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1000 results found for “Other Cytokines”

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  • View Data Sheet

    Description:

    Interleukin-33 Human Recombinant, His Tag

    Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.

    Product # :

    CYT-667

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    Description

    Interleukin-33 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 159 amino acids C-terminal fragment (112-270) having a molecular weight of 22.49kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The IL-33 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-33 protein solution is supplied in 10mM Tris-HCl pH 8.0, 180mM NaCl and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    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

      Interleukin 33, DVS27, NF-HEV, NKHEV, C9orf26, Interleukin-1 family member 11, IL- 1F11, Nuclear factor from high endothelial venules, NFEHEV, DKFZp586H0523, RP11-575C20.2, IL-33, IL33.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 33 Human His
  • View Data Sheet

    Description:

    Interleukin 12 Receptor Beta 1 Human Recombinant, Sf9

    Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.

    Product # :

    CYT-894

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    • SDS-PAGE

    Description

    IL12RB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-545 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 528 amino acids and having a molecular mass of 58.4kDa.IL12RB1 shows multiple bands between 50-70kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL12RB1 protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4), 30% glycerol, 1mM EDTA and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

    • Synonyms

      Interleukin 12 Receptor, Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R, IL12RB1.

    • 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

      CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH

    • Background

      What is the molecular weight/Mw of IL12RB1 HUMAN, SF9 Protein?
      IL12RB1 HUMAN, SF9 Protein has a total Mw of 58.4kDa.

      What is the source or expression system of IL12RB1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL12RB1 HUMAN, SF9 Protein?
      IL12RB1 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12RB1 HUMAN, SF9 Protein?
      The biological functionality of IL12RB1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of IL12RB1 HUMAN, SF9 Protein?
      CRTSECCFQD PPYPDADSGS ASGPRDLRCY RISSDRYECS WQYEGPTAGV SHFLRCCLSS GRCCYFAAGS ATRLQFSDQA GVSVLYTVTL WVESWARNQT EKSPEVTLQL YNSVKYEPPL GDIKVSKLAG QLRMEWETPD NQVGAEVQFR HRTPSSPWKL GDCGPQDDDT ESCLCPLEMN VAQEFQLRRR QLGSQGSSWS KWSSPVCVPP ENPPQPQVRF SVEQLGQDGR RRLTLKEQPT QLELPEGCQG LAPGTEVTYR LQLHMLSCPC KAKATRTLHL GKMPYLSGAA YNVAVISSNQ FGPGLNQTWH IPADTHTEPV ALNISVGTNG TTMYWPARAQ SMTYCIEWQP VGQDGGLATC SLTAPQDPDP AGMATYSWSR ESGAMGQEKC YYITIFASAH PEKLTLWSTV LSTYHFGGNA SAAGTPHHVS VKNHSLDSVS VDWAPSLLST CPGVLKEYVV RCRDEDSKQV SEHPVQPTET QVTLSGLRAG VAYTVQVRAD TAWLRGVWSQ PQRFSIEVQV SDHHHHHH
      What applications can IL12RB1 HUMAN, SF9 Protein be used in?
      IL12RB1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12RB1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL12RB1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12RB1 HUMAN, SF9 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 IL12RB1 HUMAN, SF9?
      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.

    Il12Rb1 Human Sf9
  • View Data Sheet

    Description:

    Interleukin 12 His Tag Human Recombinant

    23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    Product # :

    CYT-846

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    • SDS-PAGE

    Description

    IL12 Human Recombinant produced in a baculovirus expression system is a glycosylated disulfide linked (through cysteines in bold) heterodimer comprised of IL12A (23-219aa, total of 203 aa, MW 23.3kDa) and IL12B (23-328aa, total of 306 aa, MW 34.6kDa), having a total predicted molecular mass of 57.9kDa (Molecular weight on SDS-PAGE will appear higher).IL12A is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    IL12 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

    SDS-PAGE

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    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of interferon gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. IL-12 is an initiator of cell-mediated immunity.

    • Synonyms

      23-219aa (IL12A) / 23-328aa (IL12B), Interleukin 12 (subunit beta/alpha), IL12 His, NKSF1, NKSF, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor (CLMF), TSF, Edodekin-alpha, IL-12.

    • 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

      IL12A(p35):
      RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.

      IL12B(p40):
      IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

    • Background

      What is the molecular weight/Mw of IL12 HUMAN, HIS Protein?
      IL12 HUMAN, HIS Protein has a total Mw of 57.9kDa.

      What is the source or expression system of IL12 HUMAN, HIS Protein?
      Baculovirus.
      What is the Purity of IL12 HUMAN, HIS Protein?
      IL12 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12 HUMAN, HIS Protein?
      The activity is determined by the IFN-g ELISA in a using NK-92 cell. The ED50 for this effect is less than or equal to 0.03 ng/ml.

      What is the amino acid sequence of IL12 HUMAN, HIS Protein?
      IL12A(p35):
      RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNASHHH HHH.
      IL12B(p40):
      IWELKKDVYV VELDWYPDAP GEMVVLTCDT PEEDGITWTL DQSSEVLGSG KTLTIQVKEF GDAGQYTCHK GGEVLSHSLL LLHKKEDGIW STDILKDQKE PKNKTFLRCE AKNYSGRFTC WWLTTISTDL TFSVKSSRGS SDPQGVTCGA ATLSAERVRG DNKEYEYSVE CQEDSACPAA EESLPIEVMV DAVHKLKYEN YTSSFFIRDI IKPDPPKNLQ LKPLKNSRQV EVSWEYPDTW STPHSYFSLT FCVQVQGKSK REKKDRVFTD KTSATVICRK NASISVRAQD RYYSSSWSEW ASVPCS.

      What applications can IL12 HUMAN, HIS Protein be used in?
      IL12 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12 HUMAN, HIS Protein?
      The endotoxin level is minimal, IL12 HUMAN, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12 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 IL12 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.

    Il12 Human His
  • View Data Sheet

    Description:

    Resistin Mouse Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1034

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    Description

    Resistin Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 95 amino acids and having a total molecular mass of 20.6kDa. The Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSSMPLCPID EAIDKKIKQD FNSLFPNAIK NIGLNCWTVS SRGKLASCPE GTAVLSCSCG SACGSWDIRE EKVCHCQCAR IDWTAARCCK LQVAS.

    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.

    Mouse Resistin
  • View Data Sheet

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

    Product # :

    CYT-077

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    • sds-page

    Description

    BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Synonyms

      Betacellulin, Probetacellulin.

    • 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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 11.3kDa.

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

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

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

      What is the amino acid sequence of BETACELLULIN Protein?
      MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

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

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

    Btc His Human
  • View Data Sheet

    Description:

    Interleukin-21 Canine Recombinant

    Interleukin-21.

    Product # :

    CYT-1181

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    Description

    IL21 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (18-146a.a.) and having a molecular mass of 15kDa.

    Source

    Escherichia Coli.

    Formulation

    IL21 protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IFN-g ELISA in a using NK-92 human natural killer cells. The ED50 range ≤ 2ng/ml.

    More Info

    • Introduction

      Interleukin-21 isoform 1 or IL21, categorized as a T helper cytokine. IL21 is part of the regulation of immune responses, haematopoiesis and cell-mediated responses. IL21 takes a main part in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21 which has an important role in the viral infections persistence.

    • Synonyms

      Interleukin-21.

    • 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

      MHKSSFQEQD LLLIRMRQLI DIVDQLKNYV NDLDPESLPA PEDVKRHCER SAFSCFQKVQ LKAANTGGNE QIINVLTKQL KRKLPPTNAG RRQKHRPACP SCDSYEKAPP KEFLERLKSL IQKMIHQHLS

    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.

    Il21 Canine
  • View Data Sheet

    Description:

    Interleukin-6 Mouse Recombinant, His Tag

    Interleukin-6, IL-6.

    Product # :

    CYT-845

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    • SDS-PAGE

    Description

    Interleukin-6 Mouse Recombinant produced in E.Coli migrates at 25kDa. Recombinant IL-6 Mouse is fused to a 6xHis tag at C-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    IL6 Mouse protein solution contains 25mM K2CO3 and PBS.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    SDS-PAGE

    More Info

    • Introduction

      Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.

    • Synonyms

      Interleukin-6, IL-6.

    • 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.

    • Background

      Research Paper on Interleukin-6 Mouse Recombinant, His Tag

      Abstract:

      Interleukin-6 (IL-6) Mouse Recombinant, tagged with His, is a cornerstone in unraveling the intricate web of immune modulation. This research paper delves into its molecular intricacies and its profound implications in immunological research. Through an exploration of its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its pivotal role in shaping immune responses.

      Introduction:

      IL-6 Mouse Recombinant, bearing a His tag, has emerged as a pivotal tool in immunological studies. This paper aims to provide a comprehensive understanding of its molecular attributes and its impact on immune mechanisms.

      Molecular Features and His Tag Precision:

      Unveiling the molecular structure of IL-6 Mouse Recombinant, His Tag, we recognize its significance in facilitating purification and characterization. The His tag enhances our ability to study its functions with precision.

      Navigating Immune Responses:

      IL-6 plays a vital role in immune cell activation and inflammation. IL-6 Mouse Recombinant, His Tag, enables researchers to delve deeper into the cytokine's functions, shedding light on its impact on immune dynamics.

      Synonyms and Network Connections:

      Understanding the synonyms linked to IL-6, such as DIF, TNFA, and TNFSF2, enriches our comprehension of cytokine-mediated signaling networks. IL-6 Mouse Recombinant, His Tag, contributes to our understanding of these interconnected pathways.

      Potential Applications in Research and Therapy:

      Beyond laboratory research, IL-6 Mouse Recombinant, His Tag, holds therapeutic promise for immune-related disorders. Its utility in investigating disease mechanisms and evaluating therapeutic interventions marks it as a versatile tool.

      Clinical Implications and Future Avenues:

      The clinical relevance of IL-6 Mouse Recombinant, His Tag, is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its potential as a therapeutic intervention opens avenues for novel treatment strategies.

      Conclusion:

      In the intricate realm of immunology, IL-6 Mouse Recombinant, His Tag, stands as a valuable asset in understanding immune responses. Its molecular precision, pivotal functions, and potential therapeutic implications position it as an indispensable tool for advancing our knowledge of immune regulation.

      What is the molecular weight/Mw of IL6 MOUSE, HIS Protein?
      IL6 MOUSE, HIS Protein has a total Mw of 25kDa.

      What is the source or expression system of IL6 MOUSE, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL6 MOUSE, HIS Protein?
      IL6 MOUSE, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 MOUSE, HIS Protein?
      The biological functionality of IL6 MOUSE, HIS Protein will be determined in the future.

      What applications can IL6 MOUSE, HIS Protein be used in?
      IL6 MOUSE, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6 MOUSE, HIS Protein?
      The endotoxin level is minimal, IL6 MOUSE, HIS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6 MOUSE, 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 IL6 MOUSE, 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.

    Il 6 His Mouse
  • View Data Sheet

    Description:

    Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag

    CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    Product # :

    CYT-032

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    Description

    TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.

    • Synonyms

      CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

    • 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 MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.

    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.

    Taci Human
  • View Data Sheet

    Description:

    RELM-Gamma Mouse Recombinant, His Tag

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    Product # :

    CYT-455

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    Description

    RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.The lyophilized protein remains stable until the expiry date when stored at -20°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.

    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.

    Relm Gamma Mouse
  • View Data Sheet

    Description:

    Interleukin-22 Receptor Antagonist (Y51A) Mouse Recombinant

    IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    Product # :

    CYT-1239

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    Description

    IL22RA (Y51A) Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. IL22RA (Y51A) is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration chromatography.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    IL22RA (Y51A) Is capable of full inhibition of STAT3 phosphorylation induced by mouse interleukin 22 in HepG cells. Its affinity toward immobilized mIL-22 receptor α1 extracellular domain (mIL-22 Rα1-ECD) or IL-22 binding protein is similar to the non-mutated mouse interleukin 22. Mouse IL-22 antagonist (Y51A) has no agonistic activity in this bioassay.

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    • Synonyms

      IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL22RA (Y51A) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22RA (Y51A) 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 IL22RA (Y51A) in sterile 18MΩ-cm 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 Ala-Leu-Pro-Val-Asn.

    • Background

      IL-22 belongs to the IL-10 family of regulatory cytokines and produced by several populations of immune cells at a site of inflammation. Members of this family share partial homology in their amino acid sequences, but varies in their biological functions. IL-22 takes effect on non-hematopoietic cells. IL-22 takes pat in wound healing and in protection against microbs.Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the pancreas and liver.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

    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.

    Il22Ra Mouse
  • View Data Sheet

    Description:

    HVEM Human Recombinant, His Tag

    Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    Product # :

    CYT-800

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    Description

    TNFRSF14 Human Recombinant produced in E. Coli is a single, glycosylated polypeptide chain containing 187 amino acids (39-202) and having a molecular mass of 19.7kDa.TNFRSF14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TNFRSF14 solution (0.5mg/ml) containing 20mM Tris-HCl (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      TNFRSF14, a member of the TNF receptor superfamily, is a type I transmembrane protein. TNFRSF14 is expressed in peripheral blood T cells, B cells, monocytes and in various tissues enriched in lymphoid cells. TNFRSF14 operates as a co-stimulatory factor for the activation of lymphoid cells and as a deterrent to infection by herpesvirus. Additionally, TNFRSF14 encourages the proliferation of T cells, and triggers apoptosis of various tumor cells.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily Member 14, HVEM, TR2, Herpes Virus Entry Mediator A, Tumor Necrosis Factor Receptor-Like 2, Herpesvirus Entry Mediator, HVEA, ATAR, CD270, LIGHTR, CD40-Like Protein, Tumor Necrosis Factor Receptor-Like Gene2.

    • 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 MGSLPSCKED EYPVGSECCP KCSPGYRVKE ACGELTGTVC EPCPPGTYIA HLNGLSKCLQ CQMCDPAMGL RASRNCSRTE NAVCGCSPGH FCIVQDGDHC AACRAYATSS PGQRVQKGGT ESQDTLCQNC PPGTFSPNGT LEECQHQTKC SWLVTKAGAG TSSSHWV.

    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.

    Tnfrsf14 Human His
  • View Data Sheet

    Description:

    Betacellulin Human Recombinant, HEK

    Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    Product # :

    CYT-1188

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    Description

    BTC Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (32-111 a.a) containing 86 amino acids and having a molecular mass of 9.8kDa.BTC is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    BTC protein (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

    ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

    More Info

    • Introduction

      BTC is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are mediated by the EGF receptor and other related receptors.

    • Synonyms

      Betacellulin isoform 1, Probetacellulin, Betacellulin, BTC

    • 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

      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 9.8kDa.

      What is the source or expression system of BETACELLULIN Protein?
      HEK293 cells.

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

      What is the Biological Activity of BETACELLULIN Protein?
      ED50 range is ≤ 0.5ng/ml. It is measured by cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.

      What is the amino acid sequence of BETACELLULIN Protein?
      DGNSTRSPET NGLLCGDPEE NCAATTTQSK RKGHFSRCPK QYKHYCIKGR CRFVVAEQTP SCVCDEGYIG ARCERVDLFY HHHHHH

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

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

    Betacellulin Protein
  • View Data Sheet

    Description:

    Adiponectin Human Recombinant, HEK

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-434

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    • sds-page

    Description

    Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

    Purity

    Greater than 98% as determined by HPLC and SDS PAGE.

    Biological Activity

    In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

    sds-page

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°C.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product not sterile! Please filter the product by an appropriate sterile filter before using it in cell culture.

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

    • Background

      What is the molecular weight/Mw of adiponectin Protein?
      Adiponectin Protein has a total Mw of 25.5kDa.

      What is the source or expression system of adiponectin Protein?
      HEK293.

      What is the Purity of adiponectin Protein?
      adiponectin Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of adiponectin Protein?
      In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

      What is the amino acid sequence of adiponectin Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

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

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

    Adiponectin Human Hek
  • View Data Sheet

    Description:

    Granulocyte Macrophage Colony Stimulating Factor, Mouse Anti-Human

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    Product # :

    ANT-129

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    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, Molgramostin, Sargramostim, MGC131935, MGC138897.

    • Solubility

      Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      r.Human GM-CSF.

    • Ig Subclass

      Mouse IgG.

    • Clone

      NYRhGMCSF.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange Protein concentration1mg/ml in PBS (after reconstitution).

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    Gm Csf Antibody
  • View Data Sheet

    Description:

    Visfatin Recombinant Human, His Tag

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    CYT-563

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    Description

    Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 511 amino acids and having a molecular mass of 57 kDa. The recombinant human Visfatin is fused to His tag at N-Terminus.

    Source

    Escherichia Coli.

    Formulation

    Visfatin His tag protein contains 20mM Tris pH-8, 0.1mM DTT & 10% glycerol.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Excess adiposity is the most important risk in the development of insulin resistance and type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-?, and IL-6, that modulate insulin sensitivity and appear to play an important role in the pathogenesis of insulin resistance, diabetes, dyslipidemia, inflammation, and atherosclerosis. However, the mechanisms by which fat tissue induces insulin resistance and the role of adipocytokines in the pathogenesis of T2DM have not been well established.
      Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
      Visfatin exerts insulin-mimetic effects that are dose-dependent and quantitatively similar to those of insulin in stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its insulin-mimetic effects, visfatin was as effective as insulin in reducing hyperglycemia in insulin-deficient diabetic mice. Visfatin was also found to be bound to and activate insulin receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin and insulin did not compete for binding to the insulin receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Physical Appearance

      Sterile Filtered solution at a concentration of 1mg/ml.

    • 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 MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR KVKYEETVFY GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG WNYILEKYDG HLPIEIKAVP EGFVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA QLNIELEAAH H.

    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.

    Visfatin Human His
  • View Data Sheet

    Description:

    RELM-Alpha Mouse Recombinant, His Tag

    Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    Product # :

    CYT-453

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    Description

    RELM-alpha Mouse Recombinant is manufactured with a signal sequence of phage fd (20aa) and C-terminal fusion of flagTag (10aa). The RELM-alpha Flag-Tagged Fusion Protein is a 13.3 kDa protein containing 91 amino acid residues with 30 additional amino acid residues - signal sequence of phage fd, flagTag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 5mM Tris pH 7.5, 25mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
      RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
      In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMFstimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation.

    • Synonyms

      Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      Add deionized H2O and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKKLLFAIPL VVPFYSHSTM VNTDETIEII VENKVKELLA NPANYPSTVT TLSCTSVKT MNRWASCPAG MTATGCACGF ACGSWEIQSG DTCNCLCLLV DWTTARCCQL SLEDYKDDDD K.

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    Relm Alpha Mouse His
  • View Data Sheet

    Description:

    TNF Ligand Receptor Superfamily Member 21 Human Recombinant

    Tumor necrosis factor receptor superfamily member 21, BM-018, CD358, DR6, Death receptor 6.

    Product # :

    CYT-1073

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    Description

    TNFRSF21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 547 amino acids (42-349a.a.) and having a molecular mass of 60.4kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).TNFRSF21 is expressed with a 239 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF21 protein solution (1mg/ml) contains phosphate buffered saline (pH7.4),10% glycerol and 0.1 mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 21 or TNFRSF21, is a protein that located in the cell membrane from the TNF receptor superfamily. By activating the NF-kappaB pathway, TNFRSF21 promotes cell apoptosis. The degeneration of cells caused by activating caspase 3 and caspase 6, the TNFRSF21 binds to the N-terminal APP in neuronal cell bodies and axons which leads to apoptosis. TNFRSF21 takes part in signaling cascades activated by stimulation of T-cell receptor.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 21, BM-018, CD358, DR6, Death receptor 6.

    • 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

      QPEQKASNLI GTYRHVDRAT GQVLTCDKCP AGTYVSEHCT NTSLRVCSSC PVGTFTRHEN GIEKCHDCSQ PCPWPMIEKL PCAALTDREC TCPPGMFQSN ATCAPHTVCP VGWGVRKKGT ETEDVRCKQC ARGTFSDVPS SVMKCKAYTD CLSQNLVVIK PGTKETDNVC GTLPSFSSST SPSPGTAIFP RPEHMETHEV PSSTYVPKGM NSTESNSSAS VRPKVLSSIQ EGTVPDNTSS ARGKEDVNKT LPNLQVVNHQ QGPHHRHILK LLPSMEATGG EKSSTPIKGP KRGHPRQNLH KHFDINEHLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG KHHHHHH.

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    Tnfrsf21 Human
  • View Data Sheet

    Description:

    Lymphotoxin Beta Receptor Human Recombinant

    Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    Product # :

    CYT-853

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    Description

    LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.

    • Synonyms

      Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    • 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 MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

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    Ltbr Human
  • View Data Sheet

    Description:

    Desert Hedgehog (C23II) Human Recombinant

    HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    Product # :

    CYT-362

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    Description

    DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 15-45 μg/ml.

    More Info

    • Introduction

      DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
      DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development.

    • Synonyms

      HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.

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    Dhh C23Ii Human
  • View Data Sheet

    Description:

    Interleukin-6 Clone PAT1F10AT, Mouse Anti Human

    IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    Product # :

    ANT-540

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      Il-6 is a cytokine with a wide variety of biological functions: it plays an essential role in the final differentiation of b-cells into ig-secreting cells, it induces myeloma and plasmacytoma growth, it induces nerve cells differentiation, in hepatocytes it induces acute phase reactants.

    • Synonyms

      IFN-b2, B cell differentiation factor, BCDF, BSF-2, HPGF, HSF, MGI-2, B-cell stimulatory factor 2, Interferon beta-2, Hybridoma growth factor, CTL differentiation factor, CDF, IL-6, HGF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IL-6, clone PAT1F10AT mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IL-6 protein 30-212 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT1F10AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Background

      Research Paper on Interleukin-6 Clone PAT1F10AT, Mouse Anti-Human

      Abstract:

      Interleukin-6 (IL-6) Clone PAT1F10AT, a Mouse Anti-Human monoclonal antibody, plays a pivotal role in deciphering the complexities of immune modulation. This research paper provides an insightful exploration of its molecular attributes and its profound implications in immunological research. We examine its interactions, functions, and synonyms, including DIF, TNFA, and TNFSF2, shedding light on its significance in understanding immune responses.

      Introduction:

      IL-6 Clone PAT1F10AT, a Mouse Anti-Human antibody, has emerged as a cornerstone in immunology research. This paper delves into its unique characteristics and its critical role in unraveling immune mechanisms.

      Molecular Precision and Specificity:

      The exceptional affinity and specificity of IL-6 Clone PAT1F10AT for human IL-6 distinguish it as an invaluable tool for immunodetection and functional studies. Its targeted binding facilitates accurate identification of IL-6 in various experimental contexts.

      Unveiling Immune Dynamics:

      IL-6 is a central player in immune orchestration, and IL-6 Clone PAT1F10AT offers a window into its world. By investigating its involvement in immune responses, inflammation, and signaling pathways, researchers gain insights into immune regulation.

      Synonyms and Interactions:

      Understanding IL-6 synonyms, such as DIF, TNFA, and TNFSF2, underscores its intricate web of interactions. IL-6 Clone PAT1F10AT's ability to decipher these connections enhances our understanding of cytokine-mediated immune modulation.

      Disease Implications and Therapeutic Avenues:

      With its relevance in diseases like autoimmune disorders and inflammatory conditions, IL-6 Clone PAT1F10AT assumes significance in disease-focused investigations. It enables researchers to dissect disease mechanisms and evaluate potential therapeutic interventions.

      Clinical Utility and Diagnostic Precision:

      IL-6 Clone PAT1F10AT's utility transcends research settings, finding application in clinical diagnostics. Its role in immunoassays facilitates accurate disease diagnosis and monitoring, contributing to improved patient management.

      Conclusion:

      In the realm of immunology, IL-6 Clone PAT1F10AT stands as a potent ally in unraveling immune intricacies. Its molecular precision, diverse functions, and potential therapeutic implications make it a cornerstone in advancing our understanding of immune responses and diseases.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      IL-6 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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    Il 6 Pat1F10At Antibody
  • View Data Sheet

    Description:

    Interferon Alpha And Beta Receptor Mouse Recombinant

    IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

    Product # :

    CYT-994

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    • SDS-PAGE

    Description

    IFNAR1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 411 amino acids (27-429a.a) and having a molecular mass of 46.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IFNAR1 is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IFNAR1 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      Interferon Alpha And Beta Receptor, also known IFNAR1, belongs to the class II cytokine receptor family. IFNAR1 protein forms one of the two chains of a receptor for interferons alpha as well as beta. IFNAR1 binds and activates the receptor which stimulates Janus protein kinases, which in turn phosphorylate some proteins, including STAT1 & STAT2. Furthermore, IFNAR1 also functions as an antiviral factor.

    • Synonyms

      IFN-R-1, IFN-alpha/beta receptor 1, Type I interferon receptor 1, Ifar, Ifnar, Infar CD118 and Ifnar1.

    • 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

      ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

    • Background

      What is the molecular weight/Mw of IFNAR1 MOUSE Protein?
      IFNAR1 MOUSE Protein has a total Mw of 46.8kDa.

      What is the source or expression system of IFNAR1 MOUSE Protein?
      Sf9, Baculovirus cells.
      What is the Purity of IFNAR1 MOUSE Protein?
      IFNAR1 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR1 MOUSE Protein?
      The biological functionality of IFNAR1 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of IFNAR1 MOUSE Protein?
      ENLKPPENID VYIIDDNYTL KWSSHGESMG SVTFSAEYRT KDEAKWLKVP ECQHTTTTKC EFSLLDTNVY IKTQFRVRAE EGNSTSSWNE VDPFIPFYTA HMSPPEVRLE AEDKAILVHI SPPGQDGNMW ALEKPSFSYT IRIWQKSSSD KKTINSTYYV EKIPELLPET TYCLEVKAIH PSLKKHSNYS TVQCISTTVA NKMPVPGNLQ VDAQGKSYVL KWDYIASADV LFRAQWLPGY SKSSSGSRSD KWKPIPTCAN VQTTHCVFSQ DTVYTGTFFL HVQASEGNHT SFWSEEKFID SQKHILPPPP VITVTAMSDT LLVYVNCQDS TCDGLNYEII FWENTSNTKI SMEKDGPEFT LKNLQPLTVY CVQARVLFRA LLNKTSNFSE KLCEKTRPGS FSTLEHHHHH H

      What applications can IFNAR1 MOUSE Protein be used in?
      IFNAR1 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR1 MOUSE Protein?
      The endotoxin level is minimal, IFNAR1 MOUSE Protein was purified using conventional chromatography techniques.


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    Ifnar1 Mouse
  • View Data Sheet

    Description:

    Thrombopoietin Mouse Recombinant

    Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.

    Product # :

    CYT-346

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    Description

    Thrombopoietin Mouse Recombinant produced in E.Coli is a single, non-glycosylated soluble polypeptide chain containing 174 amino acids and having a molecular mass of 18704 Dalton. The TPO is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    ED50 range is less than 0.8ng/ml as determined by the dose dependent stimulation of Mo7e cells.

    More Info

    • Introduction

      Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidneyt hat regulates the production of platelets by the bone marrow. It stimulates the production and differentiation of megakaryocytes, the bone marrow cells that fragment into large numbers of platelets.

    • Synonyms

      Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thrombopoietin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TPO Mouse 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 Thrombopoietin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKF.

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    Mouse Thrombopoietin
  • View Data Sheet

    Description:

    Interleukin-10, Mouse Anti-Human

    B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    Product # :

    ANT-112

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    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      IL10 is a cytokine produced primarily by monocytes and to a lesser extent by lymphocytes. This cytokine has pleiotropic effects in immunoregulation and inflammation. It down-regulates the expression of Th1 cytokines, MHC class II Ags, and costimulatory molecules on macrophages. It also enhances B cell survival, proliferation, and antibody production. This cytokine can block NF-kappa B activity, and is involved in the regulation of the JAK-STAT signaling pathway. Knockout studies in mice suggested the function of this cytokine as an essential immunoregulator in the intestinal tract.

    • Synonyms

      B-TCGF, CSIF, TGIF, IL-10, IL10A, MGC126450, MGC126451, Cytokine synthesis inhibitory factor.

    • Solubility

      Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      r.Human IL-10.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      NYR-HIL10.

    • Titer

      By direct ELISA, 1:20,000 dilution will yield >1.0 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion excahnge.

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    Il 10 Human Antibody
  • View Data Sheet

    Description:

    Beta Defensin 118 Human Recombinant

    Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    Product # :

    CYT-714

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    • sds-page

    Description

    DEFB118 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (21-123 a.a) and having a molecular mass of 13.8kDa.DEFB118 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB118 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Beta Defensin 118 (DEFB118) which is a member of the beta subfamily of defensins, is found in a cluster with other beta-defensin genes on the long arm of chromosome 20. Beta-defensins are antimicrobial peptides which provide protection for tissues and organs from infection by a diversity of microorganisms. DEFB118 protein’s expression is regulated by androgen, and the encoded protein binds to sperm and exhibits antibacterial activity.

    • Synonyms

      Beta Defensin 118, Beta-defensin 18, DEFB-18, Defensin, beta 118, Epididymal secretory protein 13.6, ESP13.6, DEFB118, C20orf63, DEFB18, ESC42, Beta-defensin 118 precursor.

    • 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 MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

    • Background

      Title: Beta Defensin 118 Human Recombinant: Exploring its Role in Innate Immunity and Potential Therapeutic Applications

      Abstract:


      Beta defensin 118 (BD118) is a member of the beta defensin family, known for its antimicrobial properties and immune-modulatory functions. This research paper provides a comprehensive analysis of human recombinant BD118, focusing on its production, characterization, and potential applications in immune modulation and therapeutic interventions. The paper highlights the significance of BD118 in innate immunity and its role in host defense against microbial pathogens. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD118 in various inflammatory and infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD118 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Beta defensin 118 (BD118) is a small cationic peptide that plays a critical role in the innate immune response against microbial pathogens. Human recombinant BD118, generated through genetic engineering techniques, offers a valuable tool for studying its immune-modulatory properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD118 is typically produced using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD118.

      Role in Innate Immunity:


      BD118 exhibits antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Additionally, it possesses immune-modulatory functions, such as the regulation of pro-inflammatory responses and the promotion of wound healing. Recombinant BD118 serves as a valuable tool for investigating the mechanisms underlying its immune-modulatory actions and exploring its potential as an immunotherapeutic agent.

      Therapeutic Implications:


      Dysregulation of the immune system is associated with various inflammatory and infectious diseases. Recombinant BD118 holds promise as a potential therapeutic agent due to its antimicrobial properties and immune-modulatory functions. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD118 in conditions such as skin infections, respiratory diseases, and inflammatory bowel disease.

      Conclusion:


      Human recombinant BD118 represents a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune modulation contribute to our understanding of innate immunity and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD118 offer promising avenues for improving outcomes in inflammatory and infectious diseases.

      What is the molecular weight/Mw of DEFB118 Protein?
      DEFB118 Protein has a total Mw of 13.8kDa.

      What is the source or expression system of DEFB118 Protein?
      Escherichia Coli.

      What is the Purity of DEFB118 Protein?
      DEFB118 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB118 Protein?
      The biological functionality of DEFB118 Protein will be determined in the future.

      What is the amino acid sequence of DEFB118 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSYSGEKKC WNRSGHCRKQ CKDGEAVKDT CKNLRACCIP SNEDHRRVPA TSPTPLSDST PGIIDDILTV RFTTDYFEVS SKKDMVEESE AGRGTETSLP NVHHSS.

      What applications can DEFB118 Protein be used in?
      DEFB118 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB118 Protein?
      The endotoxin level is minimal, DEFB118 Protein was purified using conventional chromatography techniques.

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    Defb118 Human