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Name :
SEPX1 HumanDescription:
Selenoprotein X 1 Human Recombinant
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
Product # :
PRO-260Price :
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Shipped with Ice Packs
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Description
SEPX1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPX1 solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 7.5), 1mM DTT, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Methionine sulfoxide reductase B1 (SEPX1 or MSRB1), is a selenoprotein that contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that usually signals translation termination. SEPX1 is a member of the methionine sulfoxide reductase B (MsrB) family, and is expressed in an assortment of adult and fetal tissues. MSRs (Methionine sulfoxide reductases) catalyze the reduction of free and protein-bound methionine sulfoxides to corresponding methionines. The oxidation of methionine by ROS creates a diastereomeric mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). Two separate enzyme families evolved for reduction of these sulfoxides, with methionine-S-sulfoxide reductase (MsrA) being stereospecific for Met-S-SO and methionine-R-sulfoxide reductase (MsrB) for Met-R-SO.
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Synonyms
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344.
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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 MSFCSFFGGE VFQNHFEPGV YVCAKCGYEL FSSRSKYAHS SPWPAFTETI HADSVAKRPE HNRSEALKVS CGKCGNGLGH EFLNDGPKPG QSRFCIFSSS LKFVPKGKET SASQGH.
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 :
HNRNPAB HumanDescription:
Heterogeneous Nuclear Ribonucleoprotein A/B Human Recombinant
Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.
Product # :
PRO-1731Price :
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Description
HNRNPAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 33kDa.HNRNPAB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HNRNPAB protein solution (0.25mg/ml) containing 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Heterogeneous Nuclear Ribonucleoprotein A/B (HNRNPAB) is a member of the subfamily of ubiquitously expressed heterogeneous nuclearribonucleoproteins (hnRNPs). The hnRNPs are produced by RNA polymerase II and are components of theheterogeneous nuclear RNA (hnRNA) complexes. They are linked with pre-mRNAs in the nucleus and seem to influence pre-mRNA processing and further aspects of mRNA metabolism and transport. Whereas all of the hnRNPsare present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. HNRNPAB, which binds to one of the components of the multiproteineditosome complex, has two repeats of quasi-RRM (RNA recognition motif) domains that bind to RNAs. Among the diseases associated with HNRNPAB are wells syndrome, and cystic fibrosis.
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Synonyms
Heterogeneous Nuclear Ribonucleoprotein A/B, ABBP-1, ABBP1, APOBEC1-Binding Protein 1, HnRNP A/B, Apobec-1 Binding Protein 1, Apolipoprotein B MRNA Editing Enzyme, Catalytic Polypeptide 1-Binding Protein 1, HnRNP Type A/B Protein.
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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 MGSMSEAGEE QPMETTGATE NGHEAVPEGE SPAGAGTGAA AGAGGATAAP PSGNQNGAEG DQINASKNEE DAGKMFVGGL SWDTSKKDLK DYFTKFGEVV DCTIKMDPNT GRSRGFGFIL FKDAASVEKV LDQKEHRLDG RVIDPKKAMA MKKDPVKKIF VGGLNPEATE EKIREYFGEF GEIEAIELPM DPKLNKRRGF VFITFKEEEP VKKVLEKKFH TVSGSKCEIK VAQPKEVYQQ QQYGSGGRGN RNRGNRGSGG GGGGGGQGST NYGKSQRRGG HQNNYKPY
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 :
ANP32A HumanDescription:
Acidic Nuclear Phosphoprotein 32 Family Member A Human Recombinant
I1PP2A, LANP, MAPM, PHAP1, Leucine-rich acidic nuclear protein, PP32, Mapmodulin.
Product # :
PRO-252Price :
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Description
ANP32A Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 269 amino acids (1-249a.a.) and having a molecular mass of 30.7kDa. ANP32A is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ANP32A solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl, 0.1mM PMSF and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ANP32A often cooperate with MAP1B, TAF1A and Protein SET. ANP32A is involved in several cellular processes, such as proliferation, differentiation, caspase-dependent and caspase-independent apoptosis. Mapmodulin takes a part in E4F1-mediated transcriptional repression.
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Synonyms
I1PP2A, LANP, MAPM, PHAP1, Leucine-rich acidic nuclear protein, PP32, Mapmodulin.
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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 MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD.
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 :
ARFIP1 341 a.a. HumanDescription:
ADP-Ribosylation Factor Interacting Protein 1 341 a.a Human Recombinant
HSU52521, ADP-ribosylation factor-interacting protein 1, Arfaptin-1.
Product # :
PRO-2089Price :
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Description
ARFIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-341 a.a) and having a molecular mass of 41.0kDa.ARFIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARFIP1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ADP-Ribosylation Factor Interacting Protein 1 (ARFIP1) contains 1 AH domain and is a putative target protein of ADP-ribosylation factor.
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Synonyms
HSU52521, ADP-ribosylation factor-interacting protein 1, Arfaptin-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
MGSSHHHHHH SSGLVPRGSH MGSMAQESPK NSAAEIPVTS NGEVDDSREH SFNRDLKHSL PSGLGLSETQ ITSHGFDNTK EGVIEAGAFQ GGQRTQTKSG PVILADEIKN PAMEKLELVR KWSLNTYKCT RQIISEKLGR GSRTVDLELE AQIDILRDNK KKYENILKLA QTLSTQLFQM VHTQRQLGDA FADLSLKSLE LHEEFGYNAD TQKLLAKNGE TLLGAINFFI ASVNTLVNKT IEDTLMTVKQ YESARIEYDA YRTDLEELNL GPRDANTLPK IEQSQHLFQA HKEKYDKMRN DVSVKLKFLE ENKVKVLHNQ LVLFHNAIAA YFAGNQKQLE QTLKQFHIKL KTPGVDAPSW LEEQ.
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 :
ARL6 HumanDescription:
ADP-Ribosylation Factor-Like 6 Human Recombinant
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
Product # :
PRO-232Price :
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Description
ARL6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (1-186a.a) and having a molecular mass of 23.2kDa.ARL6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARL6 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.2M NaCl and 5mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ARL6 is a member of the ARF family of GTP-binding proteins. ARL6 has a vital part in modulating membrane trafficking and cytoskeletal functions. Mutation in ARL6 is the source of Bardet-Biedl syndrome (BBS3) which is a pleiotropic genetic disorder that causes obesity, photoreceptor degeneration, polydactyly, hypogenitalism, renal abnor-malities and developmental delay.
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Synonyms
ADP-ribosylation factor-like 6, Bardet-Biedl syndrome 3 protein, BBS3, RP55, MGC32934.
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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 MGLLDRLSVL LGLKKKEVHV LCLGLDNSGK TTIINKLKPS NAQSQNILPT IGFSIEKFKS SSLSFTVFDM SGQGRYRNLW EHYYKEGQAI IFVIDSSDRL RMVVAKEELD TLLNHPDIKH RRIPILFFAN KMDLRDAVTS VKVSQLLCLE NIKDKPWHIC ASDAIKGEGL QEGVDWLQDQ IQTVKT.
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 :
ICAM-1 HumanDescription:
Intercellular Adhesion Molecule-1 Human Recombinant
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
Product # :
PRO-383Price :
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Description
ICAM-1 Human Recombinant is expressed in E. coli containing 455 amino acids 28-483 fused to an amino terminal hexahistidine tag.The ICAM-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ICAM-1 is supplied (0.2mg/ml) in PBS, 50% Glycerol, 2mM Imidazole.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions. -
Synonyms
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
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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 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
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Applications
ICAM-I can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.
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 :
NGB Human, HisDescription:
Neuroglobin Human Recombinant, His Tag
NGB.
Product # :
CYT-1030Price :
Quantity :
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Shipped at Room temp
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Description
Neuroglobin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (1-151a.a) and having a molecular mass of 18kDa. NGB is fused to 10 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NGB is Filtered (0.4μm) and lyophilized from 0.5mg/ml in phosphate buffered saline.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Neuroglobin, 151 amino acid residue protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O (2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucleotide and enhanced by neuroglobin overexpression.
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Synonyms
NGB.
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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. Neuroglobin 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 MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E.
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 :
NPM2 HumanDescription:
Nucleophosmin 2 Human Recombinant
Nucleophosmin/nucleoplasmin 2, nucleoplasmin-2.
Product # :
PRO-1182Price :
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Description
NPM2 Human Recombinant produced in E. coli is a single polypeptide chain containing 237 amino acids (1-214) and having a molecular mass of 26.6 kDa.NPM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The NPM2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
Citations
More Info
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Introduction
NPM2 is a member of nucleoplasmin family. NPM2 is a core histones chaperone which takes part in chromatin reprogramming, particularly throughout fertilization and early embryonic development. NPM2 also takes part in sperm DNA decondensation during fertilization.
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Synonyms
Nucleophosmin/nucleoplasmin 2, nucleoplasmin-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
MGSSHHHHHH SSGLVPRGSH MGSMNLSSAS STEEKAVTTV LWGCELSQER RTWTFRPQLE GKQSCRLLLH TICLGEKAKE EMHRVEILPP ANQEDKKMQP VTIASLQASV LPMVSMVGVQ LSPPVTFQLR AGSGPVFLSG QERYEASDLT WEEEEEEEGE EEEEEEEDDE DEDADISLEE
QSPVKQVKRL VPQKQASVAK KKKLEKEEEE IRASVRDKSP VKKAKATARA KKPGFKK
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 :
SPINT2 Human, Sf9Description:
Serine Peptidase Inhibitor, Kunitz Type 2 Human Recombinant, Sf9
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
Product # :
PRO-2219Price :
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Description
SPINT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 176 amino acids (28-197 a.a.) and having a molecular mass of 20kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SPINT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPINT2 protein solution (0.2mg/ml) contains phosphate buffered saline (pH 7.4) and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
SPINT2 is a transmembrane protein acts as an inhibitor of HGF activator. SPINT2 inhibits plasmin, plasma and tissue kallikrein, and factor XIa. SPINT2 has two extracellular Kunitz domains that inhibit few serine proteases. SPINT2 is assumed tumor suppressor, mutations in SPINT2 leads to a congenital sodium diarrhea.
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Synonyms
Serine Peptidase Inhibitor, Kunitz Type, 2, Placental Bikunin, Hepatocyte Growth Factor Activator Inhibitor Type 2, Serine Protease Inhibitor, Kunitz Type, 2, HAI-2, HAI2, Kop, Kunitz-Type Protease Inhibitor 2, Placental, Bikunin, DIAR3, PB, Kunitz-type protease inhibitor 2.
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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
ADRERSIHDF CLVSKVVGRC RASMPRWWYN VTDGSCQLFV YGGCDGNSNN YLTKEECLKK CATVTENATG DLATSRNAAD SSVPSAPRRQ DSEDHSSDMF NYEEYCTANA VTGPCRASFP RWYFDVERNS CNNFIYGGCR GNKNSYRSEE ACMLRCFRQQ ENPPLPLGSK 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 :
FADD HumanDescription:
Fas-Associated Death Domain Human Recombinant
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
Product # :
PRO-733Price :
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Description
FADD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-208 a.a.) and having a molecular mass of 27.4 kDa.FADD is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FADD protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FADD is an adaptor protein that cooperates with a variety of cell surface receptors and mediates cell apoptotic signals. Using its C-terminal death domain, FADD is recruited by TNFRSF6/Fas-receptor, tumor necrosis factor receptor, TNFRSF25, and TNFSF10/TRAIL-receptor, and consequently it take parts in the death signaling initiated by these receptors. FADD interaction with the receptors reviels the N-terminal effector domain of, which allows it to recruit caspase-8, and thus initiate the cysteine protease cascade. Knockout studies in mice furthermore propose the significance of FADD in premature T cell development. FADD plays a role in survival/proliferation and cell cycle development. FADD also takes part in cellular sublocalization, protein phosphorylation, and inhibitory molecules.
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Synonyms
GIG3, MORT1, MGC8528, FADD, Fas (TNFRSF6)-associated via death domain, Protein FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity, Growth-inhibiting gene 3 protein.
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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
MRGSHHHHHHGMASMTGGQQ MGRDLYDDDD KDRWGSMDPF LVLLHSVSSS LSSSELTELK FLCLGRVGKR KLERVQSGLD LFSMLLEQND LEPGHTELLR ELLASLRRHD LLRRVDDFEA GAAAGAAPGE EDLCAAFNVI CDNVGKDWRR LARQLKVSDT KIDSIEDRYP RNLTERVRES LRIWKNTEKE NATVAHLVGA LRSCQMNLVA DLVQEVQQAR DLQNRSGAMS PMSWNSDAST SEAS.
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 :
CCL17 Human, HisDescription:
Thymus and Activation Regulated Chemokine Human Recombinant (CCL17), His Tag
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
Product # :
CHM-359Price :
Quantity :
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Shipped with Ice Packs
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Description
TARC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 92 amino acids (24-94 a.a.) and having a molecular mass of 10.3 kDa. The TARC is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TARC protein (0.5mg/ml) contains 1xPBS (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by Analysis by SDS-PAGE.
Citations
More Info
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Introduction
TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.
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Synonyms
C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.
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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 MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.
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Background
What is the molecular weight/Mw of CCL17 HUMAN, HIS Protein?
CCL17 HUMAN, HIS Protein has a total Mw of 10.3kDa.
What is the source or expression system of CCL17 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CCL17 HUMAN, HIS Protein?
CCL17 HUMAN, HIS Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL17 HUMAN, HIS Protein?
The biological functionality of CCL17 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CCL17 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.
What applications can CCL17 HUMAN, HIS Protein be used in?
CCL17 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL17 HUMAN, HIS Protein?
The endotoxin level is minimal, CCL17 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CCL17 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CCL17 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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 :
TIMP1 Human, Sf9Description:
Tissue Inhibitor of Metalloprotease 1 Human Recombinant, Sf9
TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 1.
Product # :
ENZ-876Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TIMP1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 190 amino acids (24-207a.a.) and having a molecular mass of 21.5kDa. TIMP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TIMP1 protein solution (0.2mg/ml) contains phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
TIMP1 is a member of the TIMP family. TIMP1 is an inducible glycoprotein produced by various cell types. The TIMP1 glycoprotein is a natural inhibitor of the matrix metalloproteinases, which a group of peptidases involved in degradation of the extracellular matrix. TIMP1 binds in a reversible mode to MMPs, with regions in the N-terminal domain binding to the MMP substrate-binding site. On top of its inhibitory function against most of the known MMPs, TIMP1 is able to promote cell proliferation in a broad range of cell types, and may also have an anti-apoptotic role. Furthermore, TIMP1 has erthyroid-potentiating activity via translocation to the nucleus and also inhibits apoptosis in B-cells. The TIMP1 gene is situated within intron 6 of the synapsin I gene and is transcribed in the opposite direction. TIMP1 activity is dependent on the existence of disulfide bonds. TIMP1 transcription is extremely inducible in reaction to many cytokines and hormones.
Increased TIMP1 levels are connected with squamous cell laryngeal carcinoma. TIMP1 overexpression is linked to gastric cancer. -
Synonyms
TIMP Metallopeptidase Inhibitor 1, TIMP, EPA, Tissue Inhibitor Of Metalloproteinases 1, Fibroblast Collagenase Inhibitor, Erythroid-Potentiating Activity, Collagenase Inhibitor, TIMP-1, CLGI, Tissue Inhibitor Of Metalloproteinase 1 (Erythroid Potentiating Activity, Collagenase Inhibitor), Erythroid Potentiating Activity, Metalloproteinase Inhibitor 1, EPO, HCI, Metalloproteinase inhibitor 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. 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.
- View Data Sheet
Name :
Follistatin Human, HisDescription:
Follistatin Human Recombinant, His Tag
FST, FS, Activin-binding protein.
Product # :
CYT-029Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FST His Protein is 36.0 kDa protein containing 325 amino acid residues of the FST His and the 10 aa N-Terminal His-tag.
Source
E. coli.
Formulation
FST His Tag was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.
Citations
More Info
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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
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Synonyms
FST, FS, Activin-binding protein.
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Stability
Store lyophilized FST His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted FST His 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
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
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Background
What is the molecular weight/Mw of FOLLISTATIN HUMAN, HIS Protein?
FOLLISTATIN HUMAN, HIS Protein has a total Mw of 36kDa.
What is the source or expression system of FOLLISTATIN HUMAN, HIS Protein?
Escherichia Coli.
What is the Biological Activity of FOLLISTATIN HUMAN, HIS Protein?
The biological functionality of FOLLISTATIN HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of FOLLISTATIN HUMAN, HIS Protein?
MKHHHHHHAS GNCWLRQAKN GRCQVLYKTE LSKEECCSTG RLSTSWTEED VNDNTLFKWM IFNGGAPNCI PCKETCENVD CGPGKKCRMN KKNKPRCVCA PDCSNITWKG PVCGLDGKTY RNECALLKAR CKEQPELEVQ YQGRCKKTCR DVFCPGSSTC VVDQTNNAYC VTCNRICPEP ASSEQYLCGN DGVTYSSACH LRKATCLLGR SIGLAYEGKC IKAKSCEDIQ CTGGKKCLWD FKVGRGRCSL CDELCPDSKS DEPVCASDNA TYASECAMKE AACSSGVLLE VKHSGSCNSI SEDTEEEEED EDQDYSFPIS SILEW.
What applications can FOLLISTATIN HUMAN, HIS Protein be used in?
FOLLISTATIN HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FOLLISTATIN HUMAN, HIS Protein?
The endotoxin level is minimal, FOLLISTATIN HUMAN, HIS 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.
- View Data Sheet
Name :
LGALS2 Mouse, ActiveDescription:
Galectin-2, BioActive Mouse Recombinant
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
Product # :
CYT-1155Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGALS2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids (1-130 a.a) and having a molecular mass of 17.3kDa.LGALS2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
LGALS2 protein (1mg/ml) contains 10% glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
Citations
More Info
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Introduction
Galectin-2 or LGALS2 is a protein, part of the galectin proteins family. The galectin proteins family holds galectin proteins family lectins that mediates adhesion between cells or cells to ECM. This family also take part in pre-mRNA splicing, apoptosis & tumor progression. Galectin-2 induces apoptosis in T cells that are activated & binds to lymphotoxin-a, also can implicatate on myocardial infarction. LGALS2 from human and mouse share about 65% amino acid sequence resemblance.
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Synonyms
Galectin-2, Gal-2, Lgals2, 2200008F12Rik, AI324147.
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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 MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE
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Background
What is the molecular weight/Mw of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein has a total Mw of 17.3kDa.
What is the source or expression system of LGALS2 MOUSE, ACTIVE Protein?
Escherichia Coli.
What is the Purity of LGALS2 MOUSE, ACTIVE Protein?
LGALS2 MOUSE, ACTIVE Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS2 MOUSE, ACTIVE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 is ≥ 20ug/ml.
What is the amino acid sequence of LGALS2 MOUSE, ACTIVE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMSEKFEV KDLNMKPGMS LKIKGKIHND VDRFLINLGQ GKETLNLHFN PRFDESTIVC NTSEGGRWGQ EQRENHMCFS PGSEVKITIT FQDKDFKVTL PDGHQLTFPN RLGHNQLHYL SMGGLQISSF KLE.
What applications can LGALS2 MOUSE, ACTIVE Protein be used in?
LGALS2 MOUSE, ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS2 MOUSE, ACTIVE Protein?
The endotoxin level is minimal, LGALS2 MOUSE, ACTIVE 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.
- View Data Sheet
Name :
LILRB1 HumanDescription:
Leukocyte Immunoglobulin Like Receptor B1 Human Recombinant
Leukocyte immunoglobulin-like receptor subfamily B member 1,Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Product # :
PRO-2668Price :
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Shipped with Ice Packs
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Description
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The LILRB1 solution (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Biological activity is > 50%. It is defined by the ability of the immobilized protein to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells, while the cells are added to LILRB1 coated plates at 5ug/ml.
Citations
More Info
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Introduction
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1) is a member of the leukocyteimmunoglobulinlike receptor (LIR) family. LILRB1is expressed on immune cells, binds to MHC classI molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immuneresponse. LILRB1 controls inflammatory responses and cytotoxicity to help focus the immune responseand limit autoreactivity. LILRB1 is also expressed on the surface of B cells and monocytes, subsets of NKcells, gamma δ T cells,memory/effector CD8+ T cells and monocyte-derived dendritic cells.
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Synonyms
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B -
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
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE 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.
- View Data Sheet
Name :
ULBP2 Human, Sf9Description:
UL16 Binding Protein 2 Human Recombinant, Sf9
ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-2.
Product # :
PRO-2378Price :
Quantity :
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Shipped with Ice Packs
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Description
ULBP2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (26-216a.a) and having a molecular mass of 22.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). ULBP2 is fused to a 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ULBP2 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
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Introduction
ULBP2 is a member of the MHC class I family. ULBP2 is ligand for the NKG2D receptor, composed with at least ULBP1 and ULBP3. ULBPs promote multiple signaling pathways in primary NK cells, triggering the production of cytokines and chemokines. Binding of ULBPs ligands to NKG2D encourages calcium mobilization and activation of the JAK2, STAT5, ERK and PI3K kinase/Akt signal transduction pathway. In CMV infected cells, ULBP2 cooperates with soluble CMV glycoprotein UL16. This cooperation is blocked with the NKG2D receptor, providing a mechanism in which CMV infected cells can escape the immune system. Additionally, UL16 causes ULBP2 to be held in the ER and cis-Golgi apparatus so that it does not reach the cell surface.
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Synonyms
ULBP2, ALCAN-alpha, N2DL2, NKG2DL2, RAET1H, UL16 Binding Protein 2, Retinoic Acid Early Transcript 1H, UL16-Binding Protein 2, ALCAN-Alpha, NKG2D Ligand 2, N2DL-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
ADPGRADPHS LCYDITVIPK FRPGPRWCAV QGQVDEKTFL HYDCGNKTVT PVSPLGKKLN VTTAWKAQNP VLREVVDILT EQLRDIQLEN YTPKEPLTLQ ARMSCEQKAE GHSSGSWQFS FDGQIFLLFD SEKRMWTTVH PGARKMKEKW ENDKVVAMSF HYFSMGDCIG WLEDFLMGMD STLEPSAGAP LAMSHHHHHH.
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 :
EBI3 Human, HisDescription:
Epstein Barr Virus Induced 3 Human Recombinant, His Tag
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
Product # :
CYT-668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EBI3 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 209 amino acids fragment (21-229) having a molecular weight of 34kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The EBI3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
EBI3 protein is supplied in 1xPBS, 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
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Synonyms
Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein, EBI3, IL27B.
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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. Please avoid freeze thaw cycles.
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Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 34kDa.
What is the source or expression system of EBI3 Protein?
Escherichia Coli.
What is the Purity of EBI3 Protein?
EBI3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.
What is the amino acid sequence of EBI3 Protein?
EBI3 Protein is composed from 209 amino acids.
What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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.
- View Data Sheet
Name :
ANGPTL4 HumanDescription:
Angiopoietin-like Protein 4 Human Recombinant
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
Product # :
CYT-249Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The ANGPTL4 Human Recombinant is manufactured with N-terminal fusion of His Tag. The Angiopoietin-like Protein 4 His -Tagged Fusion Protein is 25 kDa protein containing 204 amino acid residues of the Angiopoietin-like Protein 4 and 16 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
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Introduction
FIAF (fasting-induced adipose factor) a.k.a ANGPTL4 or PGAR or HFARP is an adipocytokine up-regulated by fasting, by peroxisome proliferator-activated receptor agonists, and by hypoxia. ANGPTL4 is found in human and mouse blood plasma both as a native protein and in a truncated form. In human white adipose tissue and SGBS adipocytes, only the native form of ANGPTL4 could be detected, whereas in mice the differentiation of mouse 3T3-L1 adipocytes is associated with the production of truncated ANGPTL4. However, the truncated ANGPTL4 is produced by human liver. In human blood plasma FIAF is mainly presented in a truncated form (FIAF-S2), whose levels treatment increases (as shown by experimental data). There is an inter individual variation in ANGPTL4 levels of both the truncated and the native form, however those levels were not influenced by prolonged semistarvation and are not associated with body mass index.
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Synonyms
ANGPTL4, NL2, ARP4, FIAF, PGAR, HFARP, pp1158, ANGPTL2, Fasting- Induced Adipose Factor, Hepatic Fibrinogen/Angiopoietin-Related Protein, PPARG Angiopoietin-Related Protein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Angiopoietin-like Protein 4 Human recombinant at -20°C. Aliquot the ANGPTL4 after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted ANGPTL4 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
Add 0.1M Acetate buffer pH4 and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited.
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Amino Acid Sequence
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
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Background
Angiopoietin-like Protein 4 Human Recombinant: A Promising Therapeutic Approach for Metabolic Disorders
Abstract:
Angiopoietin-like protein 4 (ANGPTL4) is a multifunctional protein involved in the regulation of lipid metabolism and energy homeostasis. It has emerged as a potential therapeutic target for metabolic disorders, including obesity, dyslipidemia, and insulin resistance. The availability of human recombinant ANGPTL4 protein has provided researchers with a valuable tool to investigate its biological functions and explore its therapeutic potential. This concise review provides an overview of the role of ANGPTL4 in metabolic regulation and discusses the potential of ANGPTL4 human recombinant protein as a therapeutic intervention.Introduction:
Metabolic disorders are a global health challenge with significant implications for cardiovascular health. ANGPTL4, a member of the angiopoietin-like protein family, has gained attention for its role in lipid metabolism and energy balance. ANGPTL4 influences the uptake, storage, and utilization of lipids, as well as glucose metabolism, making it an attractive target for therapeutic interventions.Mechanisms of ANGPTL4 Action:
ANGPTL4 exerts its effects through multiple mechanisms. It inhibits lipoprotein lipase (LPL) activity, reducing the hydrolysis of triglycerides and leading to elevated plasma triglyceride levels. ANGPTL4 also promotes adipose tissue lipolysis, facilitating the release of fatty acids for energy utilization. Moreover, ANGPTL4 affects glucose metabolism by modulating insulin signaling and glucose uptake in various tissues.Role of ANGPTL4 in Metabolic Regulation:
ANGPTL4 plays a critical role in lipid and glucose metabolism. It regulates plasma lipid levels by modulating LPL activity and lipid uptake in adipose tissue and skeletal muscle. ANGPTL4 also influences energy homeostasis by promoting lipid mobilization from adipocytes and regulating fatty acid oxidation. Additionally, ANGPTL4 impacts glucose metabolism by modulating insulin sensitivity and glucose uptake in skeletal muscle and adipose tissue.Therapeutic Potential of ANGPTL4 Human Recombinant Protein:
The availability of ANGPTL4 human recombinant protein opens new avenues for therapeutic interventions targeting metabolic disorders. Administration of ANGPTL4 recombinant protein or modulation of ANGPTL4 activity offers potential strategies to improve lipid profiles, reduce adiposity, and enhance insulin sensitivity. Preclinical studies have shown promising results, demonstrating the potential of ANGPTL4 as a therapeutic target for metabolic disorders.Conclusion:
ANGPTL4 represents a promising target for therapeutic interventions in metabolic disorders. Its involvement in the regulation of lipid and glucose metabolism makes it an attractive candidate for the development of novel treatment approaches. The availability of ANGPTL4 human recombinant protein enables further exploration of its therapeutic potential and may contribute to the development of effective interventions for metabolic disorders.What is the molecular weight/Mw of ANGPTL4 Protein?
ANGPTL4 Protein has a total Mw of 25kDa.
What is the source or expression system of ANGPTL4 Protein?
Escherichia Coli.
What is the Purity of ANGPTL4 Protein?
ANGPTL4 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ANGPTL4 Protein?
The biological functionality of ANGPTL4 Protein will be determined in the future.
What is the amino acid sequence of ANGPTL4 Protein?
MRGSHHHHHH GMASHMGPVQ SKSPRFASWD EMNVLAHGLL QLGQGLREHA ERTRSQLSAL ERRLSACGSA CQGTEGSTDL PLAPESRVDP EVLHSLQTQL KAQNSRIQQL FHKVAQQQRH LEKQHLRIQH LQSQFGLLDH KHLDHEVAKP ARRKRLPEMA QPVDPAHNVS RLHRLPRDCQ ELFQVGERQS GLFEIQPQGS PPFLVNCKMT SDGGWTVIQR.
What applications can ANGPTL4 Protein be used in?
ANGPTL4 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ANGPTL4 Protein?
The endotoxin level is minimal, ANGPTL4 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.
- View Data Sheet
Name :
LDL HumanDescription:
Low-Density Lipoprotein Human
Low Density Lipoprotein, LDL.
Product # :
PRO-562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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Description
Human Low Density Lipoprotein (LDL) produced in Human plasma.
Source
Human plasma.
Citations
More Info
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Introduction
LDL is a low-density lipoprotein that transports cholesterol and triglycerides from the liver to peripheral tissues. LDL (like all lipoproteins) facilitates the movement of fats and cholesterol within the water based solution of the blood stream. Each natural LDL particle contains a single Apo B-100 molecule (apolipoprotein B-100 is a protein with 4536 amino acid residues) that circulates the fatty acids and keeps them soluble in the aqueous environment. Additionally, the LDL core is highly-hydrophobic, consisting of linoleate (a polyunsaturated fatty acid) and about 1500 esterified cholesterol molecules. This core is enclosed by a shell of phospholipids and unesterified cholesterol in addition to a single copy of B-100 large protein (514 kD). Even though the LDL particles are approximately 22 nm in diameter and have a mass of about 3 million Daltons, they have a mass and size distribution since the LDL particles contain a varying number of fatty acids. LDL receptors are synthesized and placed in the plasma membrane when a cell requires cholesterol. The LDL receptors scatter freely until they link to clathrin-coated pits. LDL particles in the blood stream attach to these extracellular LDL receptors. The clathrin-coated pits at that time form vesicles that are endocytosed into the cell. Once the clathrin coat is dropped, the vesicles transport the LDL and their receptors to early endosomes, onto late endosomes to lysosomes. At this point the cholesterol esters in the LDL are hydrolysed. The LDL receptors are recovered back to the plasma membrane. Since LDLs convey cholesterol to the arteries and can be retained there by arterial proteoglycans initializing the formation of plaques, increased levels are linked to atherosclerosis, and thus heart attack, stroke, and peripheral vascular disease. And so, cholesterol within LDL lipoproteins is habitually called "bad" cholesterol. This is a misconception since the cholesterol transported on LDL is the same as the one transported on other lipoprotein particles, it is in itself not "bad", rather it is how and where the cholesterol is being transported, and in what amounts ultimately, which causes adverse effects. HDL / LDL ratio can give an indication of risk for arteriosclerosis.
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Synonyms
Low Density Lipoprotein, LDL.
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Physical Appearance
Yellow to orange liquid.
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Stability
Human LDL although stable at 4°C for 1 week, should be stored below -15°C (short term i.e. < 3 months) and below -70°C for long term.Human LDL can be further diluted with saline + 15% sucrose.
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Human Virus Test
Starting material donor tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies and Syphilis, HIV1 / HCV / HBV NAT.
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 :
MBP HumanDescription:
Myelin Basic Protein Human Recombinant
Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.
Product # :
PRO-1713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-197) and having a molecular mass of 23.9kDa.MBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MBP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
MBP is a major component of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system, although, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs emerge from the long MBP gene which holds three additional exons located upstream of the classic MBP exons. The Golli mRNAs contain three exons unique to Golli-MBP, spliced in-frame to one or more MBP exons. The second family of transcripts contains only MBP exons and produces the well characterized myelin basic proteins. MBP transcription unit is an essential part of the Golli transcription unit and the arrangement is important for the function and/or regulation of these genes.
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Synonyms
Myelin basic protein, MBP, Myelin A1 protein, Myelin membrane encephalitogenic protein.
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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 MGSMGNHAGK RELNAEKAST NSETNRGESE KKRNLGELSR TTSEDNEVFG EADANQNNGT SSQDTAVTDS KRTADPKNAW QDAHPADPGS RPHLIRLFSR DAPGREDNTF KDRPSESDEL QTIQEDSAAT SESLDVMASQ KRPSQRHGSK YLATASTMDH ARHGFLPRHR DTGILDSIGR FFGGDRGAPK RGSGKVSSEE
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 :
LA/SS-B Human, BiotinDescription:
LA / SS-B Human Recombinant, Biotinylated
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-2562Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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 48 kDa. The LA/SS-B is expressed with a -6x His tag at N-terminus and 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 80.0% 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.
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Immunological Functions
1. Binds IgG type human auto antibodies.2. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)
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 :
CRYZ HumanDescription:
Crystallin Zeta Human Recombinant
Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.
Product # :
PRO-2016Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CRYZ Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 352 amino acids (1-329 a.a.) and having a molecular mass of 37.6kDa.CRYZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CRYZ protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
Crystallin Zeta, also known as CRYZ, Binds NADP and participates in a one-electron transfer process. CRYZ takes part in the detoxification of xenobiotics and Interacts with (AU)-rich elements (ARE) in the 3'-UTR of target mRNA species. CRYZ improves the mRNA coding for BCL2.
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Synonyms
Quinone oxidoreductase, NADPH:quinone reductase, Zeta-crystallin, CRYZ, Quinone oxidoreductase isoform a, Crystallin, zeta (quinone reductase), Crystallin Zeta.
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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 MGSMATGQKL MRAVRVFEFG GPEVLKLRSD IAVPIPKDHQ VLIKVHACGV NPVETYIRSG TYSRKPLLPY TPGSDVAGVI EAVGDNASAF KKGDRVFTSS TISGGYAEYA LAADHTVYKL PEKLDFKQGA AIGIPYFTAY RALIHSACVK AGESVLVHGA SGGVGLAACQ IARAYGLKIL GTAGTEEGQK IVLQNGAHEV FNHREVNYID KIKKYVGEKG IDIIIEMLAN VNLSKDLSLL SHGGRVIVVG SRGTIEINPR DTMAKESSII GVTLFSSTKE EFQQYAAALQ AGMEIGWLKP VIGSQYPLEK VAEAHENIIH GSGATGKMIL LL.
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 :
CUTC HumanDescription:
cutC Copper Transporter Homolog Human Recombinant
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
Product # :
PRO-911Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CUTC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 293 amino acids (1-273 a.a) and having a molecular mass of 31.5kDa.CUTC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CUTC protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
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Introduction
CUTC belongs to the Cut family and may be involved in efflux trafficking of cuprous ion. The Cut family is linked with the copper homeostasis and involved in several vital metabolisms, such as uptake, storage, delivery, and efflux of copper. Copper which is an essential heavy metal trace element has an imperative role in cell physiology.
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Synonyms
Copper homeostasis protein cutC homolog, CUTC, CGI-32, RP11-483F11.3.
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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 MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV.
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 :
CXCL17 RatDescription:
VEGF Co-regulated Chemokine 1 Rat Recombinant
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Product # :
CHM-281Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.Citations
More Info
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Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
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Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
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Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.
What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.
What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 RAT Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL17 RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL17 RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
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.