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1000 results found for “beta lactamase”
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Name :
DsbA E.ColiDescription:
Disulfide Oxidoreductase E.Coli Recombinant
Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.
Product # :
ENZ-1143Price :
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Description
DsbA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (20-208) and having a molecular mass of 21.2 kDa. DsbA E.Coli is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DsbA E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 7.5) and 2mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Disulfide Oxidoreductase or DsbA is a protein, found in the plasma. It is part of the thioredoxin protein family. The protein creates disulfide bonds in the target proteins by contributing disulfide bond from its Cys30-Pro31-His32-Cys33 active site to a couple of cysteine residues.
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Synonyms
Disulfide oxidoreductase A, dsbA, rpbB, Disulfide oxidoreductase (DsbA) E Coli, DsDNA-binding protein A, Doublestranded DNA-binding protein, Disulfide oxidoreductase A periplasmic protein disulfide isomerase I, Thiol disulfide interchange protein dsbA.
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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
MAQYEDGKQY TTLEKPVAGA PQVLEFFSFF CPHCYQFEEV LHISDNVKKK LPEGVKMTKY HVNFMGGDLG KDLTQAWAVA MALGVEDKVT VPLFEGVQKT QTIRSASDIR DVFINAGIKG EEYDAAWNSF VVKSLVAQQE KAAADVQLRG VPAMFVNGKY QLNPQGMDTS NMDVFVQQYA DTVKYLSEKK.
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 :
C3b MouseDescription:
Complement C3b Mouse
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Product # :
PRO-2707Price :
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Description
Mouse Complement C3b produced in Mouse plasma having a molecular weight of 175kDa.
Source
Mouse Plasma.
Formulation
C3b solution contains Phosphate buffered saline, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
C3b is derived from native C3 upon cleavage with the alternative pathway C3 convertase and release of C3a. C3b is essential to the function of all 3complement pathways. Initiation of each pathway generates proteolytic enzyme complexes (C3 convertases) which binds the target surface. These enzymes cleave a peptide bond in C3 releasing the anaphylatoxin C3a and activating C3b. Most of the C3b created during complement activation. Surface-bound C3b is needed in all 3 pathways for effective activation of C5 and formation of C5b-9 complexes which lyse the target cell membrane. Surface-bound C3b and its breakdown products iC3b and C3d are identifyid by various receptors on lymphoid and phagocytic cells which use the C3b ligand to stimulate antigen presentation to cells of the adaptive immune system. It results in an expansion of target-specific B-cell and T-cell populations.
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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
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Physical Appearance
Sterile filtered solution.
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Stability
C3b Mouse is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
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 :
HBV core (1-186)Description:
Hepatitis B Virus Core (1-186 a.a.) Recombinant
Product # :
HBV-232Price :
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Description
The E.coli derived recombinant protein contains the HBV core immunodominant region amino acids 1-186, and fused to a His tag at N- terminus.
Formulation
25mM Tris-HCl pH-8.0, 1.5mM EDTA, 1.5mM Urea and 50% glycerol.
Purity
HBV Core protein is >90% pure as determined by 10% PAGE (Coomassie staining).
Citations
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Introduction
Hepatitis B is one of a few known non-retroviralviruses which employ reverse transcriptionas a part of its replication process. (HIV, a completely unrelated virus, also uses reverse transcription, but it is a retrovirus.) HBV invades the cell by binding to surface receptor and become internalized. The viral core particles then migrate to the hepatocyte nucleus and the partially double-stranded, relaxed circular genomes (RC-DNA) are repaired to form a covalently closed circular DNA (cccDNA), which is the template for viral genomic and sub-genomic RNAs by cellular RNA polymerase II. Of these, the pregenomic RNA(pgRNA is selectively packaged into progeny capsids and is then reverse-transcribed into new RC-DNA. The core can either bud into the endoplasmic reticulum to be enveloped or exported from the cell or recycled back into the genome for conversion to cccDNA.
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Stability
HBV Core protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Immunoreactive with sera HBV-infected individuals.
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Purification Method
HBV Core 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.
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Name :
CBFB HUmanDescription:
Core Binding Factor Beta Human Recombinant
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
Product # :
PRO-534Price :
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Description
CBFB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 182 amino acids (1-202 a.a.) and having a molecular mass of 23.6 kDa. The CBFB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
0.5mg/ml solution containing 20mM MES pH-6, 0.1mM PMSF & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CBFB beta subunit is a heterodimeric core-binding transcription factor that is part of the PEBP2/CBF transcription factor family which controls a host of genes particulary to hematopoiesis and osteogenesis. CBFB is a non-DNA binding regulatory subunit which increases DNA binding by alpha subunit.
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Synonyms
PEBP2B, polyomavirus enhancer binding protein b, PEA2, CBF-beta.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
CBFB Human although stable at 4C for 1 week, should be stored below -18C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRVVPDQRS KFENEEFFRK LSRECEIKYT GFRDRPHEER QARFQNACRD GRSEIAFVAT GTNLSLQFFP
ASWQGEQRQT PSREYVDLER EAGKVYLKAP MILNGVCVIW KGWIDLQRLD GMGCLEFDEE RAQQEDALAQ QAFEEARRRT REFEDRDRSH
REEMEVRVSQ LLAVTGKKTT RP.
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 :
GLO1 MouseDescription:
Glyoxalase-I Mouse Recombinant
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
Product # :
ENZ-953Price :
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Description
GLO1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 192 amino acids (1-184a.a.) and having a molecular mass of 21.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GLO1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GLO1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 210 units/mg, and is defined as the amount of enzyme that will form 1.0 µmol of S-lactoylglutathione from methylglyoxal and reduced glutathione per minute at pH 6.5 at 25C.Citations
More Info
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Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
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Synonyms
Lactoylglutathione lyase, Aldoketomutase, Glyoxalase I, Glx I, Ketone-aldehyde mutase, Methylglyoxalase, S-D-lactoylglutathione methylglyoxal lyase.
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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
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI ATIILEHHHH 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 :
OCM HumanDescription:
Oncomodulin-1 Human Recombinant
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
Product # :
PRO-143Price :
Quantity :
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Shipped at Room temp
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Description
The Recombinant Human Oncomodulin-1 produced in E.coli has a molecular mass of 13.21kDa containing 117 amino acid residues of the human Oncomodulin-1 and fused to a 9 a.a. His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Oncomodulin-1 was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.
Citations
More Info
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Introduction
Oncomodulin is a member of the superfamily of calmodulin proteins, otherwise known as the EF-hand proteins. It is a high-affinity calcium ion-binding protein. Oncomodulin is an oncodevelopmental protein which is found in early embryonic cells in the placenta and also in tumors.
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Synonyms
Oncomodulin-1, OM, Parvalbumin beta, OCM, OCM1, OCMN.
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Stability
Store lyophilized protein 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS ITDVLSADDI S ITDVLSADDI AAALQECRDP DTFEPQKFFQ TSGLSKMSAN QVKDVFRFID NDQSGYLDEE ELKFFLQKFE SGARELTESE TKSLMAAADN DGDGKIGAEE FQEMVHS.
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Applications
Western blotting.
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 :
M.Pneumoniae P116Description:
Mycoplasma Pneumoniae P116 Recombinant
Product # :
PRO-513Price :
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Description
The Recombinant Mycoplasma Pneumoniae P116 was expressed in E. coli having an Mw of 116 kDa. P116 is fused to a His-Tag.
Source
E.Coli
Formulation
Mycoplasma Pneumoniae P116 is formulated in 1xPBS, pH 7.4 and 25mM arginine.
Purity
Greater than 95% as determined by 10% PAGE (Coomassie staining).
Citations
More Info
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Introduction
Mycoplasma pneumonia is part of the atypical pneumonia subtype which is caused by the bacteria M. pneumoniae. Mycoplasma pneumonia affects individuals younger than 40. It makes up 15 - 50% of all pneumonia cases in adults and especially in school-aged children. People at great risk for mycoplasma pneumonia comprise of those living or working in busy areas such as schools and homeless shelters, although many people who contract mycoplasma pneumonia have no identifiable risk factor. P1, P30, and P116 of mycoplasma pneumonia membrane proteins have been recognized as adhensive factors, P1 is considered as a main adhension protein of the organism colonization.
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Physical Appearance
Streile filtered colorless solution.
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Stability
Upon arrival, Store at -20°C.Please prevent freeze-thaw cycles.
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Applications
Immunoassay.
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Purification Method
The recombinant fusion protein was purified by GSH affinity chromatography 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.
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Name :
RNASEH1 E.ColiDescription:
Ribonuclease H1 E.Coli Recombinant
Ribonuclease HI, RNase HI, Ribonuclease H, RNase H, rnhA, dasF, herA, rnh, sdrA, b0214, JW0204.
Product # :
ENZ-164Price :
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Shipped with Ice Packs
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Description
RNASEH1 E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-155 a.a.) and having a molecular mass of 20kDa.RNASEH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RNASEH1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
RNHA is an endonuclease which specifically degrades the RNA of RNA-DNA hybrids. Localized to the nucleus, the RNHA protein mediates the removal of Okazaki fragment RNA primers which are present on the lagging strand during DNA replication. RNHA catalyzes the endonucleolytic cleavage of RNA to a 5'-phosphomonoester and is capable of binding magnesium or manganese as cofactors.
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Synonyms
Ribonuclease HI, RNase HI, Ribonuclease H, RNase H, rnhA, dasF, herA, rnh, sdrA, b0214, JW0204.
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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
MGSSHHHHHH SSGLVPRGSH MGSMLKQVEI FTDGSCLGNP GPGGYGAILR YRGREKTFSA GYTRTTNNRM ELMAAIVALE ALKEHCEVIL STDSQYVRQG ITQWIHNWKK RGWKTADKKP VKNVDLWQRL DAALGQHQIK WEWVKGHAGH PENERCDELA RAAAMNPTLE DTGYQVEV.
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 :
PPP3R2 HumanDescription:
Protein Phosphatase 3 Regulatory subunit, Beta Isozyme Human Recombinant
Calcineurin subunit B type 2, Calcineurin B-like protein, CBLP, Calcineurin BII, CNBII, PPP3R1-like, Protein phosphatase 2B regulatory subunit 2, Protein phosphatase 3 regulatory subunit B beta isoform, PPP3R2, PPP3RL.
Product # :
ENZ-103Price :
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Description
PPP3R2 Human Recombinant fused with a 20 a.a. His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a. 1-173) containing 193 amino acids and having a molecular mass of 22kDa.The PPP3R2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PPP3R2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
PPP3R2 is a calcium-dependent, calmodulin stimulated serine/threonine protein phosphatase. In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is a crucial means of regulating a wide range of cellular functions including division, homeostasis and apoptosis. Ordinarily the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit.
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Synonyms
Calcineurin subunit B type 2, Calcineurin B-like protein, CBLP, Calcineurin BII, CNBII, PPP3R1-like, Protein phosphatase 2B regulatory subunit 2, Protein phosphatase 3 regulatory subunit B beta isoform, PPP3R2, PPP3RL.
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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 MSTMGNEASY PAEMCSHFDN DEIKRLGRRF KKLDLDKSGS LSVEEFMSLP ELRHNPLVRR VIDVFDTDGD GEVDFKEFIL GTSQFSVKGD EEQKLRFAFS IYDMDKDGYI SNGELFQVLK MMVGNNLTDW QLQQLVDKTI IILDKDGDGK ISFEEFSAVV RDLEIHKKLV LIV.
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 :
LA/SS-B HumanDescription:
LA / SS-B Human Recombinant
Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).
Product # :
PRO-327Price :
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Description
LA/SS-B Human Recombinant produced in SF9 is a single, glycosylated, polypeptide chain having a calculated molecular mass of 52 kDa, is fused to a hexahistidine purification tag.The LA/SS-B is purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
The protein solution contains 20mM HEPES, pH 7.5, 400mM NaCl, 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
The La protein is a 47 kDa polypeptide that frequently acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome patients. La is involved in various aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III - transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs linked to hepatitis C virus. It occurs in both the nucleus and the cytoplasm, where it assumes different roles. In the nucleus, La protein facilitates the production of tRNAs, acting as an RNA polymerase III (RNAP III) transcription factor by attaching to the U-rich 3'UTR of nascent transcripts, aiding in their folding and maturation. In the cytoplasm, La protein facilitates the translation of specific mRNAs, acting as a translation factor. As an RNA binding protein (RBP), La protein associates with subsets of mRNAs which contain a 5'-terminal oligopyrimidine (5'TOP) motif known to direct protein synthesis. The binding of La protein to particular classes of RNA molecules regulates their downstream processing, guards them from endonuclease digestion, and organizes their export from the nucleus. La/SS-B appears to be readily disposed to proteolysis, which results in many smaller (42kD, 320, and 270) nevertheless still immunoreactive polypeptides. La/SS-B antigen is strongly conserved across species. Anti-La/SS-B autoantibodies were originally found as precipitating autoantibodies in sera of Sjogren's Syndrome patients and referred to as SjT. Anti-La/SS-B precipitins are most frequently found in Sjogren's Syndrome, Systemic Lupus Erythematosus (SLE) and Subacute Cutaneous Lupus. Also, there seems to be a correlation between anti-La/SS-B and the absence of nephritis in SLE patients.
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Synonyms
Lupus La protein, Sjoegren syndrome type B antigen, SS-B, La ribonucleoprotein, La autoantigen, SSB, La, LARP3, LA/SS-B, La(SS-B).
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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. Avoid multiple 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.
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Name :
LECT2 HumanDescription:
Leukocyte Cell-Derived Chemotaxin 2 Human Recombinant
Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.
Product # :
PRO-2037Price :
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Shipped at Room temp
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Description
LECT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gly19-Leu151) containing 143 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16kDa.
Source
Escherichia Coli.
Formulation
LECT2 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl & pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Leukocyte Cell-Derived Chemotaxin 2 (LECT2) functions as a chemotactic factor to neutrophils. LECT2 stimulates the proliferation of chondrocytes and osteoblasts. LECT2 is strongly expressed in the liver and weakly in the testis. LECT2 is a secreted, 16kDa protein which serves as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. LECT2 protein has a high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in the LECT2 gene is linked with rheumatoid arthritis.
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Synonyms
Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein 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. LECT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASGPWANICAGK SSNEIRTCDR HGCGQYSAQR SQRPHQGVDI LCSAGSTVYA PFTGMIVGQE KPYQNKNAIN NGVRISGRGF CVKMFYIKPI KYKGPIKKGE KLGTLLPLQK VYPGIQSHVH IENCDSSDPT AYL.
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 :
AGA Human, sf9Description:
Aspartylglucosaminidase Human Recombinant, sf9
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
Product # :
ENZ-990Price :
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Description
AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.
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Synonyms
Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.
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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
ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH 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.
- View Data Sheet
Name :
Prolactin Human, HisDescription:
Prolactin Human Recombinant, His Tag
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-493Price :
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Description
Prolactin-His Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids fragment (29-227) and having a molecular mass of 23 kDa with an amino-terminal hexahistidine tag. The Prolactin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Prolactin His is supplied in 1x PBS and 50% glycerol.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
More Info
-
Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered clear 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. Please 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.
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Name :
INHBC HumanDescription:
Inhibin-Beta C Chain Human Recombinant
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
Product # :
HOR-010Price :
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Description
INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The INHBC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.
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Synonyms
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
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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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS
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 :
Tetanus antibodyDescription:
Tetanus toxoid scFv Recombinant antibody
Product # :
ANT-195Price :
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Description
Tetanus toxin is the neurotoxin produced by the vegetative spore of Clostridium tetani in anaerobic conditions, causing tetanus.Recombinant Anti Tetanus produced in E.Coli is a non-glycosylated, polypeptide chain containing a hexahistidine tag and having a molecular weight of 37 kDa.Tetanus Antibody is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Tetanus is supplied in 1x PBS (pH 7.4) and 0.09% azide
Purity
Greater than 95.0% as determined byAnalysis by RP-HPLC.
Analysis by SDS-PAGE.Citations
More Info
-
Physical Appearance
Sterile Filtered clear 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. Please avoid freeze thaw cycles.
-
Type
Antibody Recombinant.
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 :
GLUL Human, His ActiveDescription:
Glutamine Synthetase Human Recombinant, His Active
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
Product # :
ENZ-984Price :
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Description
GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,800 pmol/min/ug, and is defined as the amount of enzyme that convert 1.0 pmole of L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.Citations
More Info
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Introduction
GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.
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Synonyms
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
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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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.
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 :
CPA4 HumanDescription:
Carboxypeptidase A4 Human Recombinant
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
Product # :
ENZ-942Price :
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Description
CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CPA4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.
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Synonyms
Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.
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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.
-
Amino Acid Sequence
GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH 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 :
ABO HumanDescription:
ABO Blood Group Human Recombinant
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
Product # :
ENZ-167Price :
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Description
ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.
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Synonyms
Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.
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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 MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.
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 :
MMP9 RatDescription:
Matrix Metalloproteinase-9 Rat Recombinant
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
Product # :
ENZ-1185Price :
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Description
MMP9 Rat produced in HEK293 cells is a single, glycosylated polypeptide chain containing 695 amino acids (20-708 a.a.) and having a molecular mass of 77.2kDa. MMP9 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
MMP9 Rat protein solution (0.5mg/ml) contains 20mM Tris-HCl pH-7.5, 100mM NaCl , 1mM CaCl2 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
> 2000 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-7.5 at 25C.
Citations
More Info
-
Synonyms
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.
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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
APHQRQPTYV VFPRDLKTSN LTDTQLAEDY LYRYGYTRAA QMMGEKQSLR PALLMLQKQL SLPQTGELDS ETLKAIRSPR CGVPDVGKFQ TFEGDLKWHH HNITYWIQSY TEDLPRDVID DSFARAFAVW SAVTPLTFTR VYGLEADIVI QFGVAEHGDG YPFDGKDGLL AHAFPPGPGI QGDAHFDDDE LWSLGKGAVV PTYFGNANGA PCHFPFTFEG RSYLSCTTDG RNDGKPWCGT TADYDTDRKY GFCPSENLYT EHGNGDGKPC VFPFIFEGHS YSACTTKGRS DGYRWCATTA NYDQDKLYGF CPTRADVTVT GGNSAGEMCV FPFVFLGKQY STCTGEGRSD GRLWCATTSN FDADKKWGFC PDQGYSLFLV AAHEFGHALG LDHSSVPEAL MYPMYHYHED SPLHEDDIKG IQHLYGRGSK PDPRPPATTA AEPQPTAPPT MCPTAPPMAY PTGGPTVAPT GAPSPGPTGP PTAGPSEAPT ESSTPVDNPC NVDVFDAIAD IQGALHFFKD GRYWKFSNHG GSQLQGPFLI ARTWPALPAK LNSAFEDPQS KKIFFFSGRK MWVYTGQTVL GPRSLDKLGL GSEVTLVTGL LPRRGGKALL ISRERIWKFD LKSQKVDPQS VTRLDNEFSG VPWNSHNVFH YQDKAYFCHD KYFWRVSFHN RVNQVDHVAY VTYDLLQCPH HHHHH.
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Background
Matrix metalloproteinase-9 (MMP-9) is a key member of the matrix metalloproteinase family involved in the remodeling of the extracellular matrix (ECM). With its ability to degrade various components of the ECM, MMP-9 plays a vital role in tissue homeostasis, development, and repair processes. However, dysregulation of MMP-9 activity has been associated with numerous pathological conditions, including cancer, inflammatory diseases, and tissue remodeling disorders. This research paper aims to provide a comprehensive analysis of the functions, regulatory mechanisms, and implications of the MMP-9 protein. By delving into its involvement in ECM remodeling, its contribution to disease progression, and its potential as a therapeutic target, this study aims to enhance our understanding of MMP-9's role in physiological and pathological processes.
Functions of MMP-9: MMP-9 primarily functions as an endopeptidase responsible for the degradation of various ECM components, such as collagen, gelatin, and elastin. Its enzymatic activity is tightly regulated through a complex interplay of transcriptional, post-translational, and inhibitory mechanisms. Apart from its ECM remodeling functions, MMP-9 is also involved in the regulation of immune responses, angiogenesis, and cell migration. Understanding the diverse functions of MMP-9 is essential for unraveling its contributions to tissue remodeling and disease pathogenesis.
Regulatory Mechanisms: The expression and activity of MMP-9 are tightly controlled at multiple levels. Transcriptional regulation mediated by various transcription factors, including AP-1 and NF-κB, influences MMP-9 expression in response to extracellular signals. Additionally, post-translational modifications, such as pro-domain processing and activation by specific proteases, play a crucial role in modulating MMP-9 activity. Furthermore, the action of endogenous inhibitors, such as tissue inhibitors of metalloproteinases (TIMPs), serves as a regulatory mechanism to prevent excessive ECM degradation. Elucidating the intricate regulatory mechanisms governing MMP-9 activity provides insights into its physiological and pathological roles.
Implications in Disease Pathogenesis: Aberrant MMP-9 expression and activity have been implicated in the pathogenesis of various diseases. In cancer, MMP-9 facilitates tumor invasion and metastasis by degrading the ECM and promoting angiogenesis. Inflammatory diseases, such as rheumatoid arthritis and chronic obstructive pulmonary disease, exhibit increased MMP-9 activity, contributing to tissue damage and inflammation. Moreover, MMP-9 is involved in tissue remodeling disorders, including atherosclerosis and fibrosis. Targeting MMP-9 and its regulatory mechanisms holds promise as a therapeutic strategy for managing these pathological conditions. Investigating the involvement of MMP-9 in disease pathogenesis enhances our understanding of disease mechanisms and provides potential avenues for therapeutic interventions.
Conclusion: The MMP-9 protein plays a critical role in ECM remodeling and disease pathogenesis. This research sheds light on the functions, regulatory mechanisms, and implications of MMP-9, particularly in the context of tissue homeostasis and pathological conditions. Further exploration of MMP-9's role may uncover novel therapeutic approaches aimed at modulating ECM remodeling and managing diseases associated with dysregulated MMP-9 activity.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on MMP-9 for a comprehensive list of references and sources.
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 :
ALCAM (CD166) MouseDescription:
Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant
Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.
Product # :
PRO-2749Price :
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Description
ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.
Citations
More Info
-
Introduction
CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.
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Synonyms
Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.
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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
WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK 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 :
NAT1 HumanDescription:
N-Acetyltransferase 1 Human Recombinant
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
Product # :
ENZ-144Price :
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Description
NAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290) and having a molecular mass of 36.1 kDa.The NAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NAT1 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 10% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
NAT1 is a member of the arylamine N-acetyltransferase family. NAT1 catalyzes N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a large number of drugs. Several alleles triggering high levels of N-acetyltransferase activity were linked to colon and urinary bladder cancers, since NAT1 also bioactivate numerous known carcinogens. NAT1 aids metabolize drugs and other xenobiotics, and takes part in the detoxification of a plethora of hydrazine and arylamine drugs.
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Synonyms
N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.
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Physical Appearance
NAT1 is supplied as a sterile filtered clear 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.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCIF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI
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 :
NIT2 HumanDescription:
Nitrilase Family Member 2 Human Recombinant
Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.
Product # :
ENZ-039Price :
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Description
NIT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276a.a.) and having a molecular mass of 33kDa.NIT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NIT2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 0.1M NaCl, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NIT2 is a member of the nitrilase superfamily. NIT2 protein has an omega-amidase activity which removes potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. In addition, Nit2 is widely distributed in nature and is thought to be a tumor suppressor protein.
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Synonyms
Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSFRLA LIQLQISSIK SDNVTRACSF IREAATQGAK IVSLPECFNS PYGAKYFPEY AEKIPGESTQ KLSEVAKECS IYLIGGSIPE EDAGKLYNTC AVFGPDGTLL AKYRKIHLFD IDVPGKITFQ ESKTLSPGDS FSTFDTPYCR VGLGICYDMR FAELAQIYAQ RGCQLLVYPG AFNLTTGPAH WELLQRSRAV DNQVYVATAS PARDDKASYV AWGHSTVVNP WGEVLAKAGT EEAIVYSDID LKKLAEIRQQ IPVFRQKRSD LYAVEMKKP
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 :
CHI3L2 Human, Sf9Description:
Chitinase 3-Like 2 Human Recombinant, Sf9
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, Chitinase-3-like protein 2.
Product # :
ENZ-932Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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- Citations
Description
CHI3L2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 372 amino acids (27-390a.a.) and having a molecular mass of 41.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CHI3L2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CHI3L2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity, but not heparin.
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Synonyms
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, Chitinase-3-like protein 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
YKLVCYFTNW SQDRQEPGKF TPENIDPFLC SHLIYSFASI ENNKVIIKDK SEVMLYQTIN SLKTKNPKLK ILLSIGGYLF GSKGFHPMVD SSTSRLEFIN SIILFLRNHN FDGLDVSWIY PDQKENTHFT VLIHELAEAF QKDFTKSTKE RLLLTAGVSA GRQMIDNSYQ VEKLAKDLDF INLLSFDFHG SWEKPLITGH NSPLSKGWQD RGPSSYYNVE YAVGYWIHKG MPSEKVVMGI PTYGHSFTLA SAETTVGAPA SGPGAAGPIT ESSGFLAYYE ICQFLKGAKI TRLQDQQVPY AVKGNQWVGY DDVKSMETKV QFLKNLNLGG AMIWSIDMDD FTGKSCNQGP YPLVQAVKRS LGSLLEHHHH 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.
- View Data Sheet
Name :
LPL Human, HEKDescription:
Lipoprotein Lipase Human Recombinant, HEK
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
Product # :
ENZ-087Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
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Description
The Recombinant Human LPL produced in HEK293 cell line has a molecular mass of 51.8kDa containing 461 amino acid residues of the human LPL (Ala28-Gly475, variant Asn > Ser318) and fused to a 13 a.a. Flag-tag at N-terminus.
Source
HEK293 (Human Embryonic Kidney cell line).
Formulation
LPL was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.
Citations
More Info
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Introduction
LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.
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Synonyms
Lipoprotein lipase, LPL, LIPD, HDLCQ11.
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Physical Appearance
Filtered white lyophilized powder.
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Stability
Store lyophilized protein 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGADQRRDF IDIESKFALR TPEDTAEDTC HLIPGVAESV ATCHFNHSSK TFMVIHGWTV TGMYESWVPK ADQRRDF IDIESKFALR TPEDTAEDTC HLIPGVAESV ATCHFNHSSK TFMVIHGWTV TGMYESWVPK LVAALYKREP DSNVIVVDWL SRAQEHYPVS AGYTKLVGQD VARFINWMEE EFNYPLDNVH LLGYSLGAHA AGIAGSLTNK KVNRITGLDP AGPNFEYAEA PSRLSPDDAD FVDVLHTFTR GSPGRSIGIQ KPVGHVDIYP NGGTFQPGCN IGEAIRVIAE RGLGDVDQLV KCSHERSIHL FIDSLLNEEN PSKAYRCSSK EAFEKGLCLS CRKNRCNNLG YEISKVRAKR SSKMYLKTRS QMPYKVFHYQ VKIHFSGTES ETHTNQAFEI SLYGTVAESE NIPFTLPEVS TNKTYSFLIY TEVDIGELLM LKLKWKSDSY FSWSDWWSSP GFAIQKIRVK AGETQKKVIF CSREKVSHLQ KGKAPAVFVK CHDKSLNKKS G.
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.