Recombinant Human Interleukin-32 (IL32) Protein (His-sumostar)

Name: Recombinant Human Interleukin-32 (IL32) Protein (His-sumostar)
Brand: Beta LifeScience
SKU: BLC-06088P
Price: 460.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Interleukins and receptors, Recombinant proteins

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Product Overview

Description	Recombinant Human Interleukin-32 (IL32) Protein (His-sumostar) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P24001
Target Symbol	IL32
Synonyms	Natural killer cells protein 4Tumor necrosis factor alpha-inducing factor
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His-sumostar
Target Protein Sequence	AWVSACDTEDTVGHLGPWRDKDPALWCQLCLSSQHQAIERFYDKMQNAESGRGQVMSSLAELEDDFKEGYLETVAAYYEEQHPELTPLLEKERDGLRCRGNRSPVPDVEDPATEEPGESFCDKVMRWFQAMLQRLQTWWHGVLAWVKEKVVALVHAVQALWKQFQSFCCSLSELFMSSFQSYGAPRGDKEELTPQKCSEPQSSK
Expression Range	31-234aa
Protein Length	Full Length of Mature Protein
Mol. Weight	36.5 kDa
Research Area	Cytokine
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	Cytokine that may play a role in innate and adaptive immune responses. It induces various cytokines such as TNFA/TNF-alpha and IL8. It activates typical cytokine signal pathways of NF-kappa-B and p38 MAPK.
Subcellular Location	Secreted.
Database References	HGNC: 16830 OMIM: 606001 KEGG: hsa:9235 UniGene: Hs.943
Tissue Specificity	Selectively expressed in lymphocytes. Expression is more prominent in immune cells than in non-immune cells.

Gene Functions References

IL-32gamma functions as intracellular effector in hepatocytes for suppressing hepatitis b virus replication. PMID: 30115930
Results indicate that interleukin-32 gamma (IL-32gamma) plays a protective role for bone loss, providing clinical evidence of a negative correlation between IL-32gamma and DKK1 (Dickkopf-1) as bone metabolic markers. PMID: 28079119
Our study shows a functional effect of a promoter single-nucleotide polymorphism (SNP) in IL32 on lipid profiles in RA patients and individuals, suggesting a possible protective role of this SNP against CVD. PMID: 28134327
IL-32 may be an important pro-inflammatory molecule involved in calcific aortic valve disease. PMID: 29748157
High IL32 expression is associated with hepatocellular carcinoma. PMID: 29286122
Strong expression of IL-32 was detected in cardiomyocytes from heart failure patients. PMID: 28747035
The increase in serum levels of IL-32 in accordance with additive effect of the presence of C allele in Multiple sclerosis patients might introduce IL-32 as a key player in MS pathogenesis or immunedysregulation PMID: 28716229
high expression of both IL17A and IL32 leads to enhancement of T cell responses in breast tumors PMID: 28470472
In transgenic mice, the presence of IL-32gamma contributes to the lesion healing caused by Leishmania braziliensis but not by Leishmania amazonensis. PMID: 28709468
High IL32 expression is associated with lung metastasis in melanoma. PMID: 27589563
In Kaposi sarcoma (KS) splicing ratio of the IL-32 isoforms showed IL-32gamma as the highest expressed isoform, followed by IL-32beta, in HIV-related KS cases compared with controls. Our data suggest a possible survival mechanism by the splicing of IL-32gamma to IL-32beta and also IL-6, IL-8, and CXCR1 signaling pathways to reverse the proapoptotic effect of the IL-32gamma isoform, leading to tumor cell survival and th... PMID: 29037857
Three single nucleotide polymorphisms (SNPs) (rs28372698, rs12934561, rs4786370) of the IL32 gene have been proposed as modifiers for different diseases. The present study found no significant differences in the genotypic frequencies between the patients and healthy controls and no relation to survival for any of the SNPs. PMID: 29277790
This study showed that the induction level of IL-32 was increased in chronic rhinosinusitis with nasal polyps compared to normal nasal mucosa and that LPS-induced IL-32 expression in nasal polyp-derived fibroblasts was regulated via the TLR4/JNK/AKT/CREB signaling pathway. PMID: 27173130
findings show that IL-32alpha acts on NK cells to inhibit IL-15-mediated STAT5 phosphorylation and to suppress their IL-15-induced effector molecule expression and cytolytic capacity. IL-32alpha also acted on DCs by downregulating IL-15-induced IL-18 production, an important cytokine in NK cell activity. PMID: 28701509
Thus, endogenous IL-32 is a crucial cytokine involved in the host defense against Leishmania parasites. PMID: 28241012
Study indicated the overexpression of IL-32 in induced sputum of smokers and chronic obstructive pulmonary disease (COPD) patients, which was correlated with smoking exposure index and the degree of airway obstruction. It demonstrated that IL-32 might play critical role in smokers with COPD. PMID: 24761997
this study shows that IL-32 might be involved in the pathogenesis of hepatic fibrosis by inducing TIMP-1 expression PMID: 27302771
serum levels of IL-32 and TNF-alpha may be diagnostic markers, and serum IL-29 levels may be associated with good prognosis in patients with gastric cancer PMID: 26219901
the importance of IL-32 polymorphism and mRNA expression in susceptibility and influence of survival status in lung cancer PMID: 27775437
Data identify interleukin-32 (IL-32) as a potential therapeutic target. PMID: 26978598
Low IL-32 expression is associated with colon cancer. PMID: 26824417
Results show low plasma IL-32 levels in patients with systemic lupus erythematosus (SLE) and the rs28372698 SNP was associated with the susceptibility to SLE suggesting a possible role as a candidate marker to monitor SLE disease stability and screening in future. PMID: 27069296
High IL32 expression is associated with acute myeloid leukemia. PMID: 26516703
highlight some of the potential mechanisms by which the immunomodulatory effect of IL-32 occurs against mycobacterial infections but also areas where mechanistic clarifications are needed PMID: 26144292
Additional IL-32gamma stimulation in precursor cells enhanced osteoblast differentiation potentially PMID: 26634249
This study demonstrates that IL-32gamma and IL-32beta can induce caspase-8-dependent cell death whereas this was not observed for IL-32alpha PMID: 26678222
High IL32 expression is associated with Sezary syndrome. PMID: 26551670
soluble IL-6R expression upregulated the levels of its own ligand, IL-6 and those of the pro-inflammatory cytokine IL-32. PMID: 25176527
Our results suggest that NKP30-B7-H6 interaction can aggravate hepatocyte damage, probably through up-regulation of IL-32 expression in hepatitis B virus-related acute-on-chronic liver failure PMID: 26241657
These results suggest that IL-32beta could activate NF-kappaB and STAT3, and thus affect neuroinflammation as well as amyloidogenesis, leading to worsening memory impairment. PMID: 25159479
IL-32 is involved in the pathogenesis of airway inflammation. PMID: 26151454
High IL-32 expression may stimulate the organic metastasis and the lymph node metastasis of colorectal cancer. PMID: 25889282
data further confirms that reduced IL32 methylation is associated with JIA, and that SNPs play an interactive role PMID: 26057774
IL-32alpha can prevent cerebral ischemia damage via STAT3 activation and inhibition of NF-kappaB activation. PMID: 24854197
In IL-32alpha-Tg mice, azoxymethane-induced colon cancer incidence was decreased, but expression of TNFR1 and TNFR1-mediated apoptosis was increased. IL-32alpha increased ROS production, prolonging JNK activation. In colon cancer patients, IL-32alpha was increased. PMID: 25909160
IL-32 stimulation promotes the invasion and motility of osteosarcoma cells, possibly via the activation of AKT and the upregulation of MMP-13 expression. PMID: 25846944
The anti-Mycobacterium tuberculosis effects of IL-32gamma are mediated through classical caspase-3-dependent apoptosis as well as caspase-3-independent apoptosis. PMID: 25887904
IL-32 gamma delays, in a dose-dependent manner, the spontaneous apoptosis of human blood neutrophils by activating mainly p38 MAPK through rapid p38 phosphorylation. PMID: 25275312
we demonstrate that the newly discovered isoform, IL-32theta;, suppresses monocyte differentiation by regulating the expression of the PU.1 transcription factor. PMID: 25726525
This study demonstrates that IL-32 gene polymorphisms are significantly associated with increased endometrial cancer susceptibility in Chinese Han women PMID: 25663496
These results suggest that IL-32gamma enhances an innate immune response against local infection but inhibits the spread of immune responses, leading to systemic immune disorder. PMID: 24743568
Transgenic mice that express human interleukin-32 are protected from high-fat diet-induced hepatic steatosis. PMID: 25645248
overexpression of IL-32gamma contributes to initial islet beta-cells injury and inflammation in pancreas and aggravates streptozotocin-induced type 1 diabetes. PMID: 25022955
IL32 may play a unique role in mycosis fungoides progression as an autocrine cytokine PMID: 24938282
Our results clearly suggest that IL-32 is an important mediator for gastric cancer metastasis and independent prognostic predictor of gastric cancer. PMID: 24602839
The Epstein-Barr virus LMP1-induced IL-32 traps protein kinase Cdelta in the cytoplasm and prevents it from binding to the Zta promoter, which is the key event for virus activation. PMID: 25810549
IL-32theta;, through its interaction with PKCdelta, downregulates CCL5 expression by mediating the phosphorylation of STAT3 on Ser727 to render it transcriptionally inactive. PMID: 25280942
IL-32gamma enhances host immunity to Mycobacterium tuberculosis. PMID: 25820174
IL-32alpha inhibits BCL6 SUMOylation by activating PKCepsilon, resulting in the modulation of BCL6 target genes and cellular functions of BCL6. PMID: 25245533
IL-32gamma prevents ethanol-induced hepatic injury via the inhibition of oxidative damage and inflammatory responses. PMID: 25583360

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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.