Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | O75594 |
express system | HEK293 |
product tag | C-hFc |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Innate immunity protein Tag7 (PGRP-S, PGLYRP1) can interact with the TNFα receptor, TNFR1, and block the transduction of apoptotic signals through this receptor. A complex formed between the Tag7 protein and the major heat shock protein Hsp70 can activate TNFR1 receptor and induce tumor cell death via either apoptotic or necroptotic pathway. |
molecular weight | The protein has a predicted MW of 46.2 kDa. Due to glycosylation, the protein migrates to 55-60 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human PGLYRP1 Protein 3518
$300.00 – $1,000.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Gln22-Pro196
Human PGLYRP1 Protein 3518
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Innate immunity protein Tag7 (PGRP-S, PGLYRP1) can interact with the TNFα receptor, TNFR1, and block the transduction of apoptotic signals through this receptor. A complex formed between the Tag7 protein and the major heat shock protein Hsp70 can activate TNFR1 receptor and induce tumor cell death via either apoptotic or necroptotic pathway. |
Protein names Peptidoglycan recognition protein 1 (Peptidoglycan recognition protein short) (PGRP-S) |
Gene names PGLYRP1,PGLYRP1 PGLYRP PGRP TNFSF3L SBBI68 UNQ639/PRO1269 |
Protein family N-acetylmuramoyl-L-alanine amidase 2 family |
Mass 9606Da |
Function Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:21247889, PubMed:26183779). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement (PubMed:26654597). Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system (PubMed:30713770). Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity (PubMed:28977785, PubMed:29083508). Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (PubMed:25595774, PubMed:28977785). |
Subellular location Secreted. Cytoplasmic granule . |
Tissues Highly expressed in bone marrow. Weak expression found in kidney, liver, small intestine, spleen, thymus, peripheral leukocyte, lung, fetal spleen and neutrophils. |
Structure Homodimer; disulfide-linked (PubMed:15769462, PubMed:16354652). Interacts with HSPA1A; this interaction forms a cytotoxic complex that is released by lymphokine-activated killer cells (By similarity). Interacts with HSPBP1; this interaction blocks the cytotoxic activity of the PGLYRP1-HSPA1A complex (PubMed:21247889). Interacts with TNFRSF1A; this interaction is important for cell death induction (PubMed:26183779). Interacts with S100A4; this complex acts as a chemoattractant that promotes lymphocyte movement (PubMed:26654597, PubMed:30713770). Interacts with TREM1 (PubMed:25595774). |
Post-translational modification N-glycosylated. N-glycosylation is required for bactericidal activity. |
Target Relevance information above includes information from UniProt accession: O75594 |
The UniProt Consortium |
Data
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