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Manufactured by BioVendor

Serglycin Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:HEK293
  • Other names:Hematopoietic proteoglycan core protein, Platelet proteoglycan core protein, P.PG, Secretory granule proteoglycan core protein,, SRGN
  • Species:Human
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Cat. No. Size Price


RD172368100-HEK 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 137 AA. MW: 15.5 kDa (calculated). UniProtKB acc. No. P10124 (Tyr28–Leu158). C-terminal His-tag (6 extra AA).

Amino Acid Sequence

YPTRRARYQWVRCNPDSNSANCLEEKGPMFELLPGESNKIPRLRTDLFPKTRIQDLNRIFPLSEDYSGSGFGSGSGSGSGSGSGFLTEMEQDYQLVDESDAFHDNLRSLDRNLPSDSQDLGQHGLEEDFMLHHHHHH

Source

HEK293

Purity

Purity as determined by densitometric image analysis: > 95%

SDS-PAGE Gel

14 % SDS-PAGE separation of Human Serglycin (HEK):
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. Reduced and boiled sample, 2.5 μg/lane
3. Non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 1.0 EU/μg

Formulation

0.25–0.70 mg/ml solution in phosphate buffered saline, 20 % (w/v) glycerol, filtered (0.4 μm), frozen.

Reconstitution

Defrost at ambient temperature.Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.

Applications

Western blotting, ELISA, Cell culture and/or animal studies

Shipping

On ice. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store protein at -80°C. Protein remains stable until the expiry date when stored at -80°C. Avoid repeated freezing/thawing cycles.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Apoptosis, Cardiovascular disease, Immune Response, Infection and Inflammation, Oncology

Summary

In a recent study serglycin was found to be among the most abundantly expressed proteins in adipocytes of epicardial adipose tissue in patients with coronary artery disease (CAD). It was demonstrated that TNFα induces expression and secretion of serglycin in adipocytes. Circulating serglycin might also participate in the mechanism of systemic vascular insult and atheromatous change. Serglycin is a dominant intracellular proteoglycan expressed by immune cells, where it interacts with numerous inflammatory mediators, such as proteases, chemokines, cytokines, and growth factors. Serglycin is implicated in their storage into the granules and their protection since they are secreted as complexes and delivered to their targets after secretion. Serglycin secretion can be induced in several cell types upon external inflammatory stimulation. The biosynthesis of serglycin is up-regulated by lipopolysaccharide (LPS) in macrophages, tumor necrosis factor (TNF) in endothelial cells and adipo¬cytes and interleukin 1b (IL-1b) in smooth muscle cells. Another interesting implication of serglycin in the regulation of immune system is its ability to inhibit complement system activity. Serglycin is also involved in apoptosis and immune regulation. Mast cells lacking serglycin expression preferentially died by necrosis rather than apoptosis. Serglycin has been shown to be a biomarker of acute myeloid leukemia (levels are higher than in acute lymphoblastic leukemia patients). Invasive nasopharyngeal carcinoma (NPC) cells secrete higher levels of serglycin and expression is elevated in NPC cells with higher metastasis potential. Serglycin is also highly expressed in breast cancer tissues and by an aggressive breast cancer cell line.

Summary References (14)

References to Serglycin

  • Imoto-Tsubakimoto H, Takahashi T, Ueyama T, Ogata T, Adachi A, Nakanishi N, Mizushima K, Naito Y, Matsubara H. Serglycin is a novel adipocytokine highly expressed in epicardial adipose tissue. Biochem Biophys Res Commun. 2013 Mar 1;432 (1):105-10
  • Kolset SO, Pejler G. Serglycin: a structural and functional chameleon with wide impact on immune cells. J Immunol. 2011 Nov 15;187 (10):4927-33
  • Kolseth IB, Reine TM, Vuong TT, Meen AJ, Fan Q, Jenssen TG, Gronning-Wang LM, Kolset SO. Serglycin is part of the secretory repertoire of LPS-activated monocytes. Immun Inflamm Dis. 2015 Mar;3 (1):23-31
  • Korpetinou A, Skandalis SS, Labropoulou VT, Smirlaki G, Noulas A, Karamanos NK, Theocharis AD. Serglycin: at the crossroad of inflammation and malignancy. Front Oncol. 2014 Jan 13;3:327
  • Korpetinou A, Skandalis SS, Moustakas A, Happonen KE, Tveit H, Prydz K, Labropoulou VT, Giannopoulou E, Kalofonos HP, Blom AM, Karamanos NK, Theocharis AD. Serglycin is implicated in the promotion of aggressive phenotype of breast cancer cells. PLoS One. 2013;8 (10):e78157
  • Li XJ, Ong CK, Cao Y, Xiang YQ, Shao JY, Ooi A, Peng LX, Lu WH, Zhang Z, Petillo D, Qin L, Bao YN, Zheng FJ, Chia CS, Iyer NG, Kang TB, Zeng YX, Soo KC, Trent JM, Teh BT, Qian CN. Serglycin is a theranostic target in nasopharyngeal carcinoma that promotes metastasis. Cancer Res. 2011 Apr 15;71 (8):3162-72
  • Li XJ, Qian CN. Serglycin in human cancers. Chin J Cancer. 2011 Sep;30 (9):585-9
  • Melo FR, Grujic M, Spirkoski J, Calounova G, Pejler G. Serglycin proteoglycan promotes apoptotic versus necrotic cell death in mast cells. J Biol Chem. 2012 May 25;287 (22):18142-52
  • Niemann CU, Abrink M, Pejler G, Fischer RL, Christensen EI, Knight SD, Borregaard N. Neutrophil elastase depends on serglycin proteoglycan for localization in granules. Blood. 2007 May 15;109 (10):4478-86
  • Niemann CU, Cowland JB, Klausen P, Askaa J, Calafat J, Borregaard N. Localization of serglycin in human neutrophil granulocytes and their precursors. J Leukoc Biol. 2004 Aug;76 (2):406-15
  • Niemann CU, Kjeldsen L, Ralfkiaer E, Jensen MK, Borregaard N. Serglycin proteoglycan in hematologic malignancies: a marker of acute myeloid leukemia. Leukemia. 2007 Dec;21 (12):2406-10
  • Scully OJ, Chua PJ, Harve KS, Bay BH, Yip GW. Serglycin in health and diseases. Anat Rec (Hoboken). 2012 Sep;295 (9):1415-20
  • Skliris A, Happonen KE, Terpos E, Labropoulou V, Borset M, Heinegard D, Blom AM, Theocharis AD. Serglycin inhibits the classical and lectin pathways of complement via its glycosaminoglycan chains: implications for multiple myeloma. Eur J Immunol. 2011 Feb;41 (2):437-49
  • Zernichow L, Abrink M, Hallgren J, Grujic M, Pejler G, Kolset SO. Serglycin is the major secreted proteoglycan in macrophages and has a role in the regulation of macrophage tumor necrosis factor-alpha secretion in response to lipopolysaccharide. J Biol Chem. 2006 Sep 15;281 (37):26792-801
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