Recombinant Human Anamorsin (CIAPIN1) Protein (His-SUMO)

Name: Recombinant Human Anamorsin (CIAPIN1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04278P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Anamorsin (CIAPIN1) 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	Q6FI81
Target Symbol	CIAPIN1
Synonyms	2810413N20Rik; Anamorsin; CIAPIN 1; CIAPIN1; CPIN1_HUMAN; Cytokine induced apoptosis inhibitor 1; Cytokine-induced apoptosis inhibitor 1; DRE2; Fe-S cluster assembly protein DRE2 homolog; Predicted protein of HQ0915; PRO0915
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKELQREPLTPEEVQSVREHLGHESDNLLFVQITGKKPNFEVGSSRQLKLSITKKSSPSVKPAVDPAAAKLWTLSANDMEDDSMDLIDSDELLDPEDLKKPDPASLRAASCGEGKKRKACKNCTCGLAEELEKEKSREQMSSQPKSACGNCYLGDAFRCASCPYLGMPAFKPGEKVLLSDSNLHDA
Expression Range	1-312aa
Protein Length	Full Length
Mol. Weight	49.6kDa
Research Area	Apoptosis
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	Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells.
Subcellular Location	Cytoplasm. Nucleus. Mitochondrion intermembrane space.
Protein Families	Anamorsin family
Database References	HGNC: 28050 OMIM: 608943 KEGG: hsa:57019 STRING: 9606.ENSP00000377914 UniGene: Hs.4900
Tissue Specificity	Ubiquitously expressed. Highly expressed in heart, liver and pancreas.

Gene Functions References

the effects of CIAPIN-1 in chondrocytes, focusing on extracellular signal-regulated kinase (ERK)-1/2 and p38 kinase signaling PMID: 27644154
results of the present study suggest that downregulation of the CIAPIN1 gene in multiple myeloma cells may be associated with the development of this disease. PMID: 25901506
CIAPIN1 and ABCA13 may be novel markers of poor outcome in pre-chemotherapy serous carcinoma effusions. PMID: 25889687
CIAPIN1 over-expression decreases NHE1 expression and ERK1/2 phosphorylation. PMID: 25724898
lentivirus-vector-mediated RNAi targeting of CIAPIN1 is a potential approach to reverse MDR of breast cancer and CIAPIN1 may participate in MDR of breast cancer by regulating P-glycoprotein and P53 expression. PMID: 24676475
the 25-kDa cleaved fragment of anamorsin was detected in post-mortem brains of Alzheimer and Parkinson disease patients PMID: 24973211
The N-terminal methyltransferase-like domain of anamorsin probably functions as a structural scaffold to inhibit methyl transfers. PMID: 24123282
CIAPIN1 targeted NHE1 to mediate differentiation of K562 cells via ERK1/2 pathway. PMID: 25043809
Mossbauer and EPR spectra of human anamorsin show that both the M1 motif and the M2 motif bind independently a [2Fe-2S] cluster through the four cysteines of each motif. PMID: 23989406
CIAPIN1 siRNA inhibited proliferation, migration and promotes apoptosis of vascular smooth muscle cells by regulating Bcl-2 and Bax. PMID: 23151078
the molecular basis of recognition between Ndor1 and anamorsin and of the electron transfer process, was investigated. PMID: 23596212
Elevated expression of nuclear CIAPIN1 negatively correlated with the survival of epithelial ovarian cancer patients PMID: 22713669
In summary, our work revealed a novel function of CIAPIN1, which might possibly be used as an independent prognostic factor and a potential therapeutic target for pancreatic cancer PMID: 22677939
Up-regulation of CIAPIN1 expression may play an important role in pathogenesis of leukemia. PMID: 21729524
Anamorsin is a Mia40-dependent but ALR-independent IMS-protein and binds a [2Fe-2S] cluster before and after specific Mia40-driven Cys-oxidation. PMID: 21700214
Results of immunohistochemical study showed that CIAPIN1 might play an important role in esophageal carcinogenesis, and it could be considered as a prognostic indicator in esophageal squamous cell carcinoma. PMID: 20411424
Low expression of CIAPIN1 is associated with colorectal cancer. PMID: 20815902
it is concluded that CIAPIN1 confers multidrug resistance in gastric cancer cells, likely by upregulating MDR-1 and MRP-1 PMID: 16410721
CIAPIN1 was localized in both the cytoplasm and the nucleus and was accumulated in the nucleolus. Bioinformatic prediction disclosed a putative nuclear localization signal and a putative nuclear export signal within human CIAPIN1. PMID: 16957168
CIAPIN1 might be a DNA or RNA methyltransferase. PMID: 17935775
These findings suggest that downregulating CIAPIN1 could sensitize leukemia cells to chemotherapeutic drugs by downregulating MDR-1 and Bcl-2 and by upregulating Bax. PMID: 18059532
anamorsin expression in DLBCL patients with a low IPI was shown to be an unfavorable biomarker; anamorsin might play some roles in the abnormal growth of DLBCL. PMID: 18203020
CIAPIN1 is a suppressor of gastric cancer cell proliferation; CIAPIN1 might play an important role in the development of human gastric cancer. PMID: 18293492
Knock down of CIAPIN1 by adenovirus-delivered siRNA may be a potential therapeutic strategy for treatment of hepatocellular carcinoma in which CIAPIN1 is overexpressed. PMID: 18299278
correlation between CIAPIN1 down regulation and decreased MDR1 transcriptional activity were observed. PMID: 18389626
the CIAPIN1 genet could be used as a clinical marker to identify patients with CCRCC. PMID: 19081179

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.