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Search results

1000 results found for “Listeriolysin”

Name

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  • View Data Sheet

    Name :

    Follistatin Human, His

    Description:

    Follistatin Human Recombinant, His Tag

    FST, FS, Activin-binding protein.

    Product # :

    CYT-029

    Price :

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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.

    More Info

    • 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).

    • Synonyms

      FST, FS, Activin-binding protein.

    • 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.

    • 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.

    • 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.

    • 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.

    Fst His Human
  • View Data Sheet

    Name :

    FASLG Human

    Description:

    FAS Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.

    Product # :

    CYT-031

    Price :

    Quantity :

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    • sds-page

    Description

    FASLG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (130-281 a.a.) and having a molecular mass of 19.6kDa.FASLG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FASLG protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    FASL-sds-page - Product image 1

    More Info

    • Introduction

      The type II transmembrane protein FASLG is a member of the tumor necrosis factor (TNF) superfamily. A fas ligand/receptor interaction has a significant part in the regulation of the immune system and the advancement of cancer. FASLG is expressed on the activated T cell surface as a nondisulfidelinked homotrimer. FASLG binding to Fas/CD95/TNFRSF6 on a nearby cell prompts apoptosis in the Fas expressing cell. FASLG is released from the cell surface by metalloproteinases as a soluble molecule that stays trimeric and is able to bind with Fas, but its capability to activate apoptosis is radically reduced. In addition, FASLG binds to DcR3 - a soluble trap receptor with no signal transduction capabilities. Flawed Fas-mediated apoptosis causes oncogenesis in addition to drug resistance in existing tumors. Constitutive expression of FASLG in a variety of tumors enables their immune evasion. Both mouse and human FASLG are active on mouse and human cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 6, Apoptosis antigen ligand, APTL, CD95 ligand, CD95-L, Fas antigen ligand, Fas ligand, FasL, CD178, FASLG, APT1LG1, CD95L, TNFSF6, ALPS1B.

    • 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 MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.

    • Background

      What is the molecular weight/Mw of FASL Protein?
      FASL Protein has a total Mw of 19.6kDa.

      What is the source or expression system of FASL Protein?
      Escherichia Coli.

      What is the Purity of FASL Protein?
      FASL Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FASL Protein?
      The biological functionality of FASL Protein will be determined in the future.

      What is the amino acid sequence of FASL Protein?
      MGSSHHHHHH SSGLVPRGSH MQIGHPSPPP EKKELRKVAH LTGKSNSRSM PLEWEDTYGI VLLSGVKYKK GGLVINETGL YFVYSKVYFR GQSCNNLPLS HKVYMRNSKY PQDLVMMEGK MMSYCTTGQM WARSSYLGAV FNLTSADHLY VNVSELSLVN FEESQTFFGL YKL.

      What applications can FASL Protein be used in?
      FASL Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FASL Protein?
      The endotoxin level is minimal, FASL 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.

    Faslg Human
  • View Data Sheet

    Name :

    CCL28 Human, His

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-366

    Price :

    Quantity :

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    • description
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    Description

    CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • 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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.

      What is the source or expression system of CCL28 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN, HIS Protein?
      The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

      What applications can CCL28 HUMAN, HIS Protein be used in?
      CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL28 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.

    Ccl28 Human His
  • View Data Sheet

    Name :

    KAT2A Human

    Description:

    K (lysine) Acetyltransferase 2A Human Recombinant

    Histone acetyltransferase KAT2A, General control of amino acid synthesis protein 5-like 2, Histone acetyltransferase GCN5, HsGCN5, Lysine acetyltransferase 2A, STAF97, KAT2A, GCN5, GCN5L2, HGCN5, PCAF-b.

    Product # :

    ENZ-166

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    Description

    KAT2A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (411-837 a.a) and having a molecular mass of 51.1kDa.KAT2A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KAT2A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 40% glycerol, 200mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      General control of amino acid synthesis protein 5 like 2 (KAT2A) is a member of the GCN5 family. KAT2A functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. KAT2A interacts with Ku70, TAF9, transcription initiation protein SPT3 homolog, TADA2L, Ku80 and DDB1.

    • Synonyms

      Histone acetyltransferase KAT2A, General control of amino acid synthesis protein 5-like 2, Histone acetyltransferase GCN5, HsGCN5, Lysine acetyltransferase 2A, STAF97, KAT2A, GCN5, GCN5L2, HGCN5, PCAF-b.

    • 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 MGGGSNSSLS LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK.

    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.

    Kat2A Human
  • View Data Sheet

    Name :

    LYPLA2 Human

    Description:

    Lysophospholipase II Human Recombinant

    Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    Product # :

    ENZ-076

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    Description

    LYPLA2 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 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLA2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.

    • Synonyms

      Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    • 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 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V.

    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.

    Lypla2 Human
  • View Data Sheet

    Name :

    CoV-2-S1 (319-541), Fc

    Description:

    Coronavirus 2019 Spike Glycoprotein-S1 Receptor Binding Domain (319-541 a.a), Fc Recombinant

    Product # :

    SARS-029

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    Description

    The HEK293 derived recombinant protein contains the Coronavirus 2019 Spike Glycoprotein S1 Receptor Binding Domain [ RBD ], Wuhan-Hu-1 strain, amino acids 319-541 fused to Fc tag at C-terminal.

    Source

    HEK293 Cells.

    Formulation

    CoV-S1 RBD protein is lyophilized from 1x PBS pH-7.4 + 5% trehalose.

    Purity

    Protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Lyophilized freezed dried powder.

    • Stability

      Lyophilized Cov-2 S1 Glycoprotein RBD although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CoV2 Spike protein 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.

    • Purification Method

      Purified by Protein-G 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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  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopD

    Description:

    Yersinia Enterocolitica (O:9) YopD Recombinant

    Product # :

    PRO-2276

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    Description

    Recombinant Yersinia Enterocolitica (O:9) YopD produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 34,603 Dalton. Y.Enterocolitica (O:9) YopD is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Y.Enterocolitica (O:9) YopD is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Yersinia enterocolitica is a Gram-negative bacillus-shaped bacterium, which is a member of the Enterobacteriaceae family. Y.Enterocolitica is motile at temperatures between 22-29°C, however becomes non-motile at normal human body temperature. Y. Enterocolitica infection causes the yersiniosis disease, which is an animal-borne disease occurring in humans, as well as in a various groups of animals such as cattle, deer, pigs, and birds. Yersinia enterocolitica is a heterogeneous group of strains, which are conventionally classified by bio-typing into six bio-groups on the basis of phenotypic characteristics, and by serotyping into more than 57 “O” serogroups, on the basis of their O (lipopolysaccharide or LPS) surface antigen. Five of the six biogroups (1B and 2–5) are considered as pathogens. Nevertheless, only a few of these serogroups have been linked with disease in either humans or animals. Strains which belong to serogroups O:3 (biogroup 4), O:5,27 (biogroups 2 and 3), O:8 (biogroup 1B), and O:9 (biogroup 2) are most frequently isolated worldwide from human samples. Still, the main Y. enterocolitica serogroup in many European countries is serogroup O:3 followed by O:9, whereas the serogroup O:8 is mostly detected in the United States.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG- and IgM- and IgA-type human antibodies.2. Immunodot test with positive/negative sera panels.

    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.

    Yenterocolitica O 9 Yopd
  • View Data Sheet

    Name :

    IL 11 Mouse

    Description:

    Interleukin-11 Mouse Recombinant

    AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    Product # :

    CYT-646

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    Description

    Interleukin-11 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19.1kDa. The Mouse IL-11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine T11 was found to be less than 2.0 ng/ml, corresponding to a specific activity of 500,000IU/mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      AGIF, Adipogenesis inhibitory factor, IL-11, Interleukin-11, Il11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MPGPPAGSPR VSSDPRADLD SAVLLTRSLL ADTRQLAAQM RDKFPADGDH SLDSLPTLAM SAGTLGSLQL PGVLTRLRVD LMSYLRHVQW LRRAGGPSLK TLEPELGALQ ARLERLLRRL QLLMSRLALP QAAPDQPVIP LGPPASAWGS IRAAHAILGG LHLTLDWAVR GLLLLKTRL.

    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.

    Il 11 Mouse
  • View Data Sheet

    Name :

    IL 19 Mouse

    Description:

    Interleukin-19 Mouse Recombinant

    Interleukin-19, IL-19, Il19.

    Product # :

    CYT-855

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    Description

    Interleukin-19 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.7kDa. The IL-19 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered aqueous solution containing 5mM Na3PO4 and 150mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL19 is a cytokine that belongs to the IL10 cytokine subfamily. IL-19 is found to be preferentially expressed in monocytes. It can bind the IL20 receptor complex and lead to the activation of the signal transducer and activator of transcription 3 (STAT3). A similar cytokine in mouse is reported to up-regulate the expression of IL6 and TNF-alpha and induce apoptosis, which suggests a role of this cytokine in inflammatory responses. Alternatively spliced transcript variants encoding the distinct isoforms have been described.

    • Synonyms

      Interleukin-19, IL-19, Il19.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-19 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL19 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IL-19 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MLRRCLISVDMRLIEKSFHEIKRAMQTKDTFKNVTILSLENLRSIKPGDVCCMTNNLL
      TFYRDRVFQDHQERSLEVLRRISSIANSFLCVQKSLERCQVHRQCNCSQEATNATRII
      HDNYNQLEVSSAALKSLGELNILLAWIDRNHLETPAA.

    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.

    Il 19 Mouse
  • View Data Sheet

    Name :

    LIF Human

    Description:

    Leukemia Inhibitory Factor Human Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-644

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    Description

    Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.

    • Background

      Leukemia Inhibitory Factor (LIF) Background

      Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.

      LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.

      Function and Applications of LIF

      LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.

      Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.

      Structure and Interactions

      LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.

    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.

    Lif Human
  • View Data Sheet

    Name :

    LGALS16 Human

    Description:

    Galectin-16 Human Recombinant

    Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

    Product # :

    CYT-993

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    Description

    LGALS16 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 16kDa.The LGALS16 also appears as a homodimer and therefore a 32kDa band is observed as well. LGALS16 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    1x PBS and 25mM arginine.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Galectin-16 (LGALS16) binds lactose with high affinity. LGALS16 is a strong inducer of T-cell apoptosis.

    • Synonyms

      Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      The Recombinant LGALS16 protein although stable at 4°C for 1 week, should be stored 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.

    • Background

      What is the molecular weight/Mw of LGALS16 HUMAN Protein?
      LGALS16 HUMAN Protein has a total Mw of 16kDa.

      What is the source or expression system of LGALS16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS16 HUMAN Protein?
      LGALS16 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS16 HUMAN Protein?
      The biological functionality of LGALS16 HUMAN Protein will be determined in the future.


      What applications can LGALS16 HUMAN Protein be used in?
      LGALS16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS16 HUMAN Protein?
      The endotoxin level is minimal, LGALS16 HUMAN 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.

    Lgals16 Human
  • View Data Sheet

    Name :

    EREG Human

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Epiregulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Epiregulin 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Epiregulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

      What is the source or expression system of EREG Protein?
      Escherichia Coli.

      What is the Purity of EREG Protein?
      EREG Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

      What applications can EREG Protein be used in?
      EREG Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EREG Protein?
      The endotoxin level is minimal, EREG 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.

    Epiregulin Human
  • View Data Sheet

    Name :

    Polcalcin Phl p 7

    Description:

    Pollen Allergen Phl p 7 Recombinant

    Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    Product # :

    ALR-015

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    Description

    Recombinant Polcalcin Phl p 7 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9.0 kDa. Polcalcin Phl p 7 is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Polcalcin Phl p 7 is supplied in 20mM HEPES buffer pH-8.0, 0.2M NaCl, 1mM CaCl2 and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.

    • Synonyms

      Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Polcalcin Phl P 7
  • View Data Sheet

    Name :

    CoV-2 Nucleocapsid

    Description:

    Coronavirus 2019 Nucleocapsid Recombinant

    Product # :

    SARS-013

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    Description

    The E.Coli derived recombinant protein contains the Coronavirus 2019 full-length nucleocapsid: Gene bank- MN908947, fused to 6xHis tag at C-terminal and having a Mw. Of 48 kDa as appears on SDS-PAGE.

    Source

    Escherichia Coli.

    Formulation

    CoV 2019 protein solution is supplied in PBS and 25mM K2CO3.

    Purity

    CoV 2019 Nucleocapsid protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CoV 2019 Nucleocapsid protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Amino Acid Sequence

      MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKED

      LKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGAN

      KDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSR

      SRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAA

      EASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFF

      GMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADE

      TQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA

    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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  • View Data Sheet

    Name :

    CXCL13 Mouse

    Description:

    BCA-1/BLC Mouse Recombinant (CXCL13)

    C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    Product # :

    CHM-030

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    Description

    CXCL13 Mouse Recombinant (22-109) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10kDa.The BCA-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCA1 protein was lyophilized from a 0.2µm filtered solution in Acetonitrile and TFA.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

    More Info

    • Introduction

      BCA-1 is a CXC chemokine that is highly expressed in thesecondary lymphoid organs, such as follicles of the spleen, lymph nodes, and Peyer's patches. CXCL13 promotes the migration of B lymphocytes (compared to T cells and macrophages), by stimulating calcium influx into, and chemotaxis of, cells expressing Burkitt's lymphoma receptor 1 (BLR1). BCA1 therefore function in the homing of B lymphocytes to follicles. Human BCA-1 shares a 64% amino acid sequence similarity with the mouse protein and 23 - 34% amino acid sequence identity with other known CXC chemokines. Recombinant or chemically synthesized BCA1 is a potent chemoattractant for B lymphocytes but not T lymphocytes, monocytes or neutrophils. BLR1, a G protein-coupled receptor originally isolated from Burkitt’s lymphoma cells, has now been shown to be the specific receptor for BCA1. Among cells of the hematopoietic lineages, the expression of BLR-1, now designated CXCR-5, is restricted to B lymphocytes and a subpopulation of T helper memory cells.

    • Synonyms

      C-X-C motif chemokine 13, B lymphocyte chemoattractant, CXC chemokine BLC, Small-inducible cytokine B13, Cxcl13, Blc, Scyb13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BCA1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BCA1 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.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

    • Background

      What is the molecular weight/Mw of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein has a total Mw of 10kDa.

      What is the source or expression system of CXCL13 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL13 MOUSE Protein?
      CXCL13 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL13 MOUSE Protein?
      The ED50, as measured by its ability to chemoattract human CXCR5-transfected mouse BaF3 cells, is less than 2µg/ml.

      What is the amino acid sequence of CXCL13 MOUSE Protein?
      ILEAHYTNLK CRCSGVISTV VGLNIIDRIQ VTPPGNGCPK TEVVIWTKMK KVICVNPRAK WLQRLLRHVQ SKSLSSTPQA PVSKRRAA.

      What applications can CXCL13 MOUSE Protein be used in?
      CXCL13 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL13 MOUSE Protein?
      The endotoxin level is minimal, CXCL13 MOUSE 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.

    Bca 1 Mouse
  • View Data Sheet

    Name :

    IL 16 Human, His

    Description:

    Interleukin-16 Human Recombinant, His Tag

    IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    Product # :

    CYT-562

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    Description

    Interleukin-16 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain (502-631 a.a) containing 150 amino acids and having a molecular mass of 15.5kDa. The IL-16 is fused to a 20 a.a His-Tag at N-Terminus.The IL-16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-16 His tag protein (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM PMSF & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-16 is a pleiotropic cytokine that functions as a chemoattractant, a modulator of T cell activation, and an inhibitor of HIV replication. The signaling process of IL-16 is mediated by CD4. The product of this gene undergoes proteolytic processing, which is found to yield two functional proteins. IL-16 functions exclusively attributed to the secreted C-terminal peptide, while the N-terminal product may play a role in cell cycle control. Caspase 3 is reported to be involved in the proteolytic processing of this protein. Two transcript variants encoding different isoforms have been found for this gene.
      IL-16 stimulates a migratory response in cd4+ lymphocytes, monocytes, and eosinophils. Also induces t-lymphocyte expression of interleukin 2 receptor, ligand for cd4.

    • Synonyms

      IL16, Interleukin-16, LCF, Lymphocyte Chemoattractant Factor, prIL-16, IL-16, FLJ16806, FLJ42735, FLJ44234, HsT19289.

    • Physical Appearance

      Sterile Filtered 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPDLNSSTDS AASASAASDV SVESTAEATV CTVTLEKMSAGLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETVQPGD EILQLGGTAM QGLTRFEAWN IIKALPDGPV TIVIRRKSLQ SKETTAAGDS.

    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.

    Il 16 Human His
  • View Data Sheet

    Name :

    IL 1RA Rat

    Description:

    Interleukin-1 Receptor Antagonist Rat Recombinant

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    Product # :

    CYT-152

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    Description

    IL 1RA Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.5kDa.The IL 1RA Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Measured by its ability to inhibit IL1a-dependent proliferation in D10.G4.1 mouse helper T cells. The ED50 for this effect is typically 30-150ng/ml (corresponding to a specific activity of 6,667-33,334units/mg ) in the presence of 50pg/ml of rrIL1a.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, MGC10430.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 1RA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 1RA should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IL 1RA in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HPAGKRPCKM QAFRIWDTNQ KTFYLRNNQL IAGYLQGPNT KLEEKIDMVP IDFRNVFLGI HGGKLCLSCV KSGDDTKLQL EEVNITDLNK NKEEDKRFTF IRSETGPTTS FESLACPGWF LCTTLEADHP VSLTNTPKEP CTVTKFYFQE DQ

    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.

    Il 1Ra Rat
  • View Data Sheet

    Name :

    SARS MERS Spike S1

    Description:

    Mouse Anti SARS MERS Spike S1

    Product # :

    ANT-766

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    Description

    SARS MERS Spike-S1 antibody is specific for the S1 domain of the spike protein of the MERS virus.

    Formulation

    1mg/ml in PBS and 0.1% NaN3.

    Purity

    Greater than 90% as determined by SDS-PAGE gel.

    More Info

    • Introduction

      SARS Coronavirus is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. Spike (S)-glycoprotein of the virus interacts with a cellular receptor and mediates membrane fusion to allow viral entry into susceptible target cells. Accordingly, S-protein plays an important role in virus infection cycle and is the primary target of neutralizing antibodies.It has recently been shown that SARS is caused by a human coronavirus. Human coronaviruses are the major cause of upper respiratory tract illness in humans, such as the common cold. Coronaviruses are positive-stranded RNA viruses, featuring the largest viral RNA genomes known to date (27-31 kb). The first step in coronavirus infection is binding of the viral spike protein, a 139-kDa protein, to certain receptors on host cells. The spike protein is the main surface antigen of the coronavirus. The most prominent protein in the culture supernatants infected with SARS virus is a 46 kDa nucleocapsid protein. This suggests that the nucleocapsid protein is a major immunogen that may be useful for early diagnostics.

    • Physical Appearance

      Sterile Filtered liquid formulation.

    • Stability

      Store at 4°C, stable for 2 weeks. For long-term storage, store at -20°C.

    • Applications

      ELISA.

    • Isotype

      IgG1.

    • Type

      Mouse antibody Monoclonal.

    • Purification Method

      Protein A affinity purified.

    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.

    Cov Mers Antibody
  • View Data Sheet

    Name :

    CoV-2 S1, Sf9

    Description:

    Coronavirus 2019 Spike Glycoprotein-S1 Sf9, Recombinant

    Product # :

    SARS-019

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    Description

    The Sf9 derived recombinant protein contains the Coronavirus 2019 CoV-2 Spike Glycoprotein S1, Wuhan-Hu-1 strain, amino acids 1-674 fused to His tag at C-terminal.

    Source

    Sf9, Baculovirus Cells.

    Formulation

    CoV-2 S1 protein solution is supplied in DPBS.

    Purity

    Protein is >85% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CoV-2 S1 Glycoprotein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      Purified by Metal-Afinity 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.

    product_image.jpg
  • View Data Sheet

    Name :

    IL1A Human

    Description:

    Interleukin-1 alpha Human Recombinant

    Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    Product # :

    CYT-253

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    Description

    Interleukin-1 alpha Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 159 amino acids and having a molecular mass of 18022 Dalton. The IL-1A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 25mM Tris-HCl, pH 8.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

    More Info

    • Introduction

      IL-1 alpha is produced by activated macrophages, stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1A proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Hematopoietin-1, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL-1 alpha,IL1, IL-1A, IL1F1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1 alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 1 alpha in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

    • Background

      What is the molecular weight/Mw of IL1A HUMAN Protein?
      IL1A HUMAN Protein has a total Mw of 18kDa.

      What is the source or expression system of IL1A HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL1A HUMAN Protein?
      IL1A HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1A HUMAN Protein?
      The ED50 as determined by the dose-dependant stimulation of murine D10S cells is < 0.001 ng/ml, corresponding to a Specific Activity of 1 x 109 IU/mg.

      What is the amino acid sequence of IL1A HUMAN Protein?
      SAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAV KFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITG SETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILE NQA.

      What applications can IL1A HUMAN Protein be used in?
      IL1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1A HUMAN Protein?
      The endotoxin level is minimal, IL1A HUMAN Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.13 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IL-1 as a Reference Standard.

    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.

    Il 1 Alpha Human
  • View Data Sheet

    Name :

    IL 11 Human, Pichia

    Description:

    Interleukin-11 Human Recombinant, Pichia

    Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    Product # :

    CYT-013

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    • More Info

    Description

    IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.

    More Info

    • Introduction

      IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

    • Synonyms

      Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin -11 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.

    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.

    Il 11 Human Pichia
  • View Data Sheet

    Name :

    IL33 Mouse, His

    Description:

    Interleukin-33 Mouse Recombinant, His Tag

    9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.

    Product # :

    CYT-847

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    Description

    IL33 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (109-266 a.a) and having a molecular mass of 18.1kDa.IL33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL33 protein solution (0.5mg/ml) containing Phosphate buffered saline,10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ 0.1ng/ml.

    More Info

    • Introduction

      Interleukin 33 (IL-33) is a 32kDa proinflammatory cytokine that may also regulate gene transcription in producer cells. IL-33 is structurally related to IL-1, which induces helper T cells to produce type 2 cytokines and acts through the receptor IL1RL-1 (IL1 receptor-like-1), which is known also as ST2. Binding of IL-33 to this receptor activates NF-kappa-B and MAP kinases and induces in vitro Th2 cells to produce cytokines. In vivo, IL-33 induces expression of IL-4, IL-5, IL-13 and leads to severe pathological changes in mucosal organs and in vitro, it can be divided to N-terminal fragment of 12kDa and C-terminal fragment of 18kDa by cleavage of caspase-1.

    • Synonyms

      9230117N10Rik, Il-33, Il1f11, NF-HEV, Interleukin-33.

    • 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. 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 MGSSIQGTSL LTQSPASLST YNDQSVSFVL ENGCYVINVD DSGKDQEQDQ VLLRYYESPC PASQSGDGVD GKKLMVNMSP IKDTDIWLHA NDKDYSVELQ RGDVSPPEQA FFVLHKKSSD FVSFECKNLP GTYIGVKDNQ LALVEEKDES CNNIMFKLSK I.

    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.

    Il33 Mouse His
  • View Data Sheet

    Name :

    TRAIL Human (114-281 a.a.), Active

    Description:

    TRAIL/APO 2 Ligand (114-281 a.a.) Human Recombinant, Active

    Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    Product # :

    CYT-1014

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    Description

    Soluble TNF-related apoptosis-inducing ligand Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (114-281) and having a molecular mass of 19.6 kDa. The sTRAIL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TRAIL protein solution (1mg/ml) containing 20mM Tris-HCl pH-7.5, 300mM NaCl, 0.1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell cytotoxicity assay using Jurkat human T lymphocyte. The ED50 for this effect is less or equal to 1 ng/ml.

    More Info

    • Introduction

      TNF-related apoptosis-inducing ligand (TRAIL) is a ligand molecule which induces apoptosis. It is a type II transmembrane protein with homology to other members of the tumor necrosis factor family.
      In humans, the gene that encodes for TRAIL is located at chromosome 3q26.
      TRAIL binds to the death receptors, DR4 and DR5. The process of apoptosis is caspase-8-dependent. This protein preferentially induces apoptosis in transformed and tumor cells, but does not appear to kill normal cells although it is expressed at a significant level in most normal tissues.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 10, TNF-related apoptosis-inducing ligand, Protein TRAIL, Apo-2 ligand, Apo-2L, CD253 antigen, TL2, APO2L, TNFSF10.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • 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

      MVRERGPQRV AAHITGTRGR SNTLSSPNSK NEKALGRKIN SWESSRSGHS FLSNLHLRNGELVIHEKGFY YIYSQTYFRF QEEIKENTKN DKQMVQYIYK YTSYPDPILL MKSARNSCWSKDAEYGLYSI YQGGIFELKE NDRIFVSVTN EHLIDMDHEA SFFGAFLVG.

    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.

    Trail Human 114 281 Aa Active
  • View Data Sheet

    Name :

    LY9 Human

    Description:

    Lymphocyte Antigen 9 Human Recombinant

    Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.

    Product # :

    PRO-2338

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    LY9 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 416 amino acids (48-454 aa) and having a molecular mass of 45.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LY9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    LY9 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.

    • Synonyms

      Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.

    • 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

      ADLKDSAPTV VSGILGGSVT LPLNISVDTE IENVIWIGPK NALAFARPKE NVTIMVKSYL GRLDITKWSY SLCISNLTLN DAGSYKAQIN QRNFEVTTEE EFTLFVYEQL QEPQVTMKSV KVSENFSCNI TLMCSVKGAE KSVLYSWTPR EPHASESNGG SILTVSRTPC DPDLPYICTA QNPVSQRSSL PVHVGQFCTD PGASRGGTTG ETVVGVLGEP VTLPLALPAC RDTEKVVWLF NTSIISKERE EAATADPLIK SRDPYKNRVW VSSQDCSLKI SQLKIEDAGP YHAYVCSEAS SVTSMTHVTL LIYRRLRKPK ITWSLRHSED GICRISLTCS VEDGGNTVMY TWTPLQKEAV VSQGESHLNV SWRSSENHPN LTCTASNPVS RSSHQFLSEN ICSGPERNTK 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.

    Ly9 Human
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