3 in the apo-form and in complex with the DUSP-UBL domain of USP15 at 2.0 and 3.0 A, respectively. Structural analysis reveals SART3 contains 12 half-a-tetratricopeptide (HAT) repeats, organized into two subdomains, HAT-N and HAT-C. SART3 dimerizes through the concave surface of HAT-C, whereas the HAT-C convex surface binds USP15 in a novel bipartite mode. PMID: 27255711 miR-124 regulates Tip110 expression and differentiation of human cord blood CD34(+) cells PMID: 25928721 Hypoxia led to Tip110 protein degradation through the ubiquitin-proteasome system. Under hypoxia, Tip110 stabilized p53, which in return destabilized Tip110. PMID: 25939381 SART3 recruits ubH2B, which may be evicted from DNA during transcription, for deubiquitination by Usp15 PMID: 24526689 these findings have provided additional and mechanistic evidence to support Tip110 function in HIV-1 transcription. PMID: 24217245 Results identify a novel frameshift mutation in this gene implicated in disseminated superficial actinic porokeratosis in 4 Chinese families PMID: 23834120 YB-1 potentiates the Tip110/Tat-mediated transactivation of the HIV-1 LTR promoter. PMID: 23822148 findings show C-MYC upregulates transcription of TIP110 through interaction with the TIP110 E-box in the TIP110 promoter, ensuring high-level Tip110 expression in proliferating embryonic stem cells (hESCs); further show TIP110 regulates OCT4 alternative splicing in hESCs PMID: 23088399 TIP110 is also expressed in human embryonic stem cells (hESCs) and expression was decreased with differentiation of these ESCs. PMID: 22132941 detectable in majority of colorectal carcinoma tissues studied; could be an appropriate molecule for use in specific immunotherapy for colorectal carcinoma PMID: 11920522 Results suggest that U4 and U6 small nuclear ribonucleoproteins (snRNPs) accumulate in Cajal bodies for the purpose of assembly into U4/U6 snRNPs by SART3/p110. PMID: 12578909 involvement of U6-p110 (SART3) in recycling of the U4atac/U6atac snRNP PMID: 14749385 Tip110 is a negative regulator of AR transcriptional activation, and may be directly involved in AR-related developmental, physiological, and pathological processes PMID: 15031286 Data suggest a model whereby p110 (SART3) brings together U4 and U6 snRNAs through both RNA-protein and protein-protein interactions. PMID: 15314151 Both purified and recombinant LSm2-8 proteins are able to recruit p110 protein to U6 snRNA via interaction with the highly conserved C-terminal region of p110. PMID: 18567812 Levels of anti-SART3 peptide antibody in prostate cancer patients are significantly higher than those of non-cancer subjects. PMID: 19148489

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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.