Intelectin-1a Antibodies

Intelectin-1a (Itln1)

Lectin that specifically recognizes microbial carbohydrate chains at a calcium-dependent way (PubMed:26148048). Binds to microbial glycans which contain a terminal acyclic 1,2-diol moiety, including beta-linked D- galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct- 2-ulosonic acid (KDO).

Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.

Gene Information

Mouse
Gene Name:	Itln1
Uniprot:	O88310
Entrez:	16429

Family

Belongs to:
No superfamily

Alternative Names

Endothelial lectin HL-1; FLJ20022; Galactofuranose-binding lectin; hIntL; HL-1; intelectin 1 (galactofuranose binding); Intelectin1; Intelectin-1; INTLHL1; ITLN1; Itlna; ITLNITLN-1; LFR; LFRIntestinal lactoferrin receptor; Omentin; Omentin-1

Molecular Weight

Mass (kDA):
34.953 kDA

Genomic Context

Mouse
Location:	1|1 H3
Sequence:	1;

Tissue Specificity

Expressed in small intestinal Paneth cells in uninfected mice. Expression also detected in various other tissues including stomach, kidney, ovary and brain.

Diseases

• Obesity
• Insulin Resistance
• Diabetes Mellitus
• Diabetes Mellitus, Non-insulin-dependent
• Cardiovascular Diseases
• Insulin Sensitivity
• Inflammation
• Neoplasms
• Polycystic Ovary Syndrome
• Metabolic Syndrome X
• Malignant Neoplasms
• Malignant Paraganglionic Neoplasm

• Hyperinsulinism
• Crohn Disease
• Coronary Artery Disease
• Pleural Neoplasms
• Pleural Mesothelioma
• Adenocarcinoma
• Dental Plaque

Pathways

• Immune Response
• Secretion
• Innate Immune Response
• Pathogenesis
• Cell Adhesion
• Vasodilation
• Localization
• Angiogenesis
• Osteoclast Differentiation
• Cell Proliferation
• Cell Migration
• Osteoblast Differentiation
• Aging

• Tube Formation
• Glomerular Filtration
• Platelet Aggregation
• Response To Ischemia
• Endothelial Cell Migration
• Menstruation
• Reverse Transcription

PTMs

• Phosphorylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/Itln1

Boster Bio - Best Uses Of The ITLN1 Marker

In this article, you'll learn about the ITLN1 marker and its uses. This marker is produced by goblet cells and forms oligomers. Find out more about Cell proliferation tests and GWAS as a link to type-2 diabetes mellitus. These are only some of the many uses of this marker. Boster Bio is a fantastic source for researchers.

ITLN1 expression in goblet cells

Human goblet cell are a rich source of the ITLN1 gene. It is not as prevalent in paneth cells, and the ileum. This study investigated the relationship between ITLN1 and the ileal CD. In this study, we employed an anti-ITLN antibody to label goblet cells and mice with an ITLN1NTERM antibody to label Paneth cells.

ITLN-1 protein recognizes galactofuranose within the cell walls of bacterial cells. It is secreted by goblet cells from the intestinal. Experiments performed in mice showed that ITLN1 expression is enhanced when IL-13 is overexpressed in airways. However, its function in human bronchi remains undetermined. We would like to determine ITLN1 in human lungs tissues and improve our understanding of its function as an asthma trigger.

To find out whether ITLN1 expression is elevated in colonic mucus secreting cells, we used biopsies of patients with no IBD. We used antisera to identify the expression of the intelectin domain. In addition to ITLN1NTERM We also used ITLNCONS antibody to determine the goblet cells that reside in colonic tissue. In addition, we used MUC2C3 anti-mucin protein to color the secretory granules of goblet cells.

ITLN1 is a carbohydrate-binding protein that spans chordate evolutionary. Previous GWAS connected ITLN1 with Crohn's disease. LD was associated to risk alleles. Ensembl database confirmed that SNPs that cause LD are present. The genes involved in LD were also found in goblet cells from both the European and African superpopulations.

Despite the high degree of homology, there are still a number of differences between ITLN1 and ITLN2. For instance, both proteins contain two signal sequences, however there is a distinct N-terminus . Also, those regions that overlap with the protein are highly dissimilar. The 20-amino-amino-amino acid regions delineate ITLN1 from ITLN2 and ITLN2, while the rest of the mature protein has a greater conservation.

ITLN1 oligomerization

We studied ITLN1 oligomerization with the Boster Bio ITLN1 assay. To determine if genetic variation can affect ITLN1 oligomerization, we analyzed ileal specimens of homozygote individuals. Genotypes VV, DD and V109D did not affect ITLN1 oligomerization. The binding of ITLN1 was not affected by the V109D genotype.

The colon and small intestine are the main home for the human mRNA and the proteins of ITLN1. Quantitative real-time real-time RTPCR has been used in our research. We also investigated the impact of the V109D genotype on copy number. The results indicated that oligomerization in V109-ITLN1 can be reversed. The binding kinetics of V109-ITLN1 D-galactofuranose that was immobilized were the same as those of D109-ITLN1.

Previous research has linked Crohn's disease to ITLN1 oligomerization. The Ensembl database identified disease-related SNPs in LD. SNPs linked to LD were identified in both African and European populations. The analysis of intestinal tissue proved that it was goblet-cell derived. However, further research is required to better understand the function of ITLN1 oligomerization in the inflammatory intestinal disease.

ITLN1 is implicated in various human diseases, including Type 2 Diabetes and Inflammatory Bowel Disease. It is a multimeric protein that possesses a calcium-dependent carbohydrate binding domain. In humans, ITLN1 has been linked to a variety of illnesses and is related to the innate immune system. It can be classified into ITLN1-like proteins according to amino acid length and primary sequence.

Boster Bio has conducted several studies using ITLN1 peptide that is coupled with keyhole limpet hemocyanin, maleimide activated KLH, as well as an antigen to control. The protocol was approved by the U.S. Department of Health and Human Services, Public Health Service and Animal Welfare Assurance Committee. Find out more about testing the ITLN1 protein in Boster Bio.

Assay for cell proliferative capacity

The most important regulator of tumor growth is the ITLN1 gene. A recent study revealed that patients suffering from HGSC have significantly lower levels of this protein. This could be due the formation of stress fibers and calcium mobilization that are both essential for tumor cells' greater motility and invasive ability. We transfected SHY5Y cells by transfecting them with sh-Scb, empty vectors, ITLN1, or an ITLN1 vector to test the expression of ITLN1 in tumor cells. We then examined the effect of these proteins on the proliferation of cancer cells in vitro and in vivo, and found that the ITLN1 gene blocked both of these actions.

In addition to its proliferation-specific activity, ITLN1 inhibits LTF's effect on OC motility and invasive potential, and suppresses OC motility and invasive potential. These characteristics of ITLN1 make it an effective marker for studying OC development. It has been shown to be a reliable biomarker in predicting prognosis of patients with different types of cancers.

ITLN1 is highly correlated with other genes that are found in NB tumors. It is interesting to note that ITLN1 has positive correlations with DCUN1D5 ENO1, MACF1 PPM1G, NDRG2, which are all related to cancer. We also found an association between ITLN1 and NDRG2 transcript levels in 88 NB cases using Pearson's coefficient correlation analysis.

Western analysis of ITLN1 proteins revealed that LTF increased the levels of p–ERK1/2 and P–Jun (S73), total June and MMP1. LTF also prevented the growth of c cells by reducing the amount of d cells. The LTF-LTN1 interaction was weakened by ITLN1.

GWAS association type 2 diabetes mellitus

The GWAS association was linked to type 2 diabetes melitus. These results were strong even in African populations. The main variant, rs12277475, was included in both the Zulu and AADM studies. This variant could be a brand new type 2 diabetes risk gene. However it is not linked with the VNTR. The study's findings are positive However, further research is needed to understand the role of the variant and the potential impact it could have on disease.

A meta-analysis of genome-wide association studies (GWASs) suggests that there are additional susceptibility loci. These findings aren't new, but they suggest that drug development could have additional targets. It is important to note that the PCSK9 target was discovered using a traditional family-based design. However, many more targets could be discovered through GWAS. GWAS is an effective tool for development of new drugs.

Two major genetic loci are involved in type 2 diabetes mellitus. Both loci were identified in GWAS studies of individuals with European ancestry. The GWAS-T2D connections were also identified by a meta-analysis involving 32 GWAS for participants with European ancestry. Although GWAS-T2D findings are publicly accessible however individual GWAS results are not. However, these data provide new insight into the pathogenesis of T2D.

GWAS in human genetics offers many advantages, however, there are some limitations. For instance, the GWAS associated signal is usually not a precise indicator of the causal variant. The genotyping arrays used in GWAS are designed to determine the haplotype of a person using a few SNPs. The sequence of other SNPs within the linkage disequilibrium block could be inferred from the tag SNP.

Body mass index quantitative trait locus 11

The BMI QTL11 marker has been used to identify possible genes that could be responsible for obesity and metabolic disorders in general. In FHS data there are two QTLs influence BMI, one of them being 7q31-q34 and the other on 13q14. The QTL 7q31-q34 contains a prominent candidate gene, leptin that has significant physiological effects on energy balance. Another region also has an unproven QTL at 13q14. Further research is needed to identify possible candidate genes. Other links that suggest a linkage were detected on 1q23-24, 2q37, 3q29, as well as 5q23-q35.

The BMI-QTL11 test revealed that the apoD location was linked to %BF as well as six skinfold measurements. The same region was associated with obesity-related characteristics in white British subjects. The evidence from Rainwater and colleagues. Rainwater et al. identified an LOD score of 4.11.

While the BMI-QTL11 marker is an accurate predictor of BMI but it is difficult to determine which BMI genes are associated with specific diseases. There are many variables that can influence the genetic linkage, including the population studied, effectiveness of the sample unit, and the method of analysis. Further research is required to determine if a gene is associated with or not with BMI.

QTL11 has been used in salmon breeding since. It has been used routinely by salmon breeding companies such as AquaGen genetics and Hendrix genetics. For example, Houston et al. (2008) discovered a significant QTL in post-smolts, which was responsible for up to 79% of phenotypic variation in four segregating families.