Recombinant Human Peptidoglycan Recognition Protein 1 (PGLYRP1) Protein (His&Myc)

Name: Recombinant Human Peptidoglycan Recognition Protein 1 (PGLYRP1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-05176P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Peptidoglycan Recognition Protein 1 (PGLYRP1) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O75594
Target Symbol	PGLYRP1
Synonyms	MGC126894; MGC126896; Peptidoglycan recognition protein 1; Peptidoglycan recognition protein; Peptidoglycan recognition protein short; PGLYRP; PGLYRP1; PGRP; PGRP S; PGRP-S; PGRP1_HUMAN; PHRP, short; SBBI68; TAG7; TNF superfamily, member 3 (LTB)-like (peptidoglycan recognition protein); TNFSF 3L; TNFSF3L; UNQ639/PRO1269
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	QETEDPACCSPIVPRNEWKALASECAQHLSLPLRYVVVSHTAGSSCNTPASCQQQARNVQHYHMKTLGWCDVGYNFLIGEDGLVYEGRGWNFTGAHSGHLWNPMSIGISFMGNYMDRVPTPQAIRAAQGLLACGVAQGALRSNYVLKGHRDVQRTLSPGNQLYHLIQNWPHYRSP
Expression Range	22-196aa
Protein Length	Full Length of Mature Protein
Mol. Weight	26.9 kDa
Research Area	Cancer
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.
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	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. 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. In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement. Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system. 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 cell specificity. Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor.
Subcellular Location	Secreted. Cytoplasmic granule.
Protein Families	N-acetylmuramoyl-L-alanine amidase 2 family
Database References	HGNC: 8904 OMIM: 604963 KEGG: hsa:8993 STRING: 9606.ENSP00000008938 UniGene: PMID: 29850628 the results of this study provide evidence for a novel role of the Tag7 protein in the immune response PMID: 28977785 Tag7 activates lymphocytes capable of Fasl-Fas-dependent contact killing of virus-infected cells. PMID: 29083508 The interaction of Fas receptor with FasL leads to an activation of the Tag7-Hsp70 complex in the lymphocyte membrane fraction, and here FasL acts as a receptor that induces intracellular signaling in lymphocytes.An interaction of the MicA stress ligand with the NKG2D receptor is necessary for the release of this cytotoxic complex PMID: 27868339 interaction of Tag7-Hsp70 with the TNFR1 receptor triggered a certain sequence of events: at first, it activated RIP1 kinase, and later on, increased intracellular concentration of capital ES, Cyrillicsmall a, Cyrillic(2+) ions and an activation of calpains, which led to the permeabilization of the lysosomal membranes PMID: 26796882 Tag7-Mts1 complex causes chemotactic migration of lymphocytes, with NK cells being a preferred target. PMID: 26654597 Tag7, can bind to the TNFR1 receptor, thereby inhibiting the cytotoxic actions of the Tag7-Hsp70 complex and TNF-alpha, an acquired immunity cytokine. PMID: 26183779 The role for PGLYRP1 as a TREM-1 activator provides a new mechanism by which bacteria can trigger myeloid cells, linking two known, but previously unrelated, pathways in innate immunity. PMID: 25595774 The association study in a discovery sample of 200 French trio families revealed a significant association with rheumatoid arthritis for one SNP, PGLYRP1-rs2041992 (p = 0.019). PMID: 25221852 shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complex PMID: 22037021 The PGRP-S promoter provides a useful reporter of M cell mucosal epithelium lineage commitment, corresponding to the expression of PGRP in M cells. PMID: 21984701 HspBP1 inhibited the cytotoxic activity of the Tag7-Hsp70 complex secreted by lymphocytes. HspBP1 PMID: 21247889 Various types of human blood cells were tested for expression of the Tag7/PGRP-SA and TagL/PGRP-L proteins, which belong to the family of proteins possessing the lysozyme-like peptidoglycan recognition protein (PGRP) domain PMID: 12669421 identification as an N-acetylmuramoyl-l-alanine amidase and this function is conserved in prokaryotes, insects, and mammals PMID: 14506276 Peptidoglycan recognition protein tag7 forms a cytotoxic complex with heat shock protein 70 in solution and in lymphocytes. PMID: 14585845 crystal structure of the C-terminal PGN-binding domain of PGRP-Ialpha in two oligomeric states, monomer and dimer PMID: 15140887 determined the crystal structure, at 2.30-A resolution, of the C-terminal PGN-binding domain of human PGRP-Ialpha in complex with a muramyl tripeptide representing the core of lysine-type PGNs from Gram-positive bacteria PMID: 15572450 crystal structure of peptidoglycan recognition protein S PMID: 15769462 human PGRP-S plays a role in innate immunity in the context of neutrophils by contributing to the killing of intracellular and extracellular bacteria PMID: 15956276 Association of psoriasis to PGLYRP and SPRR genes at PSORS4 locus on 1q shows heterogeneity between Finnish, Swedish and Irish families. PMID: 18643845 peptidoglycan recognition protein-1 has a role in coronary and peripheral atherosclerosis PMID: 18774573 Data show that removal of both Tag7 and S100A4 from neutrophil conditioned medium reduced lysis of E. coli, while addition of the Tag7-S100A4 complex to the medium restored antibacterial activity. PMID: 19023966 S100A4 has opposite roles in Tag7 and Hsp70- mediated tumoricidal mechanisms PMID: 19666596

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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.