Recombinant Human Sorcin (SRI) Protein (GST)

Name: Recombinant Human Sorcin (SRI) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09280P
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 Human Sorcin (SRI) 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	P30626
Target Symbol	SRI
Synonyms	22 kDa protein; Calcium binding protein amplified in mutlidrug resistant cells ; CP 22; CP-22; CP22; SCN; Sorcin (class 4 gene); Sorcin; SORCN_HUMAN; SRI; V19
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAYPGHPGAGGGYYPGGYGGAPGGPAFPGQTQDPLYGYFAAVAGQDGQIDADELQRCLTQSGIAGGYKPFNLETCRLMVSMLDRDMSGTMGFNEFKELWAVLNGWRQHFISFDTDRSGTVDPQELQKALTTMGFRLSPQAVNSIAKRYSTNGKITFDDYIACCVKLRALTDSFRRRDTAQQGVVNFPYDDFIQCVMSV
Expression Range	1-198aa
Protein Length	Full Length
Mol. Weight	48.7kDa
Research Area	Signal Transduction
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	Calcium-binding protein that modulates excitation-contraction coupling in the heart. Contributes to calcium homeostasis in the heart sarcoplasmic reticulum. Modulates the activity of RYR2 calcium channels.
Subcellular Location	Cytoplasm. Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Relocates to the sarcoplasmic reticulum membrane in response to elevated calcium levels.
Database References	HGNC: 11292 OMIM: 182520 KEGG: hsa:6717 STRING: 9606.ENSP00000265729 UniGene: PMID: 28726784 Sorcin overexpression in HCT116 cells resulted in a significant increase in cell migration and invasion. Sorcin stimulated epithelial-mesenchymal transition through activating PI3K/Akt signaling. PMID: 25567655 The authors verified that NS5A of hepatitis C virus interacted with sorcin through domain I of NS5A, and phosphorylation of the threonine residue 155 of sorcin played a crucial role in protein interaction. PMID: 26719254 Drug resistance can be effectively reversed in cisplatin-resistance and adriamycin-resistant myeloma cells through delivery of siRNAs targeting sorcin. PMID: 26045737 Sorcin is highly expressed in the heart and in the brain, and overexpressed in many cancer cells. [Review] PMID: 25197934 Sorcin antibody as a possible predictive factor in conversion from radiologically isolated syndrome to multiple sclerosis: a preliminary study PMID: 25001342 Sorcin links calcium signaling to vesicle trafficking, regulates Polo-like kinase 1 and is necessary for mitosis. PMID: 24427308 Key cellular signaling pathways were triggered by sorcin silencing in the drug resistance of human nasopharyngeal carcinoma. PMID: 24376145 sorcin regulates epithelial-mesenchymal transition and cancer stem cells partly through E-cadherin and vascular endothelial growth factor expression. PMID: 24337682 overexpression of sorcin increased the phosphorylation of CREB1 and the binding of CREB1 to the CRE sequence of mdr1/p-gp promoter, and induced the expression of MDR1/P-gp PMID: 24796664 down-regulation of sorcin did not alter expression or function of P-gp, but induced cell apoptosis and chemosensitivity in K562/ A02 and MCF-7/A02 PMID: 24013575 The role of sorcin in multidrug resistance in cancer. [Review] PMID: 22701893 sorcin retains ChREBP in the cytosol at low glucose concentrations and may act as a Ca(2+) sensor for glucose-induced nuclear translocation and the activation of ChREBP-dependent genes. PMID: 22338092 Data show that colorectal cancer cells overexpress sorcin as an adaptive mechanism to prevent endoplasmic reticulum stress and escape apoptosis triggered by chemotherapeutic agents. PMID: 22052463 Upregulation of sorcin is associated with gastric cancer. PMID: 19885748 Overexpression of sorcin by gene transfection was able to confer drug resistance in gastric cancer cells PMID: 21109982 Overexpression of sorcin was associated with gemcitabine resistance in non-small cell lung cancer. PMID: 20012234 The study indicates that stomatin, sorcin, and synexin are echinophilic membrane components that mainly locate outside GM1 rafts in the human erythrocyte membrane. PMID: 20858460 Depletion of TRAP1 by short hairpin RNA in colorectal carcinoma cells lowered Sorcin levels in mitochondria, whereas the depletion of Sorcin by small interfering RNA increased TRAP1 degradation. PMID: 20647321 Overexpression of sorcin could induce low level of multidrug resistant (MDR) in SGC7901 cells, indicating that sorcin is associated with MDR of SGC7901 cells. PMID: 18423116 Tetrandrine reverses multidrug-resistance of K562/A02 cells through regulation of expression of SORCIN. PMID: 18315902 relationship between soluble resistance-related calcium-binding protein (sorcin) gene and multidrug resistance gene (mdr1), and their significance in clinical drug resistance and prognosis of acute myeloid leukemia (AML) PMID: 12408767 Sorcin gene overexpression is significantly associated with clinical multidrug resistance and prognosis, it is one of the indicators for predicting prognosis of acute myeloid leukemia patients PMID: 12411058 data indicate that sorcin modulates intracellular calcium cycling and calcium influx pathways in the heart PMID: 12754254 SRI interacts with GCA in vivo and in vitro. PMID: 12804766 Overexpression of SOR improves cardiac contractility independent of beta-adrenergic stimulation. PMID: 15808837 Semi-quantitative RT-PCR experiments with 6 of those genes confirmed higher expression of DNCH2, ARHGEF6, NPM1 and SRI and lower expression of NRGN and TM4SF2 in GBM tumors. PMID: 16320026 sorcin plays an important role in the emergence of MDR in leukemia cells via regulating cell apoptosis pathways PMID: 16934756 Knock-down of SRI induces up-regulation of MDR1 in HeLa cells. PMID: 17541155 provide a plausible structural and functional framework that helps elucidate the phenotypic alterations of mice overexpressing F112L-sorcin PMID: 17699613 Sorcin interacts with and modulates ryanodine receptor activity in rat vascular smooth muscle cells. PMID: 16931553

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.