Recombinant Human Baculoviral Iap Repeat-Containing Protein 1 (NAIP) Protein (His-SUMO)

Name: Recombinant Human Baculoviral Iap Repeat-Containing Protein 1 (NAIP) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-04059P
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 Baculoviral Iap Repeat-Containing Protein 1 (NAIP) 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	Q13075
Target Symbol	NAIP
Synonyms	Baculoviral IAP repeat containing 1; Baculoviral IAP repeat-containing protein 1; BIRC 1; BIRC1; BIRC1_HUMAN; Birc1a; FLJ42520; NAIP; Naip1; Neuronal apoptosis inhibitory protein; NLR family apoptosis inhibitory protein; NLR family BIR domain containing 1; NLRB 1; NLRB1; Nucleotide binding oligomerization domain leucine rich repeat and BIR domain containing 1; Psi neuronal apoptosis inhibitory protein; psiNAIP; Similar to occludin
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	EAKRLKTFVTYEPYSSWIPQEMAAAGFYFTGVKSGIQCFCCSLILFGAGLTRLPIEDHKRFHPDCGFLLNKDVGNIAKYDIRVKNLKSRLRGGKMRYQEEEARLASFRNWPFYVQGISPCVLSEAGFVFTGKQDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLRSKKSSEEITQYIQSYKGFVDITGEHFVNSWVQRELPMASAYCNDSIFAYEELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFL
Expression Range	60-345aa
Protein Length	Partial
Mol. Weight	48.6kDa
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

Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.; Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila.

Database References

HGNC: 7634

OMIM: 600355

KEGG: hsa:4671

STRING: 9606.ENSP00000428657

UniGene: PMID: 29311650

Data document a previously unknown localization of NAIP along the entire cytokinetic process whose dynamics exhibits a distinct behavior. PMID: 28059125

NAIP expression is most abundant in M2 macrophages, while cIAP1 and cIAP2 show an inverse pattern of expression in polarized cells, cIAP2 is preferentially expressed in M1-macrophages and cIAP1 in M2-macrophages. IAP antagonist treatment of resting M0 macrophages preceding polarization stimulation, induced upregulation of NAIP in M2 and downregulation of cIAP1 in M1 and M2 but an induction of cIAP2 in M1 macrophages. PMID: 29518103

Deletion in NAIP gene is associated with spinal muscular atrophy. PMID: 27754957

NAIP and survivin expressions were significantly reduced following varicocele induction when compared to sham animals whereas PDRN-treated rats showed an increase in NAIP and survivin levels. PMID: 26347229

The copy numbers and gene structures of NAIP genes were different in Chinese spinal muscular atrophy patients and healthy controls PMID: 25888055

results revealed that SMN2 and NAIP copy numbers significantly influenced the age at onset, risk of death, and life expectancy in the spinal muscular atrophy patients and that the effect of SMN2 was more significant PMID: 25330799

human Naip functions to activate the inflammasome in response to flagellin, similar to murine Naip5/6. PMID: 26109648

Modulation of chemotherapeutic drug resistance in neuroblastoma SK-N-AS cells by the neural apoptosis inhibitory protein and miR-520f. PMID: 25137037

Copy number variations of SMN2 and NAIP genes in patients are related to spinal muscular atrophy clinical types (P < 0.05). PMID: 24711022

/NAIP1 and NAIP2/5 formed a large oligomeric complex with NLRC4 in the presence of corresponding bacterial ligands, and could support reconstitution of the NLRC4 inflammasome in a ligand-specific manner. PMID: 23940371

identified an intronic region of the NAIP gene responding to TEAD1/YAP activity, suggesting that regulation of NAIP by TEAD1/YAP is at the transcriptional level PMID: 23994529

the NAIP5-NLRC4 inflammasome is induced by direct interactions with conserved N- and C-terminal regions of flagellin PMID: 23012363

NAIPFull gene duplication might have been evolutionary maintained, or even selected for, because it may confer an advantage to the host against flagellated bacteria PMID: 22067212

There is a close relationship between SMN2, NAIP and H4F5 gene copy number and spinal muscular atrophy disease severity PMID: 21821450

NOD domain is essential for effective inhibition of procaspase-9 and procaspase-3 cleavage by the NAIP protein in apoptosis. PMID: 21371431

an inhibitor of procaspase-9 preventing apoptosis at the initiation stage PMID: 20171302

Expression of NAIP may be associated with enhanced survival of prostate cancer in response to castration PMID: 20044205

Results provide the first structures of BIR domains from human NAIP and cIAP2. PMID: 19923725

NAIP gene deletion was higher in type I spinal muscular atrophy than in type U or V. In type I patients lacking the NAIP gene, deterioration in their respiratory function is more rapid than in those type I patients retaining the NAIP gene. PMID: 11912351

NAIP-deltaEx10-11: a novel splice variant of the apoptosis inhibitor NAIP is differently expressed in drug-sensitive and multidrug-resistant HL60 leukemia cells. NAIP transcripts might be involved in tumor resistance to chemotherapeutic agents. PMID: 12127562

NAIP:Structural requirements for binding hippocalcin and effects on survival of sympathetic neurons. PMID: 12445469

NAIP does not interact with Smac and requires ATP to bind caspase-9 PMID: 15280366

Alterations in C/CAAT enhancer binding protein alpha and neuronal apoptosis inhibitory protein expression occurred in human adipose stromal-vascular cells after weight loss PMID: 15340105

Multiple, domesticated long terminal repeats (LTRs) of endogenous retroviral elements provide NAIP promoter function in human, mouse, and rat. PMID: 17222062

a role for NAIP in increasing the survival of cells undergoing terminal differentiation as well as the possibility that the protein serves as an intestinal pathogen recognition protein was suggested PMID: 17510375

80% neuronal apoptosis inhibitory protein gene deletion in 5q-spinal muscular atrophy patients (91% spinal muscular atrophy-I, 50% spinal muscular atrophy-II and -III), and in 5% (two of forty) of spinal muscular atrophy parents, was found. PMID: 17903057

While there was no evidence of NAIP expression in the normal breast tissue, NAIP was expressed in all breast cancer samples. PMID: 17923748

May be a modifying factor for disease severity of spinal muscular atrophy. PMID: 17932457

The present study is the first one giving detailed information on SMN and NAIP deletion rates in Iranian SMA patients. PMID: 18071605

Data show elevated expression of NAIP in peripheral mononuclear cells from children with Fabry disease. PMID: 18339188

hNAIP and hIpaf mediate innate intracellular defense against flagellated Legionella in human cells. PMID: 18453601

The presence of one NAIP copy, that is, heterozygous NAIP deletion, was common in Vietnamese SMA, regardless of clinical phenotype. PMID: 18533950

HIAP-1 and HIAP-2 mRNA levels were elevated in resting T cells while NAIP mRNA was increased in whole blood in multiple sclerosis PMID: 18566024

in glioma & glioblastoma multiforme, selective upregulation of miRNA-221 & down-regulation of a miRNA-221 mRNA target encoding BIRC1 were observed; expression of BIRC5 & caspase-3 were found to be significantly up-regulated, particularly in stage IV GBM PMID: 18759060

Data show that NAIP deletion predicts disease severity in spinal muscular atrophy. PMID: 18842367

Among the SMA Type I patients, 43% showed deletions of SMN1 and NAIP. PMID: 18974562

findings of homozygous deletions of exon 7 and/or exon 8 of SMN1 gene confirmed the diagnosis of SMA, and suggested that the deletion of SMN1 exon 7 is a major cause of SMA in southern Chinese children. PMID: 19198020

higher number of SMN2 copies makes the clinical symptoms more benign, and the NAIP gene deletion is associated with a more severe phenotype PMID: 19287802

a novel NAIP isoform derives from intragenic Alu SINE promoters PMID: 19488400

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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.

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