Recombinant Human ITLN1
Cat.No. : | ITLN1-29873TH |
Product Overview : | Recombinant Full Length Human ITLN1 produced in Saccharomyces cerevisiae; amino acids 1-313; 313 amino acids, MWt 32.9 kDa. Protein is tagged with 26 kDa proprietary tag. |
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Description : | Intelectin-1 also known as the intestinal lactoferrin receptor is a protein that in humans is encoded by the ITLN1 gene. Intelectin-1 functions both as a receptor for bacterial arabinogalactans and for lactoferrin. |
Tissue specificity : | Highly expressed in omental adipose tissue where it is found in stromal vascular cells but not in fat cells but is barely detectable in subcutaneous adipose tissue (at protein level). Highly expressed in the small intestine. Also found in the heart, testi |
Form : | Liquid |
Purity : | >90% by SDS-PAGE |
Storage buffer : | Preservative: NoneConstituents: 30% Glycerol, 0.5% Triton-X-100, 50mM HEPES, 30mM Glutathione, 100mM Sodium chloride, 1mM DTT, pH 7.5 |
Storage : | Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles. |
Sequences of amino acids : | MNQLSFLLFLIATTRGWSTDEANTY FKEWTCSSSPSLPRS CKEIKDECPSAFDGLYFLRTENGVI YQTFCDMTSGGGG WTLVASVHENDMRGKCTVGDRWSSQ QGSKAVYPEGDGN WANYNTFGSAEAATSDDYKNPGYYD IQAKDLGIWHVPNKS PMQHWRNSSLLRYRTDTGFLQTLGH NLFGIYQKYPVKY GEGKCWTDNGPVIPVVYDFGDAQKT ASYYSPYGQREFT AGFVQFRVFNNERAANALCAGMRVT GCNTEHHCIGGGGYFPEASPQQCGD FSGFDWSGYGTHVGYSSSREITEAA VLL FYR |
Sequence Similarities : | Contains 1 fibrinogen C-terminal domain. |
Gene Name : | ITLN1 intelectin 1 (galactofuranose binding) [ Homo sapiens ] |
Official Symbol : | ITLN1 |
Synonyms : | ITLN1; intelectin 1 (galactofuranose binding); intelectin-1; FLJ20022; hIntL; HL 1; ITLN; LFR; |
Gene ID : | 55600 |
mRNA Refseq : | NM_017625 |
Protein Refseq : | NP_060095 |
MIM : | 609873 |
Uniprot ID : | Q8WWA0 |
Chromosome Location : | 1q21.3 |
Function : | receptor binding; sugar binding; |
Products Types
◆ Recombinant Protein | ||
ITLN1-197H | Recombinant Human ITLN1 Protein | +Inquiry |
ITLN1-3575H | Recombinant Human ITLN1 | +Inquiry |
ITLN1-4958H | Recombinant Human ITLN1 Protein, GST-tagged | +Inquiry |
ITLN1-113H | Recombinant Human Intelectin 1 (galactofuranose binding) | +Inquiry |
ITLN1-57H | Active Recombinant Human Omentin 1, FLAG-tagged | +Inquiry |
Related Gene
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (6)
Ask a questionIn future studies, it is worth paying attention to the relationship between structure and function, expression regulation, association with other proteins or diseases, and therapeutic potential. At the same time, further research is needed on the similarities and differences between them and other protein inhibitors, as well as their differences in different species.
The expression level of ITLN1 is regulated by a variety of factors, including processes such as gene transcription, translation, and post-translational modifications, as well as hormones, nutrients, and other environmental factors in the body.
Yes, ITLN1 may have other biological activities in addition to trypsin inhibitory activity. For example, it may play a role in processes such as immune regulation, cell growth, and apoptosis.
Yes, there may be some differences in ITLN1 in different species, such as different degrees of variation in structure, function, and expression levels.
The synthesis and secretion of ITLN1 in the human body involves multiple steps and complex regulatory mechanisms, including gene transcription, translation, post-translational modification and secretion.
There are certain similarities and differences between ITLN1 and other protein inhibitors in terms of structure, function, and mechanism of action. For example, other protein inhibitors may have different mechanisms of inhibition and ranges of action.
Customer Reviews (3)
Write a reviewITLN1 activity is good, and the required biological activity experiments can be carried out effectively.
The results show that the protein has good crystallinity, which is helpful for crystallographic study.
Its high solubility allows for easy preparation of the required concentration.
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