Recombinant Human Leucine-rich repeat-containing protein 15 (LRRC15), partial

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Code CSB-EP819484HU
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Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Others
Alternative Names
hLib; Leucine-rich repeat protein induced by beta-amyloid homolog; Leucine-rich repeat-containing protein 15; LIB; LRC15_HUMAN; LRRC15
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
22-538aa
Target Protein Sequence
YHGCPSECTCSRASQVECTGARIVAVPTPLPWNAMSLQILNTHITELNESPFLNISALIALRIEKNELSRITPGAFRNLGSLRYLSLANNKLQVLPIGLFQGLDSLESLLLSSNQLLQIQPAHFSQCSNLKELQLHGNHLEYIPDGAFDHLVGLTKLNLGKNSLTHISPRVFQHLGNLQVLRLYENRLTDIPMGTFDGLVNLQELALQQNQIGLLSPGLFHNNHNLQRLYLSNNHISQLPPSVFMQLPQLNRLTLFGNSLKELSPGIFGPMPNLRELWLYDNHISSLPDNVFSNLRQLQVLILSRNQISFISPGAFNGLTELRELSLHTNALQDLDGNVFRMLANLQNISLQNNRLRQLPGNIFANVNGLMAIQLQNNQLENLPLGIFDHLGKLCELRLYDNPWRCDSDILPLRNWLLLNQPRLGTDTVPVCFSPANVRGQSLIIINVNVAVPSVHVPEVPSYPETPWYPDTPSYPDTTSVSSTTELTSPVEDYTDLTTIQVTDDRSVWGMTQAQSG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
65.2 kDa
Protein Length
Partial
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

To express the recombinant human LRRC15 protein in E.coli cells, a DNA fragment encoding the human LRRC15 protein (22-538aa) is inserted into a plasmid vector along with the N-terminal 10xHis and C-terminal Myc-tag gene and transferred to the E.coli cells. Cells containing the plasmid are screened, cultured, and induced to express the LRRC15 protein. Lysing the cells allows for the collection of the recombinant human LRRC15 protein, which is purified through affinity purification and then identified through SDS-PAGE and subsequent staining of the gel with Coomassie Brilliant Blue. The purity of the recombinant human LRRC15 protein obtained is greater than 90%.

LRRC15 is a cell surface glycoprotein that plays crucial roles in various biological processes. It is normally expressed in specific tissues like the invasive cytotrophoblast layer of the placenta [1]. LRRC15 has been identified as a tumor antigen and is overexpressed in androgen-independent metastatic prostate cancer [2]. Recent studies have highlighted LRRC15's significance in cancer biology, particularly in the context of tumor immunity suppression [3]. LRRC15 is associated with cancer-associated fibroblasts (CAFs) and linked to cancer grade and outcome [4]. Moreover, LRRC15 has been implicated in viral infections, such as being a receptor for SARS-CoV-2 spike protein and influencing antiviral and antifibrotic transcriptional programs [5]. It has also been suggested that LRRC15 may have a role in controlling infection and suppressing lung fibrosis [6].

LRRC15's involvement in various diseases and its potential as a therapeutic target has garnered significant attention. Studies have explored targeting LRRC15 for inhibiting metastatic dissemination in ovarian cancer [7]. J. Purcell and his colleagues have developed LRRC15 as a stromal target for antibody-drug conjugates in cancer treatment [8]. Furthermore, LRRC15 has been proposed as a promising anti-cancer target due to its overexpression in mesenchymal-derived tumors and cancer-associated fibroblasts in the microenvironment of different types of tumors [9].

References:
[1] M. Stanbrough, G. Bubley, K. Ross, T. Golub, M. Rubin, T. Penninget al., Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer, Cancer Research, vol. 66, no. 5, p. 2815-2825, 2006. https://doi.org/10.1158/0008-5472.can-05-4000
[2] Y. Gong, Z. Wang, A. Beitelshees, C. McDonough, T. Langaee, K. Hallet al., Pharmacogenomic genome-wide meta-analysis of blood pressure response to β-blockers in hypertensive african americans, Hypertension, vol. 67, no. 3, p. 556-563, 2016. https://doi.org/10.1161/hypertensionaha.115.06345
[3] A. Krishnamurty, J. Shyer, M. Thai, V. Gandham, M. Buechler, Y. Yanget al., Lrrc15+ myofibroblasts dictate the stromal setpoint to suppress tumour immunity, Nature, vol. 611, no. 7934, p. 148-154, 2022. https://doi.org/10.1038/s41586-022-05272-1
[4] P. Baurand, J. Balland, C. Reynas, M. Ramseyer, D. Vivier, P. Bellayeet al., Development of anti-lrrc15 small fragments for imaging purposes using a phage-display scfv approach, International Journal of Molecular Sciences, vol. 23, no. 20, p. 12677, 2022. https://doi.org/10.3390/ijms232012677
[5] L. Loo, M. Waller, C. Moreno, A. Cole, A. Stella, O. Popet al., Fibroblast-expressed lrrc15 is a receptor for sars-cov-2 spike and controls antiviral and antifibrotic transcriptional programs, Plos Biology, vol. 21, no. 2, p. e3001967, 2023. https://doi.org/10.1371/journal.pbio.3001967
[6] J. Orgel, Molecular tissue responses to mechanical loading, International Journal of Molecular Sciences, vol. 23, no. 4, p. 2074, 2022. https://doi.org/10.3390/ijms23042074
[7] U. Ray, D. Jung, L. Jin, Y. Xiao, S. Dasari, S. Bhattacharyaet al., Targeting lrrc15 inhibits metastatic dissemination of ovarian cancer, Cancer Research, vol. 82, no. 6, p. 1038-1054, 2022. https://doi.org/10.1158/0008-5472.can-21-0622
[8] J. Purcell, S. Tanlimco, J. Hickson, M. Fox, M. Sho, L. Durkinet al., Lrrc15 is a novel mesenchymal protein and stromal target for antibody–drug conjugates, Cancer Research, vol. 78, no. 14, p. 4059-4072, 2018. https://doi.org/10.1158/0008-5472.can-18-0327
[9] U. Ray, C. Pathoulas, P. Thirusangu, J. Purcell, N. Kannan, & V. Shridhar, Exploiting lrrc15 as a novel therapeutic target in cancer, Cancer Research, vol. 82, no. 9, p. 1675-1681, 2022. https://doi.org/10.1158/0008-5472.can-21-3734

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Target Background

Gene References into Functions
  1. LRRC15 expression is significantly upregulated in human masticatory mucosa during wound healing PMID: 28005267
  2. Lib may contribute to regulation of cell-matrix adhesion interactions with respect to astrocyte recruitment around senile plaques in Alzheimer's disease brain PMID: 16098915
  3. Tumor antigen LRRC15 impedes adenoviral infection: implications for virus-based cancer therapy are presented. PMID: 18385238
  4. LRRC15 is induced by EWS-WT1(+KTS) in the tumor DSRCT and may play a role in cellular invasion. PMID: 12923058
Subcellular Location
Membrane; Single-pass type I membrane protein.
Tissue Specificity
Brain and placenta.
Database Links

HGNC: 20818

KEGG: hsa:131578

STRING: 9606.ENSP00000389128

UniGene: Hs.288467

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