Recombinant Human Apoptosis Regulatory Protein Siva (SIVA1) Protein (His-SUMO)

Name: Recombinant Human Apoptosis Regulatory Protein Siva (SIVA1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10718P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Apoptosis Regulatory Protein Siva (SIVA1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O15304
Target Symbol	SIVA1
Synonyms	Apoptosis regulatory protein Siva; CD27 binding (Siva) protein; CD27-binding protein; CD27BP; Siva 1 ; Siva 2; SIVA_HUMAN; Siva1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MPKRSCPFADVAPLQLKVRVSQRELSRGVCAERYSQEVFDPSGVASIACSSCVRAVDGKAVCGQCERALCGQCVRTCWGCGSVACTLCGLVDCSDMYEKVLCTSCAMFET
Expression Range	1-110aa
Protein Length	Full Length of Isoform 2
Mol. Weight	27.8kDa
Research Area	Cell Biology
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	Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis.
Subcellular Location	Cytoplasm. Nucleus. Note=In the nucleus, accumulates in dot-like structures.
Database References	HGNC: 17712 OMIM: 605567 KEGG: hsa:10572 STRING: 9606.ENSP00000329213 UniGene: Hs.112058
Tissue Specificity	Ubiquitous. Mostly expressed in thymus, testis, ovary, prostate, small intestine and spleen and less in colon.

Gene Functions References

Loss of SIVA1 expression is associated with nasopharyngeal carcinoma. PMID: 26406409
These findings collectively reveal a novel role for the p53 target gene SIVA both in regulating metabolism and in enabling tumorigenesis, independently of p53. PMID: 25813352
Functional test demonstrated that Siva1 significantly inhibited the invasion and migration of HCT116 cells. PMID: 25374190
electrical stimulation -inducible SIVA1 modulates p53 activities in proliferating keratinocytes, and exogenous electrical stimulation affects p53/HDM2/SIVA1 axis leading to increased proliferation during re-epithelialization PMID: 25431847
SIVA1 interacts with RAD18 and serves as a molecular bridge between RAD18 and PCNA, thus targeting the E3 ligase activity of RAD18 onto PCNA. PMID: 24958773
Siva1 promotes the ubiquitination and degradation of ARF, which in turn affects the stability of p53. PMID: 23462994
Upon stimulation of thromboxane A2, degradation of Siva1 is impeded, resulting in an accumulation of the protein, which translocates from the nucleus to the cytosol. PMID: 22343716
negative regulator of IL-2 gene expression in Treg cells PMID: 21955384
Data show that low levels of Siva1 and Ser16-phosphorylated stathmin correlate with high metastatic states of breast cancer cells. PMID: 21768358
These findings suggest that the caspase-dependent pathway for induction of apoptosis is involved in Siva-1-mediated influenza A virus replication. PMID: 21048035
These results suggest that Siva-mediated unprovoked apoptosis is not likely to be involved in the pathogenesis of Familial Mediterranean fever. PMID: 20934406
Siva-1 forms a functional complex with Tyk2 and participates in the transduction of signals that inhibit B lymphocyte growth. PMID: 20727854
Siva-1 putative amphipathic helical region (SAH) binds BCL-XL and sensitizes cells to UV radiation induced apoptosis PMID: 14739602
Overexpression of Siva-1 in T lymphocytes triggers the activation of a caspase-dependent death pathway including a pivotal mitochondrial step. Both N- and C-terminal domains of Siva proteins display the ability to induce a cell death process in T cells. PMID: 15034012
Siva-1 has a role, through its inhibitory effect on NF-kappaB activity, in TCR-mediated AICD with implications in peripheral tolerance, T-cell homeostasis and cancer PMID: 16491128
determined the N-terminal part of Siva as the binding region for CD27; the peroxisomal membrane protein PMP22 is a new interaction partner of Siva and may be involved in the host response against CVB3. PMID: 16683188
Confirming the anti-apoptotic role of HPV-16 E7 in the HaCaT cellular model, evaluated by nuclear morphology, it was also found that Siva-1 expression produced a significant increase of the apoptotic rate in UV radiation-exposed HaCaT cells. PMID: 17348035
Results suggest that Siva-1 might participate in the CD4-initiated signaling apoptotic pathway induced by the HIV-1 envelope in T-lymphoid cells. PMID: 17653867
lysophosphatidic acid 2 receptor mediates down-regulation of Siva-1 to promote cell survival PMID: 17965021
Data show that Siva and pyrin are co-expressed, and that pyrin modulates the apoptotic response to oxidative stress mediated by Siva. PMID: 18330885
Telethonin might be involved in CVB3-mediated cell damage and in the resulting cardiac dysfunction due to the interaction with Siva. PMID: 18849585
Siva-1 has a role in negatively regulating NF-kappaB activation by targeting TRAF2. PMID: 19392652
Siva1 is an important mediator for the Hdm2-p53 interaction and is an integral component of the negative feedback mechanism for p53 inhibition. PMID: 19590512

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.