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Search results

727 results found for “Fractalkine (CX3CL1)”

Name

Description

Product #

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  • View Data Sheet

    Name :

    IL 12 p40 Human

    Description:

    Interleukin-12 p40 Human Recombinant

    NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    Product # :

    CYT-488

    Price :

    Quantity :

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    • description
    • source
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    Description

    Interleukin-12 p40 His Human Recombinant produced in E.Coli is single, a non-glycosylated, polypeptide chain containing 306 amino acids fragment (23-328) with an amino-terminal hexahistidine tag. The IL-12 p40 His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin-12 p40 His is supplied in 1xPBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.

    • Synonyms

      NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    • 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 12 P40 Human His
  • View Data Sheet

    Name :

    IL 31 Human

    Description:

    Interleukin-31 Human Recombinant

    Interleukin 31, IL31, IL-31.

    Product # :

    CYT-625

    Price :

    Quantity :

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    • description
    • source
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    Description

    IL-31 human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids (24-164 a.a.) and having a molecular mass of 15.8 kDa.

    Source

    Escherichia Coli.

    Formulation

    The IL-31 (1mg/ml) was lyophilized with 20mM Phosphate buffer, 150mM NaCl pH-7.4.

    Purity

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

    Biological Activity

    The ED50 was determined by its ability to activate STAT following receptor ligand interaction and found to be <5ng/ml, corresponding to a specific activity of 200,000 units.

    More Info

    • Introduction

      IL-31 produced by activated Th2-type T cells, cooperates with a heterodimeric receptor consisting of IL-31 Receptor Anatagonist and Onconstatin-M Receptor that is continuesly expressed on epithelial cells and keratinocytes. IL-31 plays a role in the promotion of allergic skin disorders and in regulating other allergic diseases, such as asthma. IL-31 is involved in the itching sensation and endorses the scratching behavior in NC/Nga mice with atopic dermatitis. IL-31 expression is connectd with CLA(+) T cells and contributes to the development of atopic dermatitis-induced skin inflammation and pruritus. IL-31 is a powerful inducer of proinflammatory mediators in human colonic SEMFs. IL-31 takes part as a proinflammatory cytokine derived from Th2 cells.
      Serum IL-31 level is higher in patients with atopic dermatitis. IL-31 is involved in a broad range of immune- & non-immune cells & possesses potential pleiotropic physiological functions, including regulating hematopoiesis & immune response, causing inflammatory bowel disease, airway hypersensitivity & dermatitis.

    • Synonyms

      Interleukin 31, IL31, IL-31.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-31 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-31 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-31 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHTLPVRLLR PSDDVQKIVE ELQSLSKMLL KDVEEEKGVL VSQNYTLPCL SPDAQPPNNI HSPAIRAYLK TIRQLDNKSV IDEIIEHLDK LIFQDAPETN ISVPTDTHEC KRFILTISQQ FSECMDLALK SLTSGAQQAT T.

    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 31 Human
  • View Data Sheet

    Name :

    IL 4 Rhesus Macaque

    Description:

    Interleukin-4 Rhesus Macaque Recombinant

    Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.

    Product # :

    CYT-172

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    IL-4 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 129 amino acids and having a molecular mass of 14.9kDa.The IL4 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, 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-dependent stimulation of TF1 cells is less than 0.2ng/ml, corresponding to a specific activity of >5.0×106 IU/mg.

    More Info

    • Introduction

      IL4 is a pleiotropic cytokine produced by activated T cells. IL4 is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. This gene, IL3, IL5, IL13, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL13. IL4, IL13 and IL5 are found to be regulated coordinately by several long-range regulatory elements in an over 120 kilobase range on the chromosome. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

    • Synonyms

      Interleukin-4, IL-4, B-cell stimulatory factor 1, BSF-1, Lymphocyte stimulatory factor 1, IL4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL4 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 Interleikin-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HNCHIALREI IETLNSLTEQ KTLCTKLTIT DILAASKNTT EKETFCRAAT VLRQFYSHHE KDTRCLGATA QQFHRHKQLI RFLKRLDRNL WGLAGLNSCP VKEANQSTLE DFLERLKTIM REKYSKCSS.

    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 4 Rhesus Macaque
  • View Data Sheet

    Name :

    IL1RA Mouse, His Active

    Description:

    Interleukin-1 Receptor Antagonist Mouse Recombinant, Active His Tag

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    Product # :

    CYT-1136

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    IL1RA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (27-178 aa) and having a molecular mass of 20kDa.IL1RA is fused to a 25 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL1RA solution (1 mg/ml) contains 10% Glycerol, 20mM Tris-HCl buffer (pH 8.0) and 0.1M NaCl

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by the ability to inhibit proliferation using D10.G4.1 mouse helper T cells. ED50 for this effect is ≤ 60 ng/ml with Mouse IL-1 alpha.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. IL1RAinhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. IL1RAand 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.

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    • 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 MGSHMRPSGK RPCKMQAFRI WDTNQKTFYL RNNQLIAGYL
      QGPNIKLEEK IDMVPIDLHS VFLGIHGGKL CLSCAKSGDD IKLQLEEVNI TDLSKNKEED
      KRFTFIRSEK GPTTSFESAA CPGWFLCTTL EADRPVSLTN TPEEPLIVTK FYFQEDQ

    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.

    Il1Ra Mouse
  • View Data Sheet

    Name :

    IL22RA (Y51A) Human

    Description:

    Interleukin-22 Receptor Antagonist (Y51A) Human Recombinant

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

    Product # :

    CYT-1252

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    IL22RA (Y51A) Human 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. Human IL-22 antagonist (Y51A) has no agonistic activity in this bioassay.

    More Info

    • 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-Pro-Ile-Ser-Ser.

    • Background

      IL-22 is a part of the IL-10 family of regulatory cytokines and produced by a few 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 effects on non-hematopoietic cells. IL-22 responsible for wound healing and takes part 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 Human
  • View Data Sheet

    Name :

    IL36A Mouse

    Description:

    Interleukin-36 Alpha Mouse Recombinant

    Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    Product # :

    CYT-162

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    Description

    IL36A Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 21.0kDa.The IL36A 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 SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA to bind recombinant mouse IL-1 Rrp2.

    More Info

    • Introduction

      Murine IL-36a belongs to the IL-1 family that includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36ra (IL1F5), IL-36b (IL1F8), IL-36g (IL1F9), IL-37 (IL1F7) and IL-38 (IL-1F10). The IL-1 family members display a 12 b-strand, b-trefoil configuration, and are thought to have ascended from a mutual ancestral gene. Murine IL-36a is a 160 amino acid intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. IL-36a is released as a reaction to LPS and the cell ATP-induced activation of the P2X7 receptor.
      Mouse to human, full length IL-36a/IL-1F6 shares 54% aa sequence homology. IL-36a is mostly found in skin and lymphoid tissues, but also in fetal brain, trachea, stomach and intestine.

    • Synonyms

      Interleukin 36 alpha, FIL1E, IL1F6, FIL1, IL1(EPSILON), interleukin 1 family member 6 (epsilon), MGC129552, MGC129553.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36A Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36A 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 IL36A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MNKEKELRAA SPSLRHVQDL SSRVWILQNN ILTAVPRKEQ TVPVTITLLP CQYLDTLETN RGDPTYMGVQ RPMSCLFCTK DGEQPVLQLG EGNIMEMYNK KEPVKASLFY HKKSGTTSTF ESAAFPGWFI AVCSKGSCPL ILTQELGEIF ITDFEMIVVH

    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.

    Il36A Mouse
  • View Data Sheet

    Name :

    CD276 Human

    Description:

    CD276 Human Recombinant

    CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-2.

    Product # :

    PRO-2456

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    Description

    CD276 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (29-466a.a.) and having a molecular mass of 48.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CD276 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD276 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CD276, belongs to the B7 family of immunoregulatory transmembrane glycoproteins expressed by T cells. CD276 is a costimulatory molecule for T cell activation in addition to IFN-gamma production. Furthermore CD276 upregulates BRCC3 expression, preventing DNA defects caused by 5-Fu. CD276 is correlated with TNM stage of NSCLC and act as a potential biomarker for NSCLC-derived MPEs. CD276 inhibits natural-killer mediated cell lysis in tumor cells, and act as a marker for detection of neuroblastoma cells. CD276 is implicated in the development of acute as well as chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. In addition, CD276 provides the placenta & fetus a proper immunological environment during the course of pregnancy.

    • Synonyms

      CD276 Molecule, CD276 Antigen, Costimulatory Molecule, B7 Homolog 3, 4Ig-B7-H3, B7-H3, B7H3, B7RP-2.

    • 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

      LEVQVPEDPV VALVGTDATL CCSFSPEPGF SLAQLNLIWQ LTDTKQLVHS FAEGQDQGSA YANRTALFPD LLAQGNASLR LQRVRVADEG SFTCFVSIRD FGSAAVSLQV AAPYSKPSMT LEPNKDLRPG DTVTITCSSY QGYPEAEVFW QDGQGVPLTG NVTTSQMANE QGLFDVHSIL RVVLGANGTY SCLVRNPVLQ QDAHSSVTIT PQRSPTGAVE VQVPEDPVVA LVGTDATLRC SFSPEPGFSL AQLNLIWQLT DTKQLVHSFT EGRDQGSAYA NRTALFPDLL AQGNASLRLQ RVRVADEGSF TCFVSIRDFG SAAVSLQVAA PYSKPSMTLE PNKDLRPGDT VTITCSSYRG YPEAEVFWQD GQGVPLTGNV TTSQMANEQG LFDVHSVLRV VLGANGTYSC LVRNPVLQQD AHGSVTITGQ PMTFPPEALE HHHHHH.

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    Cd276 Human
  • View Data Sheet

    Name :

    LECT2 Human

    Description:

    Leukocyte Cell-Derived Chemotaxin 2 Human Recombinant

    Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.

    Product # :

    PRO-2037

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    Description

    LECT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gly19-Leu151) containing 143 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 16kDa.

    Source

    Escherichia Coli.

    Formulation

    LECT2 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl & pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukocyte Cell-Derived Chemotaxin 2 (LECT2) functions as a chemotactic factor to neutrophils. LECT2 stimulates the proliferation of chondrocytes and osteoblasts. LECT2 is strongly expressed in the liver and weakly in the testis. LECT2 is a secreted, 16kDa protein which serves as a chemotactic factor to neutrophils and stimulates the growth of chondrocytes and osteoblasts. LECT2 protein has a high sequence similarity to the chondromodulin repeat regions of the chicken myb-induced myeloid 1 protein. A polymorphism in the LECT2 gene is linked with rheumatoid arthritis.

    • Synonyms

      Leukocyte Cell-Derived Chemotaxin 2, Leukocyte Cell-Derived Chemotaxin-2, Chondromodulin-II, Chm-II, LECT-2, HLECT2, Chm2, LECT2.

    • 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

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. LECT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASGPWANICAGK SSNEIRTCDR HGCGQYSAQR SQRPHQGVDI LCSAGSTVYA PFTGMIVGQE KPYQNKNAIN NGVRISGRGF CVKMFYIKPI KYKGPIKKGE KLGTLLPLQK VYPGIQSHVH IENCDSSDPT AYL.

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    Lect2 Human
  • View Data Sheet

    Name :

    UPK3A Human

    Description:

    Uroplakin 3A Human Recombinant

    Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.

    Product # :

    PRO-988

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    Description

    UPK3A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (19-207 a.a.) and having a molecular mass of 23.1kDa.UPK3A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    UPK3A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPK3A is a member of the uroplakin-3 family. Uroplakins (UP) which are transmembrane proteins are important components of the urothelium that pass the lipid bilayer once (UPII, UPIIIa, and UPIIIb) or four times (UPIa and UPIb; both members of the "tetraspanin" family). All hold great luminal/extracellular domains, but only UPIIIa and UPIIIb have significant cytoplasmic shares in their C-termini. UPK3A is an extremely specific and moderately sensitive immunohistochemical marker for primary and metastatic urothelial carcinomas. Alterations in this gene are related to renal adysplasia.

    • Synonyms

      Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.

    • 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 MGSHMVNLQP QLASVTFATN NPTLTTVALE KPLCMFDSKE ALTGTHEVYL YVLVDSAISR NASVQDSTNT PLGSTFLQTE GGRTGPYKAV AFDLIPCSDL PSLDAIGDVS KASQILNAYL VRVGANGTCL WDPNFQGLCN PPLSAATEYR FKYVLVNMST GLVEDQTLWS DPIRTNQLTP YSTIDTWPGR RSGG.

    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.

    Upk3A Human
  • View Data Sheet

    Name :

    IFN g Human

    Description:

    IFN-Gamma Human Recombinant

    Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-206

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    • sds-page

    Description

    IFN-gamma Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH 4.6.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay is < 0.05 ng/ml, corresponding to a specific activity of 2.0 x 10,000,000 IU/mg.

    sds-page

    IFN-Gamma Human SDS-PAGE - Product image 1

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    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.

    • Synonyms

      Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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 IFN-gamma in sterile distilled water or 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQDPYVKEAE NLKKYFNAGH SDVADNGTLF LGILKNWKEE SDRKIMQSQI VSFYFKLFKN FKDDQSIQKS VETIKEDMNV KFFNSNKKKR DDFEKLTNYS VTDLNVQRKA IHELIQVMAE LSPAAKTGKR KRSQMLFQGR RASQ.

    • Background

      IFN-gamma Human

      About IFN-gamma Human:

      IFN-gamma, often known as interferon gamma (and originally known as immune interferon), is a soluble, dimerized cytokine that is the only interferon in the type II class. Besides its primary function in preventing the spread of the vesicular stomatitis virus, interferon gamma release assays are extensively employed in the diagnosis of tuberculosis. IFN-gamma, encoded by the IFNG gene in humans, controls immunological responses by cell signaling, particularly through the JAK-STAT pathway. Subsequently, interferon gamma plays a crucial role in cancer immunotherapy by preventing tumor growth, managing immune defenses against pathogens and monitoring cells activity. In this article we will delve into the science behind IFN-gamma and explain its significance in biomedical research.



      Description:

      IFN-gamma Human Recombinant is a single non-glycosylated, polypeptide chain containing 144 amino acids and having a molecular mass of 17kDa that its original source is Escherichia Coli. This product appears as a sterile-filtered white lyophilized powder, ensuring purity and stability. Its formulation involves lyophilization from a filtered concentrated solution in PBS (pH 4.6). Its purity is determined both by analysis by RP-HPLC and SDS-PAGE and is therefore greater than 98%. In terms of stability, lyophilized IFN gamma is stable at room temperature for three weeks. However, it is preferable to store it desiccated below -18°C. In any case, you should prevent freeze thaw cycles. Additionally, reconstitution of IFN-gamma is recommended in sterile distilled water or 20mM AcOH, maintaining a concentration of at least 100µg/ml.

      Protein Function:

      Interferon gamma is a key player in immune control. It is a protein that plays a major role in complex cell signaling networks. The JAK-STAT pathway, which is essential for immunological regulation, is triggered by IFN-gamma through its interaction with the heterodimeric receptor. IFN-gamma's ability to regulate inflammation, apoptosis, cytokine signaling, and cell proliferation through protein mediated signaling skills is crucial for maintaining immune vigilance and response mechanisms. The incorporation of IFN-gamma into our product is validated by protein quantitation using two independent methods: UV spectroscopy and RP-HPLC.

      Applications and Usage:

      IFN-gamma Human is tailored for laboratory research, serving as a vital tool in elucidating immune mechanisms, exploring antiviral features, and unraveling tumor suppressor functions.

      Safety Information:

      IFN-gamma Human is only intended to be used in laboratory research, in line with safety protocols. It emphasizes adherence to ethical and regulatory norms and is not designed for use as household chemicals, pharmaceuticals, agricultural goods, or food additives.

    • Protein content

      Protein quantitation was carried out by two independent methods: 1. UV spectroscopy at 280 nm using the absorbency value of 0.640 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 calibrated solution of IFN-g 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.

    Interferon Gamma Human
  • View Data Sheet

    Name :

    OPG Human, His

    Description:

    Osteoprotegerin Human Recombinant, His Tag

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    Product # :

    CYT-290

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    Description

    Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      1. Positive control for Western blot.
      2. Antibody production.
      3. Protein assay.

    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.

    Osteoprotegerin Human His
  • View Data Sheet

    Name :

    IL 17A/F Rat

    Description:

    Interleukin-17A/F Heterodimer Rat Recombinant

    IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

    Product # :

    CYT-677

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    Description

    IL-17A/F Rat Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide chain containing 1 monomeric subunit of each IL-17A & IL-17F. The dimer contains 269 amino acids and having a total molecular mass of 30.7 kDa. The IL-17A/F Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by HPLC and SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to induce of IL-6 production from NIH-3T3 cells, is 15.3-23 ng/ml.

    More Info

    • Introduction

      Rat IL-17A/F is a glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Rat IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Rat IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).

    • Synonyms

      IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rat IL-17A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Rat IL-17A/F 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 Rat IL-17A/F in sterile water not more than 1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IL-17A: MAVLIPQSSV CPNAEANNFL QNVKVNLKVL NSLSSKASSR RPSDYLNRST SPWTLSRNED PDRYPSVIWE AQCRHQRCVN AEGKLDHHMN SVLIQQEILV LKREPEKCPF TFRVEKMLVG VGCTCVSSIV RHAS.
      IL-17F: MARRNPKVGL SALQKAGNCP PLEDNSVRVD IRIFNQNQGI SVPRDFQNRS SSPWDYNITR DPDRFPSEIA EAQCRHSGCI NAQGQEDGSM NSVPIQQEIL VLRREPQGCS NSFRLEKMLI KVGCTCVTPI VHHAA.

    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 17 A F Rat
  • View Data Sheet

    Name :

    IL12 Human, Sf9

    Description:

    Interleukin-12 Human Recombinant, Sf9

    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-1111

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    Description

    Interleukin 12 Human Recombinant is a glycosylated heterodimer containing 503 amino acids (306 amino acid rHuIL-12 p40 and the 197 amino acid rHuIL-12 p35 subunits) and having a molecular mass of 60kDa. IL12 is purified by proprietary chromatographic techniques.

    Source

    Baculovirus.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

    Greater than 97.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using PHA-stimulated human T lymphoblasts. The ED50 for this effect is 0.01-0.05 ng/mL corresponding to a specific activity of 11,000 units/μg.

    More Info

    • Introduction

      interleukin 12 subunit beta/alpha or IL12b/IL12a is a growth factor cytokine which increases the lytic activity of NK/lymphokine-activated killer cells, activated T and NK cells and prompt IFN-gamma production (through resting PBMC). IL12b/IL12a is an essential part to the process of cellular-immunity and activates the differentiation of Th1 cells originates from the precursor T helper cells. The protein is linked to IL23A and creates the IL-23 interleukin, by that, the autoimmune inflammation is induced and autoimmune inflammatory diseases and tumorigenesis are being affected.

    • 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 White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 12 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF BB 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 12 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IL-12 is a heterodimer of IL-12A and IL-12B linked through a disulfide-bond:

      >IL-12 ARNLPVATP DPGMFPCLHH SQNLLRAVSN MLQKARQTLE FYPCTSEEID HEDITKDKTS TVEACLPLEL TKNESCLNSR ETSFITNGSC LASRKTSFMM ALCLSSIYED LKMYQVEFKT MNAKLLMDPK RQIFLDQNML AVIDELMQAL NFNSETVPQK SSLEEPDFYK TKIKLCILLH AFRIRAVTID RVMSYLNAS.

      >IL-12B

      IWELKKDV YVVELDWYPD APGEMVVLTC DTPEEDGITW TLDQSSEVLG SGKTLTIQVK EFGDAGQYTC HKGGEVLSHS LLLLHKKEDG IWSTDILKDQ KEPKNKTFLR CEAKNYSGRF TCWWLTTIST DLTFSVKSSR GSSDPQGVTC GAATLSAERV RGDNKEYEYS VECQEDSACP AAEESLPIEV MVDAVHKLKY ENYTSSFFIR DIIKPDPPKN LQLKPLKNSR QVEVSWEYPD TWSTPHSYFS LTFCVQVQGK SKREKKDRVF TDKTSATVIC RKNASISVRA QDRYYSSSWS EWASVPCS.

    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 Protein
  • View Data Sheet

    Name :

    IL17A Canine

    Description:

    Interleukin 17A Canine Recombinant

    IL17A, IL17, IL-17A, CTLA8, CTLA8, Interleukin 17A, Interleukin-17A, cytotoxic T-lymphocyte-associated serine esterase 8.

    Product # :

    CYT-1207

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    Description

    IL17A Canine Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (29-155a.a) containing 133 amino acids and having a molecular mass of 15.6kDa.IL17A is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    IL17A protein (0.5mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the IL-6 ELISA in a using NIH/3T3 mouse embryonic fibroblast cells. The ED50 range ≤ 10 ng/ml.

    More Info

    • Introduction

      IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.

    • Synonyms

      IL17A, IL17, IL-17A, CTLA8, CTLA8, Interleukin 17A, Interleukin-17A, cytotoxic T-lymphocyte-associated serine esterase 8.

    • 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

      FPQNPGCRNT EDKNFPQHVK VNLNILNRNT NSRRPSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CVNNEGNINY HMNSVPIQQE ILVLRRESQH CPHSFRLEKM LVAVGCTCVT PIVRHVAHHH HHH

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

    Il17A Canine
  • View Data Sheet

    Name :

    IL21 Human, Sf9

    Description:

    Interleukin-21, Sf9 Human Recombinant

    Interleukin-21 isoform 1, CVID11, IL-21, Za11.

    Product # :

    CYT-1072

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    Description

    IL21 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 145 amino acids (30-162a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).IL21 is expressed with a 12 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL21 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    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 has a key role in haematopoiesis and immune responses regulation, therefore can affect lymphocyte development. Activation of T cells leads to production of the IL21. The protein has a crucial role in the viral infections persistence.

    • Synonyms

      Interleukin-21 isoform 1, CVID11, IL-21, Za11.

    • 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

      ADPEFMQGQD RHMIRMRQLI DIVDQLKNYV NDLVPEFLPA PEDVETNCEW SAFSCFQKAQ LKSANTGNNE RIINVSIKKL KRKPPSTNAG
      RRQKHRLTCP SCDSYEKKPP KEFLERFKSL LQKMIHQHLS SRTHGSEDSH HHHHH.

    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 Human
  • View Data Sheet

    Name :

    Recombinant TNF-a Antibody

    Description:

    Recombinant Anti Human Tumor Necrosis Factor-Alpha

    Product # :

    ANT-599

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    Description

    Recombinant TNF-a Antibody is a recombinant human IgG1 monoclonal antibody specific for human tumor necrosis factor (TNF). Recombinant TNF-a Antibody is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.

    Source

    CHO.

    Formulation

    The Recombinant TNF-a Antibody 53mg/ml solution contains 6.16 mg/ml of sodium chloride, 0.86 mg/ml of monobasic sodium phosphate dihydrate, 1.53 mg/ml of dibasic sodium phosphate dihydrate, 0.3 mg/ml of sodium citrate, 1.30 mg/ml of citric acidmonohydrate, 12 mg/ml of mannitol, 1mg/ml of polysorbate 80, pH-5.

    Purity

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

    Biological Activity

    The EC50 as determined by L929 cell proliferation assay for neutralization reaction between TNF-a Antibody and TNFA, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 1.2 X 104EU/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesisand viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Physical Appearance

      Clear and colorless solution.

    • Stability

      Recombinant TNF-a Antibody should be stored between 2-8°C and should be protected from light. DO NOT FREEZE. DO NOT SHAKE.

    • Amino Acid Sequence

      LIGHT CHAIN
      DIQMTQSPSSLSASVGDRVTITCRASQGIRNYLAWYQQKPGKAPKLLIYAASTLQSGVPSRFSGSGSGTDF
      TLTISSLQPEDVATYYCQRYNRAPYTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPR
      EAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

      HEAVY CHAIN
      EVQLVESGGGLVQPGRSLRLSCAASGFTFDDYAMHWVRQAPGKGLEWVSAITWNSGHIDYADSVEGRFTISR
      DNAKNSLYLQMNSLRAEDTAVYYCAKVSYLSTASSLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTA
      ALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVD
      KKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEV
      HNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSRD
      ELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVM
      HEALHNHYTQKSLSLSPGK.

    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.

    Recombinant Tnf A Antibody
  • View Data Sheet

    Name :

    DEFB116 Human

    Description:

    Beta Defensin 116 Human Recombinant

    Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

    Product # :

    CYT-713

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    • sds-page

    Description

    DEFB116 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 102 amino acids (24-102 a.a) and having a molecular mass of 11.5kDa.DEFB116 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DEFB116 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    sds-page

    DEFB116-sds-page - Product image 1

    More Info

    • Introduction

      Beta Defensin 116, also known as DEFB116 is a member of the beta-defensin family.DEFB116 has antibacterial activity. The innate immune system includes antimicrobial peptides that protect multicellular organisms from a diverse spectrum of microorganisms. In addition, Beta-Defensins contain one important family of mammalian antimicrobial peptides.

    • Synonyms

      Beta-Defensin 16, DEFB-16, Beta 16, defensin, Beta-Defensin 116, Defensin, Beta 16, DEFB16.

    • 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 MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

    • Background

      Title: Beta Defensin 116 Human Recombinant: An Insight into its Antimicrobial Properties and Therapeutic Applications

      Abstract:


      Beta defensin 116 (BD116) is a key member of the beta defensin family, known for its potent antimicrobial activity against various pathogens. This research paper provides an in-depth analysis of human recombinant BD116, focusing on its production, characterization, and potential applications in antimicrobial therapy. The paper highlights the significance of BD116 in innate immunity and its role in combating microbial infections. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant BD116 in various infectious diseases. The information presented in this paper aims to enhance our understanding of human recombinant BD116 and its utility as a research tool and a potential antimicrobial agent.

      Introduction:


      Beta defensin 116 (BD116) is a small cationic peptide that plays a crucial role in the innate immune response against microbial pathogens. Human recombinant BD116, produced through genetic engineering techniques, offers a valuable tool for studying its antimicrobial properties and exploring its therapeutic potential.

      Production and Characterization:


      Recombinant BD116 is typically generated using expression systems such as bacteria or yeast. The protein is then purified and characterized to ensure its structural integrity and antimicrobial activity. Rigorous quality control measures are implemented to confirm the specificity and potency of the recombinant BD116.

      Antimicrobial Properties:


      BD116 exhibits broad-spectrum antimicrobial activity against bacteria, fungi, and viruses. It functions by disrupting the microbial cell membrane and interfering with essential cellular processes. Recombinant BD116 serves as a valuable tool for investigating the mechanisms underlying its antimicrobial action and exploring its potential as an antimicrobial agent.

      Therapeutic Implications:


      The emergence of multidrug-resistant pathogens poses a significant challenge in the treatment of infectious diseases. Recombinant BD116 holds promise as an alternative therapeutic option due to its potent antimicrobial properties. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant BD116 in various infectious diseases, including bacterial skin infections and respiratory tract infections.

      Conclusion:


      Human recombinant BD116 is a valuable research tool and a potential antimicrobial agent. Its production, characterization, and applications in antimicrobial therapy contribute to our understanding of innate immunity and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant BD116 offer promising prospects for combating multidrug-resistant pathogens and improving outcomes in infectious diseases.

      What is the molecular weight/Mw of DEFB116 Protein?
      DEFB116 Protein has a total Mw of 11.5kDa.

      What is the source or expression system of DEFB116 Protein?
      Escherichia Coli.

      What is the Purity of DEFB116 Protein?
      DEFB116 Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of DEFB116 Protein?
      The biological functionality of DEFB116 Protein will be determined in the future.

      What is the amino acid sequence of DEFB116 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSGLFRSHN GKSREPWNPC ELYQGMCRNA CREYEIQYLT CPNDQKCCLK LSVKITSSKN VKEDYDSNSN LSVTNSSSYS HI.

      What applications can DEFB116 Protein be used in?
      DEFB116 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for DEFB116 Protein?
      The endotoxin level is minimal, DEFB116 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.

    Defb116 Human
  • View Data Sheet

    Name :

    EBI3 Mouse

    Description:

    Epstein Barr Virus Induced 3 Mouse Recombinant

    IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

    Product # :

    CYT-621

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    Description

    EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

    Purity

    Greater than 90% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.

    • Synonyms

      IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

    • Background

      What is the molecular weight/Mw of EBI3 Protein?
      EBI3 Protein has a total Mw of 22.9kDa.

      What is the source or expression system of EBI3 Protein?
      Escherichia Coli.

      What is the Purity of EBI3 Protein?
      EBI3 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of EBI3 Protein?
      The biological functionality of EBI3 Protein will be determined in the future.

      What is the amino acid sequence of EBI3 Protein?
      MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

      What applications can EBI3 Protein be used in?
      EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EBI3 Protein?
      The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.

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

    Ebi3 Mouse
  • View Data Sheet

    Name :

    IL 10 Mouse

    Description:

    Interleukin-10 Mouse Recombinant

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

    Product # :

    CYT-497

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    Description

    IL-10 Recombinant Mouse produced in E.coli is a single, non-glycosylated polypeptide chain containing 161 amino acids and having a molecular mass of 18785 Dalton. The Interleukin-10 Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized after extensive dialysis against PBS.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant co-stimulation with IL-4 of mouse MC-9 cells was found to be < 2ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • 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.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-10 Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Interleukin10 Mouse recombinant 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-10 Mouse Recombinant 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 Met-Ser-Arg-Gly-Gln.

    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 10 Mouse
  • View Data Sheet

    Name :

    Betacellulin His Human

    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

    Betacellulin-sds-page - Product image 1

    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

    Name :

    LGALS13 Human

    Description:

    Galectin-13 Human Recombinant

    Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.

    Product # :

    CYT-004

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    Description

    Recombinant Human LGALS13 produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 16kDa. The LGALS13 also might appear as a homodimer, having a total Mw of 32kDa. LGALS13 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS13 protein solution (0.5mg/ml) is formulated in 1xPBS buffer pH 7.4.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Galectin-13 is an E. coli expressed peptide, this protein is one of human placenta specific galectins, like all galectin family, it contains a carbohydrate recognition domain (CRD) as well. Increased blood concentration was found highly asscoaited with preeclampsia and HELLP syndrome in pregnant women. The molecular weight of galectin-13 is 16kDa.

    • Synonyms

      Galactoside-binding soluble lectin 13, Galectin-13, Gal-13, Placental tissue protein 13, PP13, Placental protein 13, LGALS13, PLAC8, GAL13.

    • 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

      MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK

      QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN

    • Background

      What is the molecular weight/Mw of LGALS13 HUMAN Protein?
      LGALS13 HUMAN Protein has a total Mw of 32kDa.

      What is the source or expression system of LGALS13 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of LGALS13 HUMAN Protein?
      LGALS13 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS13 HUMAN Protein?
      The biological functionality of LGALS13 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of LGALS13 HUMAN Protein?
      MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDM DEDSDIAFRFRVHFGNHVVMNRREFGIWMLEETTDYVPFEDGK
      QFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSFVKMVQVSRDISLTSVCVCN

      What applications can LGALS13 HUMAN Protein be used in?
      LGALS13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS13 HUMAN Protein?
      The endotoxin level is minimal, LGALS13 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.

    Lgals13 Human
  • View Data Sheet

    Name :

    NCR3 antibody

    Description:

    Mouse Anti Human Natural Cytotoxicity Triggering Receptor 3

    Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    Product # :

    ANT-740

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    • More Info

    Formulation

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

    More Info

    • Introduction

      Cytotoxicity Triggering Receptor 3 also known as NCR3 is a natural cytotoxicity receptor (NCR) which assists NK cells in the lysis of tumor cells. Moreover, NCR3 interacts with CD3-zeta (CD247), a T-cell receptor. A single nucleotide polymorphism in the 5' untranslated region of NCR3 has been related with mild malaria suceptibility. Three transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 3, LY117, 1C7, Lymphocyte Antigen 117, Activating Natural Killer Receptor P30, Natural Killer Cell P30-Related Protein, NK-p30, NKp30, CD337, MALS, Activating NK-A1 Receptor, CD337 Antigen, NKP30.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human NCR3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human NCR3 protein 19-138 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT38D9AT.

    • Applications

      NCR3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      NCR3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Ncr3 Antibody
  • View Data Sheet

    Name :

    IL18BP Human

    Description:

    Interleukin-18 Binding Protein Human Recombinant

    Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.

    Product # :

    CYT-728

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    • description
    • source
    • formulation
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    • More Info

    Description

    IL18BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (31-194 a.a) and having a molecular mass of 20kDa. IL18BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL18BP 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.

    More Info

    • Introduction

      Interleukin-18 Binding Protein (IL18BP) serves as an inhibitor of the proinflammatory cytokine, IL18. IL18BP binds IL18, inhibits the binding of IL18 to its receptor, and consequently inhibits IL18-induced IFN-gamma production, resulting in reduced T-helper type 1 immune responses. The IL18BP protein is constitutively expressed and secreted in mononuclear cells. Elevated levels of IL18BP protein are detected in the intestinal tissues of patients with Crohn's disease.

    • Synonyms

      Interleukin 18 Binding Protein, MC51L-53L-54L Homolog Gene Product, Tadekinig-Alfa, IL-18BP, IL18BPa, Interleukin-18-binding protein, Tadekinig-alfa.

    • 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 MGSTPVSQTT TAATASVRST KDPCPSQPPV FPAAKQCPAL EVTWPEVEVP LNGTLSLSCV ACSRFPNFSI LYWLGNGSFI EHLPGRLWEG STSRERGSTG TQLCKALVLE QLTPALHSTN FSCVLVDPEQ VVQRHVVLAQ LWAGLRATLP PTQEALPSSH SSPQQQG.

    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.

    Il18Bp Human
  • View Data Sheet

    Name :

    IL 28A Human, His

    Description:

    Interleukin-28A Human Recombinant, His Tag

    Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

    Product # :

    CYT-813

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    • description
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    Description

    IL 28A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (26-200 a.a.) and having a molecular mass of 22.1kDa. IL 28A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL 28A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-28A is distantly related to type I interferons and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
      IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
      IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
      IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.

    • Synonyms

      Interleukin-28A, IL-28A, IFN-Lambda 2, Interferon-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

    • 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 MGSVPVARLH GALPDARGCH IAQFKSLSPQ ELQAFKRAKD ALEESLLLKD CRCHSRLFPR TWDLRQLQVR ERPMALEAEL ALTLKVLEAT ADTDPALVDV LDQPLHTLHH ILSQFRACIQ PQPTAGPRTR GRLHHWLYRL QEAPKKESPG CLEASVTFNL FRLLTRDLNC VASGDLCV .

    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 28A Human His
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