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1000 results found for “pitpn”
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Name :
MMP12 Human (1-33)Description:
Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant
Product # :
ENZ-1201Price :
Quantity :
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Shipped at Room temp
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Description
The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized MMP12 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.
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Background
Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RYBP HumanDescription:
RING1 & YY1 Binding Protein Human Recombinant
RING1 and YY1 binding protein, Death effector domain-associated factor, Apoptin-associating protein 1, YY1 and E4TF1-associated factor 1, ring1 interactor RYBP, DED-associated factor, APAP-1, DEDAF, YEAF1.
Product # :
PRO-1139Price :
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Shipped with Ice Packs
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Description
RYBP Human Recombinant produced in E. coli is a single polypeptide chain containing 252 amino acids (1-228) and having a molecular mass of 27.4 kDa.RYBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RYBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RING1- and YY1-binding protein (RYBP) belongs to the polycomb group (PcG). RYBP interacts with MDM2 and decreases MDM2-mediated p53 ubiquitination, which leads to stabilization of p53 and an increase in p53 activity. RYBP causes cell-cycle arrest and is involved in the p53 response to DNA damage. RYBP interacts with RING1, YY1, Caspase 10, E2F3, E2F2, Mdm2, Abl gene and CBX2. RYBP inhibits ubiquitination and subsequent degradation of TP53, and thus has a role in regulating transcription of TP53 target genes. RYBP may also be involved in the regulation of the transcription as a repressor of the transcriptional activity of E4TF1. RYBP may bind to DNA, and promote apoptosis.
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Synonyms
RING1 and YY1 binding protein, Death effector domain-associated factor, Apoptin-associating protein 1, YY1 and E4TF1-associated factor 1, ring1 interactor RYBP, DED-associated factor, APAP-1, DEDAF, YEAF1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMTMGDK KSPTRPKRQA KPAADEGFWD CSVCTFRNSA EAFKCSICDV RKGTSTRKPR INSQLVAQQV AQQYATPPPP KKEKKEKVEK QDKEKPEKDK EISPSVTKKN TNKKTKPKSD ILKDPPSEAN SIQSANATTK TSETNHTSRP RLKNVDRSTA QQLAVTVGNV TVIITDFKEK TRSSSTSSST VTSSAGSEQQ NQSSSGSEST DKGSSRSSTP KGDMSAVNDE SF
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ALPL MouseDescription:
Alkaline Phosphatase Liver/Bone/Kidney Mouse Recombinant
Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.
Product # :
ENZ-1008Price :
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Shipped with Ice Packs
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Description
ALPL produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 493 amino acids (19-503 a.a.) and having a molecular mass of 54.5kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). ALPL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALPL protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 46,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of 4-Methylumbelliferyl phosphate to phosphate and 4-Methylumbelliferone per minute at pH 8.8 at 25C.More Info
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Introduction
Alkaline Phosphatase Liver/Bone/Kidney (Alpl) is a part of the alkaline phosphatases family which comprises 4 related alkaline phosphatases. Alpl is a membrane-bound glycosylated enzyme which is not expressed in any particular tissue. Alpl takes part in skeletal mineralization.
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Synonyms
Alpl, Akp-2, Akp2, ALP, APTNAP, TNAP, TNSALP, HOPS, AP-TNAP, Alkaline phosphatase 2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
VPEKERDPSY WRQQAQETLK NALKLQKLNT NVAKNVIMFL GDGMGVSTVT AARILKGQLH HNTGEETRLE MDKFPFVALS KTYNTNAQVP DSAGTATAYL CGVKANEGTV GVSAATERTR CNTTQGNEVT SILRWAKDAG KSVGIVTTTR VNHATPSAAY AHSADRDWYS DNEMPPEALS QGCKDIAYQL MHNIKDIDVI MGGGRKYMYP KNRTDVEYEL DEKARGTRLD GLDLISIWKS FKPRHKHSHY VWNRTELLAL DPSRVDYLLG LFEPGDMQYE LNRNNLTDPS LSEMVEVALR ILTKNLKGFF LLVEGGRIDH GHHEGKAKQA LHEAVEMDQA IGKAGAMTSQ KDTLTVVTAD HSHVFTFGGY TPRGNSIFGL APMVSDTDKK PFTAILYGNG PGYKVVDGER ENVSMVDYAH NNYQAQSAVP LRHETHGGED VAVFAKGPMA HLLHGVHEQN YIPHVMAYAS CIGANLDHCA WAGSGLEHHH HHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DKK1 MouseDescription:
Dickkopf-Related Protein 1 Mouse Recombinant
Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-1.
Product # :
PRO-2756Price :
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Shipped with Ice Packs
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Description
DKK1 Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-272a.a) containing 247 amino acids and having a molecular mass of 26.9kDa.DKK1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The DKK1 solution (0.25mg/ml) contains 50mM MES buffer (pH 6.5) and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Dickkopf-related protein 1 (DKK1) antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by creating a ternary complex with the transmembrane protein KREMEN which promotes internalization of LRP5/6. DKKs have a significant role in vertebrate development, where they locally inhibit Wnt controlled processes for instance antero-posterior axial patterning, limb development, somitogenesis and eye formation. Furthermore, Dkks are involved in bone formation and bone disease, cancer and Alzheimer disease in Adults.
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Synonyms
Dkk-1, mDkk-1, Dkk1, Dickkopf-related protein 1, Dickkopf-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
TLNSVLINSN AIKNLPPPLG GAGGQPGSAV SVAPGVLYEG GNKYQTLDNY QPYPCAEDEE CGSDEYCSSP SRGAAGVGGV QICLACRKRR KRCMRHAMCC PGNYCKNGIC MPSDHSHFPR GEIEESIIEN LGNDHNAAAG DGYPRRTTLT SKIYHTKGQE GSVCLRSSDC AAGLCCARHF WSKICKPVLK EGQVCTKHKR KGSHGLEIFQ RCYCGEGLAC RIQKDHHQAS NSSRLHTCQR
HHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CD105 Human, HisDescription:
Endoglin Human Recombinant, His-Tag
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-823Price :
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- sds-page
Description
Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
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Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.
What is the source or expression system of CD105 Protein?
Escherichia Coli.
What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
EPYC HumanDescription:
Epiphycan Human Recombinant
Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.
Product # :
PRO-2778Price :
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Shipped with Ice Packs
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Description
EPYC Human Recombinant produced in HEK293 Cells.is a single, glycosylated polypeptide chain containing 309 amino acids (20-322 a.a.) and having a molecular mass of 35.5kDa. EPYC is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
EPYC protein solution (0.5mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
>60% and is measured by the ability of the immobilized protein to support the adhesion of Saos‑2 human osteosarcoma cells. When cells are added to human DSPG3 1.25 ug/ml and human fibronectin 0.5 ug/ml coated plates.
More Info
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Synonyms
Epiphycan, SLRR3B, DSPG3, EPYC Dermatan sulfate proteoglycan 3, Proteoglycan-Lb, PG-Lb, Small chondroitin/dermatan sulfate proteoglycan, PGLB, epiphycan proteoglycan.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
APTLESINYD SETYDATLED LDNLYNYENI PVDKVEIEIA TVMPSGNREL LTPPPQPEKA QEEEEEEEST PRLIDGSSPQ EPEFTGVLGP HTNEDFPTCL LCTCISTTVY CDDHELDAIP PLPKNTAYFY SRFNRIKKIN KNDFASLSDL KRIDLTSNLI SEIDEDAFRK LPQLRELVLR DNKIRQLPEL PTTLTFIDIS NNRLGRKGIK QEAFKDMYDL HHLYLTDNNL DHIPLPLPEN LRALHLQNNN ILEMHEDTFC NVKNLTYIRK ALEDIRLDGN PINLSKTPQA YMCLPRLPVG SLVHHHHHH.
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Background
Epiphycan, a small leucine-rich proteoglycan, has gained recognition as a crucial player in tissue development, repair, and homeostasis. This research aims to explore the significance of epiphycan and its potential therapeutic applications in various physiological and pathological contexts. By investigating the properties and functions of epiphycan, we can uncover new insights into its role in tissue biology and its potential as a target for therapeutic interventions.
Epiphycan is a proteoglycan primarily expressed in skeletal tissues, such as the growth plate of long bones, articular cartilage, and intervertebral discs. It is an extracellular matrix component that interacts with various growth factors, cytokines, and other matrix proteins, influencing cell behavior and tissue organization. The unique structure of epiphycan, comprising a core protein and attached glycosaminoglycan chains, endows it with diverse regulatory functions.
The involvement of epiphycan in tissue development and repair has been highlighted in several studies. It plays a critical role in chondrogenesis, modulating the differentiation and proliferation of chondrocytes. Furthermore, epiphycan has been implicated in the maintenance of articular cartilage integrity and the prevention of osteoarthritis progression. Its ability to interact with growth factors, such as transforming growth factor-beta (TGF-β) and bone morphogenetic proteins (BMPs), suggests its potential as a modulator of tissue regeneration and repair.
This research will delve into the molecular mechanisms underlying epiphycan's functions and its interactions with various signaling pathways. The paper will explore the regulatory effects of epiphycan on cell behavior, matrix remodeling, and tissue architecture. Additionally, it will examine the implications of epiphycan dysregulation in pathological conditions, such as osteoarthritis, and discuss its potential as a therapeutic target for promoting tissue regeneration and repair.
The study will also investigate the diagnostic and prognostic value of epiphycan in various diseases and conditions. Understanding the expression patterns and alterations of epiphycan in different tissues and disease states may provide valuable insights into disease progression and aid in the development of personalized treatment strategies.
By unraveling the multifaceted roles of epiphycan in tissue biology and its potential therapeutic applications, this research aims to contribute to our understanding of tissue development and repair mechanisms. Furthermore, it highlights the potential of epiphycan as a target for therapeutic interventions and emphasizes the importance of further investigations to harness its full therapeutic potential.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SYT4 HumanDescription:
Synaptotagmin IV Human Recombinant
HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.
Product # :
PRO-1375Price :
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Description
SYT4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (38-425a.a) and having a molecular mass of 46.1kDa. SYT4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Synaptotagmin-4 (SYT4) is a part of the synaptotagmin proteins family. Synaptotagmins are a large gene family of synaptic vesicle type III integral membrane proteins that operate as regulators of both exocytosis and endocytosis and are involved in neurotransmitter secretion from small secretory vesicles. SYT4 is expressed in neuronal tissues, and has the highest mRNA levels in the hippocampus. The proximity of the SYT4 gene to markers of several psychiatric disorders implies an involvement of SYT4 in human disease such as pheochromocytoma, and parkinson's disease.
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Synonyms
HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCQRKSSKSN KTPPYKFVHV LKGVDIYPEN LNSKKKFGAD DKNEVKNKPA VPKNSLHLDL EKRDLNGNFP KTNLKPGSPS DLENATPKLF LEGEKESVSP ESLKSSTSLT SEEKQEKLGT LFFSLEYNFE RKAFVVNIKE ARGLPAMDEQ SMTSDPYIKM TILPEKKHKV KTRVLRKTLD PAFDETFTFY GIPYTQIQEL ALHFTILSFD RFSRDDIIGE VLIPLSGIEL SEGKMLMNRE IIKRNVRKSS GRGELLISLC YQSTTNTLTV VVLKARHLPK SDVSGLSDPY VKVNLYHAKK RISKKKTHVK KCTPNAVFNE LFVFDIPCEG LEDISVEFLV LDSERGSRNE VIGQLVLGAA AEGTGGEHWK EICDYPRRQI AKWHVLCDG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LCN2 RatDescription:
Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Rat Recombinant
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
Product # :
ENZ-920Price :
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Description
LCN2 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 201 amino acids (21-198 a.a) and having a molecular mass of 22.9kDa. LCN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCN2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core. They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.
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Synonyms
Neutrophil gelatinase-associated lipocalin, NGAL, Alpha-2-microglobulin-related protein, Alpha-2U globulin-related protein, Lipocalin-2, Siderocalin LCN2, p25.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQDSTQNL IPAPPLISVP LQPGFWTERF QGRWFVVGLA ANAVQKERQS RFTMYSTIYE LQEDNSYNVT SILVRGQGCR YWIRTFVPSS RPGQFTLGNI HSYPQIQSYD VQVADTDYDQ FAMVFFQKTS ENKQYFKVTL YGRTKGLSDE LKERFVSFAK SLGLKDNNIV FSVPTDQCID N.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LCP2 HumanDescription:
Lymphocyte Cytosolic Protein 2 Human Recombinant
Lymphocyte Cytosolic Protein 2, SH2 Domain-Containing Leukocyte Protein Of 76 KDa, 76 KDa Tyrosine Phosphoprotein, SLP-76 Tyrosine Phosphoprotein, SLP76, Lymphocyte Cytosolic Protein 2 (SH2 Domain Containing Leukocyte Protein Of 76kDa), Lymphocyte Cytosolic Protein 2 (SH2 Domain-Containing Leukocyte Protein Of 76kD), SH2 Domain-Containing Leukocyte Protein Of 76Kd, SLP-76, LCP2.
Product # :
PRO-2500Price :
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Description
LCP2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (1-533 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 542 amino acids and having a molecular mass of 61.2kDa.LCP2 is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LCP2 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
LCP2 (lymphocyte cytosolic protein 2) is an intracellular docking protein with a single SH2 recognition domain. LCP2 is implicated in T-cell antigen receptor mediated signaling. Moreover, LCP2 is phosphorylated by ZAP70 which leads to NF-AT as well as IL2 gene activation. B Cell Linker Protein Deficiency is one of the associated diseases with LCP2.
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Synonyms
Lymphocyte Cytosolic Protein 2, SH2 Domain-Containing Leukocyte Protein Of 76 KDa, 76 KDa Tyrosine Phosphoprotein, SLP-76 Tyrosine Phosphoprotein, SLP76, Lymphocyte Cytosolic Protein 2 (SH2 Domain Containing Leukocyte Protein Of 76kDa), Lymphocyte Cytosolic Protein 2 (SH2 Domain-Containing Leukocyte Protein Of 76kD), SH2 Domain-Containing Leukocyte Protein Of 76Kd, SLP-76, LCP2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPMALRNVP FRSEVLGWDP DSLADYFKKL NYKDCEKAVK KYHIDGARFL NLTENDIQKF PKLRVPILSK LSQEINKNEE RRSIFTRKPQ VPRFPEETES HEEDNGGWSS FEEDDYESPN DDQDGEDDGD YESPNEEEEA PVEDDADYEP PPSNDEEALQ NSILPAKPFP NSNSMYIDRP PSGKTPQQPP VPPQRPMAAL PPPPAGRNHS PLPPPQTNHE EPSRSRNHKT AKLPAPSIDR STKPPLDRSL APFDREPFTL GKKPPFSDKP SIPAGRSLGE HLPKIQKPPL PPTTERHERS SPLPGKKPPV PKHGWGPDRR ENDEDDVHQR PLPQPALLPM SSNTFPSRST KPSPMNPLPS SHMPGAFSES NSSFPQSASL PPYFSQGPSN RPPIRAEGRN FPLPLPNKPR PPSPAEEENS LNEEWYVSYI TRPEAEAALR KINQDGTFLV RDSSKKTTTN PYVLMVLYKD KVYNIQIRYQ KESQVYLLGT GLRGKEDFLS VSDIIDYFRK MPLLLIDGKN RGSRYQCTLT HAAGYPHHHH HH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GSTP2 Mouse, HisDescription:
Glutathione S-Transferase pi 2 Mouse Recombinant, His Tag
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
Product # :
ENZ-928Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a) and having a molecular mass of 25.9kDa. GSTP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GSTP2 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in theprotection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer ofthe dentate gyrus, which at the end leads to structural and functional damage.
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Synonyms
Glutathione S-transferase P 2 (EC:2.5.1.18), Gst P2, GST YF-YF, GST class-pi, GST-piA, Gstp2, Gstpia.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPPYTIV YFPSPGRCEA MRMLLADQGQ SWKEEVVTID TWMQGLLKPT CLYGQLPKFE DGDLTLYQSN AILRHLGRSL GLYGKNQREA AQVDMVNDGV EDLRGKYGTM IYRNYENGKN DYVKALPGHL KPFETLLSQN QGGKAFIVGD QISFADYNLL DLLLIHQVLA PGCLDNFPLL SAYVARLSAR PKIKAFLSSP EHVNRPINGN GKQ.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ZMAT3 HumanDescription:
Zinc Finger, Matrin-Type 3 Human Recombinant
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
Product # :
PRO-1635Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ZMAT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 312 amino acids (1-289) and having a molecular mass of 34.4kDa.ZMAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ZMAT3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
ZMAT3 is a protein with a nuclear localization signal and 3 zinc finger domains. The mRNA and the protein of this gene are upregulated by wildtype p53. When overexpressed, ZMAT3 can produce tumor cell growth, indicating that ZMAT3 takes part in the p53-dependent growth regulatory pathway. Alternative splicing of ZMAT3 produce two transcript variants encoding two isoforms differing in only one amino acid.
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Synonyms
Zinc Finger Matrin-Type 3, Zinc Finger Protein WIG1, P53-Activated Gene 608 Protein, P53 Target Zinc Finger Protein, WIG1.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMILLQHA VLPPPKQPSP SPPMSVATRS TGTLQLPPQK PFGQEASLPL AGEEELSKGG EQDCALEELC KPLYCKLCNV TLNSAQQAQA HYQGKNHGKK LRNYYAANSC PPPARMSNVV EPAATPVVPV PPQMGSFKPG GRVILATEND YCKLCDASFS SPAVAQAHYQ GKNHAKRLRL AEAQSNSFSE SSELGQRRAR KEGNEFKMMP NRRNMYTVQN NSAGPYFNPR SRQRIPRDLA MCVTPSGQFY CSMCNVGAGE EMEFRQHLES KQHKSKVSEQ RYRNEMENLG YV
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PDIA3 MouseDescription:
Protein Disulfide Isomerase A3 Mouse Recombinant
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Product # :
ENZ-1051Price :
Quantity :
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Shipped with Ice Packs
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Description
PDIA3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 505 amino acids (25-505 a.a) and having a molecular mass of 56.8kDa. PDIA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDIA3 protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1M NaCl and 10% glycerol .
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >15 A650/cm/min/mg,obtained by measuring the increase of insulin precipitation in absorbance at 650nm resulting from the reduction of insulin.
More Info
-
Introduction
PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
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Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
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Physical Appearance
Sterile filtered colourless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSDVLEL TDENFESRVS DTGSAGLMLV EFFAPWCGHC KRLAPEYEAA ATRLKGIVPL AKVDCTANTN TCNKYGVSGY PTLKIFRDGE EAGAYDGPRT ADGIVSHLKK QAGPASVPLR TEEEFKKFIS DKDASVVGFF RDLFSDGHSE FLKAASNLRD NYRFAHTNIE SLVKEYDDNG EGITIFRPLH LANKFEDKTV AYTEKKMTSG KIKKFIQDSI FGLCPHMTED NKDLIQGKDL LTAYYDVDYE KNAKGSNYWR NRVMMVAKKF LDAGHKLNFA VASRKTFSHE LSDFGLESTT GEVPVVAIRT AKGEKFVMQE EFSRDGKALE QFLQEYFDGN LKRYLKSEPI PESNEGPVKV VVAENFDDIV NEEDKDVLIE FYAPWCGHCK NLEPKYKELG EKLSKDPNIV IAKMDATAND VPSPYEVKGF PTIYFSPANK KLTPKKYEGG RELNDFISYL QREATNPPII QEEKPKKKKK AQEDL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VPS29 HumanDescription:
Vacuolar Protein Sorting 29 Human Recombinant
Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.
Product # :
PRO-1075Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
VPS29 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-182) and having a molecular mass of 23.2kDa.VPS29 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The VPS29 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
VPS29 is a member of a group of genes coding for vacuolar protein sorting (VPS) proteins which, when functionally damaged, lessens the efficient transfer of vacuolar hydrolases. VPS29 is a late Golgi transmembrane protein that operates as the sorting receptor for soluble vacuolar hydrolases, from the prevacuolar endosome back to the Golgi. Moreover, VPS29 takes part in the creation of the inner shell of the retromer coat for retrograde vesicles parting the prevacuolar compartment.
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Synonyms
Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMMLVLV LGDLHIPHRC NSLPAKFKKL LVPGKIQHIL CTGNLCTKES YDYLKTLAGD VHIVRGDFDE NLNYPEQKVV TVGQFKIGLI HGHQVIPWGD MASLALLQRQ FDVDILISGH THKFEAFEHE NKFYINPGSA TGAYNALETN IIPSFVLMDI QASTVVTYVY QLIGDDVKVE RIEYKKP
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ALPP HumanDescription:
Alkaline Phosphatase Placental Human Recombinant
ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-333Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Placental Alkaline Phosphatase Human Recombinant encoding 154-287 amino acids expressed in E.coli, shows a 41kDa band on SDS-PAGE (including GST tag).PLAP Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PLAP in 50mM Tris-Acetate, pH7.5, 1mM EDTA and 20% Glycerol.
More Info
-
Introduction
Placental alkaline phosphatase (PLAP) is a membrane-associated siaglycoprotein enzyme normally present at high concentration in syncytiotrophoblasts within the placenta during the third trimester of gestation. The expression of PLAP was originally thought to be restricted to term placenta but a human PLAP-like variant has been described which shares more than 85% homology with PLAP itself. PLAP is expressed only in normal term placenta, endocervix and fallopian tube and also in ovarian and proximal gastrointestinal tumors. It is also commonly expressed in germ cell tumors and more recently described in seminomas.
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Synonyms
ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
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Physical Appearance
Sterile filtered liquid.
-
Stability
Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Dnak SBD C-terminus E.ColiDescription:
Dnak Substrate Binding Domain C-terminal E.Coli Recombinant
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
Product # :
HSP-009Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Dnak Substrate Binding Domain C-terminal produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids and having a molecular mass of 27.7 kDa.
Source
Escherichia Coli.
Formulation
The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
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Synonyms
HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQGERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKTAIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SPA, HisDescription:
Staphylococcal Protein-A Recombinant, His Tag
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1925Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SPA Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with 6×His tag at C-terminus. SPA is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 306 amino acids and having a molecular mass of 34.7kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by:
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
JAM2 antibodyDescription:
Mouse Anti Human Junctional Adhesion Molecule 2
Junctional adhesion molecule B, JAM-B, Junctional adhesion molecule 2, JAM-2, Vascular endothelial junction-associated molecule, VE-JAM, CD322.
Product # :
ANT-738Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily, and the junctional adhesion molecule (JAM) family. JAM2 is a type I membrane protein which is localized at the tight junctions of both epithelial and endothelial cells. JAM2 functions as an adhesive ligand for interacting with various immune cell types, and may have a role in lymphocyte homing to secondary lymphoid organs.
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Synonyms
Junctional adhesion molecule B, JAM-B, Junctional adhesion molecule 2, JAM-2, Vascular endothelial junction-associated molecule, VE-JAM, CD322.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human JAM2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human JAM2 protein 21-238 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT21D7AT.
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Applications
JAM2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
JAM2 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
KRT5 AntibodyDescription:
Cytokeratin 5, Mouse Anti Human
Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.
Product # :
ANT-588Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
Cytokeratin 5 (KRT5) belongs to the keratin gene family. The type II cytokeratins are comprised of basic or neutral proteins which are arranged in pairs of heterotypic keratin chains coexpressed throughout differentiation of simple and stratified epithelial tissues. The type II cytokeratins are clustered in a region of chromosome 12q12-q13. The KRT5 type II cytokeratin is specifically expressed in the basal layer of the epidermis with family member KRT14. Mutations in these genes are linked with a complex of diseases termed epidermolysis bullosa simplex.
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Synonyms
Keratin 5, KRT5, EBS2, Epidermolysis Bullosa Simplex 2 Dowling-Meara/Kobner/Weber-Cockayne Types, Keratin 5 (Epidermolysis Bullosa Simplex,Dowling-Meara/Kobner/Weber-Cockayne Types), 58 KDa Cytokeratin, Type-II Keratin Kb5, CK-5, K5, DDD1, CK5, DDD, KRT5A, cytokeratin-5, Keratin, Type II Cytoskeletal 5, Cytokeratin-5, Keratin-5.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human KRT5 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human KRT5 protein 1-590 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT12C4AT.
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Applications
KRT5 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
KRT5 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
p53 HumanDescription:
p53 Protein Human Recombinant
Cellular tumor antigen p53, Tumor suppressor p53, Phosphoprotein p53, Antigen NY-CO-13, TP53, P53, LFS1, TRP53, FLJ92943.
Product # :
PRO-742Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
p53 Human Recombinant full length produced in E.Coli is a non-glycosylated, polypeptide chain having a total Mw of 81kDa. p53 Human Recombinant is fused to GST tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Purified human p53 in 50mM Tris-HCl, pH-7.5 and 10mM L-glutathione (reduced).
More Info
-
Introduction
Tumor protein p53 responds to various cellular stresses by regulating target genes that induce cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. p53 is a tumor suppressor gene expressed in a wide variety of tissue types and is involved in regulating cell growth, replication, and apoptosis. p53 is a DNA-binding protein containing transcription activation, DNA-binding & oligomerization domains.
p53 binds to mdm2, SV40 T antigen and human papilloma virus E6 protein p53 senses DNA damage and possibly facilitating repair. p53 protein is a transcription factor which is encoded in humans by the TP53 gene. Alterations of TP53 occur not only as somatic mutations in human malignancies, but also as germline mutations in some cancer-prone families with Li-Fraumeni syndrome. p53 mutants that often occur in many different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Mutation involving p53 is found in a wide variety of malignant tumors, including breast, ovarian, bladder, colon, lung, and melanoma. The p53 expression in normal cells is low and in an assortment of transformed cell lines is high, which may contribute to transformation and malignancy. Multiple p53 variants encode distinct isoforms, which can regulate p53 transcriptional activity. p53’s significance in multicellular organisms is in cell cycle regulation therefore it functions as a tumor suppressor that is involved in preventing cancer. p53’s role in conserving stability by preventing genome mutation has earned it descriptions such as "the guardian of the genome," "the guardian angel gene," and the "master watchman.” The name p53 refers to its evident molecular mass: it migrates as a 53kDa protein on SDS-PAGE. However, based on calculations from its amino acid residues, p53's mass is in fact only 43.7kDa. This difference is attributed to the high number of proline residues in the protein which slow its migration on SDS-PAGE, consequently making it appear larger than it actually is. -
Synonyms
Cellular tumor antigen p53, Tumor suppressor p53, Phosphoprotein p53, Antigen NY-CO-13, TP53, P53, LFS1, TRP53, FLJ92943.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
For long term storage store at -20°C. Avoid freeze/thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
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Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
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Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Toxoplasma P35Description:
Toxoplasma Gondii P35 (GRA8) Recombinant
Dense granule protein GRA8, GRA8, TGME49_254720
Product # :
TOX-269Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Toxoplasma Gondii P35 (GRA8) containing 217 amino acids was purified from E. coli.The Recombinant Toxoplasma Gondii P35 (GRA8) is fused to GST tag at its N terminal and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
Toxoplasma P35 solution contains 0.5mM EDTA, Phosphate buffered saline, pH 7.4.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
The life cycle of Toxoplasma gondii has 2 phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals (including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection. Recombinant Toxoplasma Gondii P35 (GRA8)) is an antigen used to test the specific Toxoplasma gondii antibody for the diagnosis of Toxoplasma gondii infection.
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Synonyms
Dense granule protein GRA8, GRA8, TGME49_254720
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Applications
Immunoassay.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CITED2 (1-160) HumanDescription:
Cbp/p300-Interacting Transactivator 2 (1-160) Human Recombinant
MRG1, P35SRJ, CIT-ED2, MSG-related protein 1, MRG-1, CITED2.
Product # :
PRO-2825Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- description
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Description
The CITED2 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CITED2 His-Tagged Fusion Protein, produced in E. coli, is a 26kDa protein containing 160 amino acid residues of the CITED2 Human, 1-160 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
MRG1, P35SRJ, CIT-ED2, MSG-related protein 1, MRG-1, CITED2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized CITED2 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
CITED2 also known as Cbp/p300-Interacting Trans activator 2 is an important transcriptional cofactor which is involved in multiple organ development. CITED2 is part of the CITED family which take an important role in gene regulation & cellular signalling.
CITED2 is a cAMP-responsive element-binding protein interacting transcriptional modulator and an anticipated negative regulator for Recombinant human CITED2 protein 1 hypoxia-inducible factor (HIF) -1alpha by competing on the binding with HIF-1alpha to CBP/p300.
CITED2 is essential for Mouse Fetal liver haematopoiesis and also mandatory for the appropriate formation of the hyaloid vasculature and for lens morphogenesis as well.
CITED2 is recognized for its relations with transcriptional coactivators, such as CBP and p300 and also takes part in various biological processes, together with cardiovascular development, metabolism, as well as response to hypoxia.
Moreover, the most valuable form of CITED2 for learning its functional roles & potential applications in cancer research and regenerative medicine is the Recombinant one which is produced by molecular cloning and expression systems.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HCV NS3, BiotinDescription:
Hepatitis C Virus NS3, Biotin Recombinant
Product # :
HCV-244Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.coli derived recombinant Biotin Labeled protein contains the HCV NS3 immunodominant regions, a.a. 1450-1643, 22 kDa. The Biotin labeled protein is fused with a 6xHis-Tag at N-terminus.
Formulation
(1mg/ml) 1.5M urea, 20mM Tris-HCl pH 8.0 and 10mM β-mercaptoethanol.
Purity
HCV NS3 Biotin labeled protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6). -
Stability
HCV NS3 Biotin although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
HCV NS3 Biotin labeled antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.
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Specificity
Reactivity with human HCV positive serum undetermined.
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Purification Method
HCV NS3 Biotin labeled protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Leptin qA Rat, PEGDescription:
Leptin Quadruple Antagonist, Pegylated Rat Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-1241Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leptin Pegylated Quadruple Antagonist Rat Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids. The Rat Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Rat Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The Rat Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.
Biological Activity
Rat Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro.
More Info
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Rat Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of rat pegylated leptin antagonist and filter sterilization rat pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Rat Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.
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Background
Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.