Recombinant Rat Suppressor Of Cytokine Signaling 3 (SOCS3) Protein (His)

Name: Recombinant Rat Suppressor Of Cytokine Signaling 3 (SOCS3) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10706P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Rat Suppressor Of Cytokine Signaling 3 (SOCS3) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O88583
Target Symbol	SOCS3
Synonyms	Socs3; Cish3Suppressor of cytokine signaling 3; SOCS-3; Cytokine-inducible SH2 protein 3
Species	Rattus norvegicus (Rat)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVETQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFSLPPTEPSFEVQEQPPAQALPGGTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
Expression Range	1-225aa
Protein Length	Full Length
Mol. Weight	26.8kDa
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

SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.

Database References

KEGG: rno:89829

STRING: 10116.ENSRNOP00000003940

UniGene: Rn.127801

Gene Functions References

These results suggest that SOCS3 might be a key molecular involved in the development of complicated cancer pain and that overexpression of SOCS3 might be an important strategy for treatment for mechanical allodynia associated with bone cancer. PMID: 28326931
SOCS3 induces neurite differentiation and promotes neuronal cell survival.SOCS3-induced neurite differentiation was mediated via the PI3 kinase pathway. PMID: 27118613
Using cultured primary neurons, JEV efficiently replicated in embryonic neurons rather than adult neurons, and the preference was accompanied by higher SOCS3 expression and protein tyrosine phosphatase activity. PMID: 28111888
results suggest that knocking down of SOCS3 enhances dendritic regeneration and prevents demyelination after SCI PMID: 26384335
alveolar macrophages can secrete SOCS1 and -3 in exosomes and microparticles, respectively, for uptake by alveolar epithelial cells and subsequent inhibition of STAT activation. PMID: 25847945
SOCS-3 expression levels increased rapidly within 12 h after SAH, more slowly after 12 h, and did not reach a peak within 48 h. SOCS-3 was involved in cerebral vasospasm after subarachnoid hemorrhage via an IL-6- and IL-10-related mechanism. PMID: 24463741
The TNF/SOCS3 pathways work through insulin receptor resistance to trigger apoptosis. PMID: 25086044
The results of study suggest that the STAT3/SOCS3 signaling pathway plays an important role in regulating neuronal death after spinal cord injury. PMID: 24959867
Data in vitro indicate that suppressor of cytokine signaling 3 (SOCS3) may play a negatively regulatory role in development and progression of vein graft failure. PMID: 24142708
SOCS3 is a crucial physiological negative regulator for vein graft failure. PMID: 24685947
SOCS3 expression accompanied the severity of inflammation and the expression of proinflammatory cytokines, as well as the activation status of STAT3 and p38 MAPK PMID: 24078776
SOCS3-induced pro-inflammatory effects were due, at least in part, to its role in controlling activation and nuclear accumulation of nuclear factor-kappaB and activity of phosphatidylinositol 3-kinase. PMID: 24088176
Prolactin stimulates normal liver growth, promotes survival, and regulates liver regeneration by mechanisms that may include hepatic downregulation of IL-6 and upregulation of SOCS-3, increased hepatocyte proliferation, and angiogenesis. PMID: 23948778
IL-1b alone did not significantly increase SOCS-3 levels but when coincubated with insulin, prevented the downregulation of SOCS-3 expression. XOMA 052 neutralized the antagonistic effect of IL-1b on insulin-induced downregulation of SOCS-3. PMID: 23401297
The expressions of C/EBPalpha and PPARgamma were significantly reduced after gene silencing of SOCS-1 or SOCS-3 in adipocytes. PMID: 23222907
Vagal afferent neurons of diet-induced obese rats become leptin resistant; LPS and SOCS-3 may play a role in the development of leptin resistance. PMID: 21521717
Data suggest that down-regulation of SOCS-1 and SOCS-3 ameliorates the capacity of glucose transport and provides a potential gene therapy approach to managing metabolic syndrome. PMID: 21364493
With respect to neurite outgrowth SOCS3 alone is (as expected) strongly inhibitory, but it can also enhance the growth-promoting activity of mitogen-activated protein kinase 8 interacting protein 1 (JIP1). PMID: 20816823
Chronic central leptin infusion increases the association of insulin receptor with SOCS3. PMID: 21255014
Our data demonstrate the negative impact of enhanced SOCS3 expression on the regenerative potential of mature central nervous system neurons. PMID: 21145973
postnatal overnutrition induced higher SOCS3 expression in adult animals,indicating central leptin resistance in adulthood. PMID: 20303731
SOCS-3 knockdown may have increased the leptin-mediated in situ fatty acid oxidation in the DIO adipocytes, and therefore, SOCS-3 might be an excellent target for therapeutic intervention for obesity. PMID: 19862646
AngII response in spontaneouly hypertensive rats associated with increased hypothalamic JAK-2/SOCS-3 expression may suggest that abnormal regulation of the central angiotensin pathways may contribute to dysfunction of water-electrolyte homeostasis. PMID: 20848345
role of SOCS3 expressed in the mediobasal hypothalamus (MBH) in development of diet-induced obesity; data suggest knockdown of Socs3 mRNA limited to the MBH increases Npy mRNA levels, which decreases locomotor activity and alters feeding patterns PMID: 20819948
SOCS3 of retina may play an important role in mitigating pathogenic effects of proinflammatory cytokines during different stages of experimental autoimmune uveoretinitis. PMID: 19176113
High leptin concentration could induce the expressions of SOCS-3 mRNA and protein in mature adipocytes. PMID: 19408656
SOCS3 knock-down does not influence the growth and adipogenic differentiation feature of adipose-derived stromal cells. PMID: 19693688
Noradrenaline acting at central beta-adrenoceptors induces Socs3 expression in rat brain. PMID: 20193756
increased expression in diabetes PMID: 20185635
Results suggest that SOCS-3 may be a mediator of hypothalamic leptin resistance in aged rats, and that increased SOCS-3 expression may be due to age-related hyperleptinemia. PMID: 12163036
Antisense knockdown of ischemia-induced SOCS-3 protein expression exacerbated transient MCAO-induced infarct volume, assigning a neuroprotective role to SOCS-3 PMID: 12437578
induced by Ang II in rat heart and neonatal rat ventricular myocytes and participates in the modulation of the signal generated by this hormone PMID: 12960061
SOCS-3 exhibits a rapid, robust, and transient induction in hippocampus after seizure, first in glia, followed by a robust induction in pyramidal and granule neurons, peaking at approximately 24 hr. PMID: 14614901
SOCS-3 participates, as a late event, in the negative cross-talk between angiotensin II and insulin, producing an inhibitory effect on insulin-induced glucose transporter-4 translocation. PMID: 15514089
Cross-talk between the SOCS/interferon and the IL-1beta pathways of signalling in pancreatic beta cells. PMID: 15578154
Socs3 overexpression leads to neuroblastoma cell death and, on the other hand, leads to primary cell differentiation, indicating the involvement of SOCS-3 in neuronal cell survival and differentiation. PMID: 15998644
Promoter deletion analysis revealed that the STAT response element (SRE) in the SOCS3 promoter is necessary for the promoter activity. PMID: 16300827
involvement of SOCS3 in a direct gene regulatory pathway downstream of leptin-activated JAK-STAT signaling in pancreatic beta-cells PMID: 16306356
These data suggest that training-induced elevations in SOCS-3 expression in skeletal muscle may contribute to the exercise-induced increase in IL-6 expression. PMID: 16484300
Leptin induced SOCS-3 expression and its association with the insulin receptor in rat skeletal muscle cells but functional significance of this increase was not apparent upon measuring glucose uptake. PMID: 17223256
SOCS-3 might have a defensive role in H. pylori-infected gastric mucosal cells PMID: 17405912
increased glomerular IL-4 in nephrotoxic nephritis inhibits infiltrating macrophages from expressing SOCS3 and was associated with attenuated glomerular injury PMID: 18424750
These results demonstrate SOCS-3 induction occurs in reactive astrocytes of the post-ischemic hippocampus, suggesting that SOCS-3 is involved in regulating the astroglial reaction to an ischemic insult. PMID: 18586073
The up-regulation of SOCS1 and SOCS3 gene expression may be one of the possible mechanisms responsible for endotoxin tolerance. PMID: 19080716
The objective of this study was to investigate the effect of SOCS-3 on TNFalpha-induced signalling in beta cells. PMID: 19643162

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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.

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