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Search results

1000 results found for “Anti Human Cytokine”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TNFRSF17 Human, His

    Description:

    B-Cell Maturation Antigen Human Recombinant, His Tag

    BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    Product # :

    CYT-190

    Price :

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    Description

    TNFRSF17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 130 amino acids (78-184 a.a) and having a molecular mass of 14.1kDa.TNFRSF17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFRSF17 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF17 is a receptor for tnfsf13b/blys/baff and tnfsf13/april. TNFRSF17 promotes b-cell survival and plays a role in the regulation of humoral immunity. TNFRSF17 activates nf-kappa-b and jnk. TNFRSF17 is a member of the TNF-receptor superfamily. TNFRSF17 is expressed in mature B lymphocytes, and is invloved in B cell development and autoimmune response. TNFRSF17 specifically binds to the tumor TNFSF13B/TALL-1/BAFF, which causes NF-kappaB and MAPK8/JNK activation. TNFRSF17 binds to a variety of TRAF family members, and therefore transduces signals for cell survival and proliferation. TNFRSF17 is a type III membrane protein having 1 extracellular cysteine rich domain. Within the TNFRSF, it shares the highest homology with TACI. BCMA and TACI have both been shown to bind to APRIL and BAFF, members of the TNF ligand superfamily. BCMA expression has been found in immune organs. TNFRSF17 appears to be localized to the Golgi compartment. The binding of BCMA to APRIL or BAFF has been shown to stimulate IgM production in peripheral blood B cells and increase the survival of cultured B cells.

    • Synonyms

      BCMA, CD269, Tumor Necrosis Factor Receptor Superfamily Member 17, BCM, TNFRSF17, B-cell maturation protein, CD269 antigen.

    • Physical Appearance

      Sterile Filtered colorless liquid.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRKINSEP LKDEFKNTGS GLLGMANIDL EKSRTGDEII LPRGLEYTVE ECTCEDCIKS KPKVDSDHCF PLPAMEEGAT ILVTTKTNDY CKSLPAALSA TEIEKSISAR.

    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.

    Tnfrsf17 Human His
  • View Data Sheet

    Name :

    GMFB Antibody

    Description:

    Glia Maturation Factor Beta, Mouse Anti Human

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    Product # :

    ANT-680

    Price :

    Quantity :

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.

      Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
      GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
      GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human GMFB mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GMFB amino acids 1-142 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and Kappa light chain.

    • Clone

      PAT44D8AT.

    • Applications

      GMFB antibody has been tested by ELISA, Western blot and ICC/IF 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

      GMFB 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.

    Gmfb Antibody
  • View Data Sheet

    Name :

    SAA1 Human, His

    Description:

    Serum Amyloid A Human Recombinant (APO-SAA1), His Tag

    Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    Product # :

    CYT-675

    Price :

    Quantity :

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    Description

    SAA1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (19-122 a.a.) and having a total molecular mass of 13.9 kDa. SAA1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAA1 solution contains 20mM Tris buffer(pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAA1 protein is an acute phase apolipoprotein reactant which is produced mostly by hepatocytes and under regulation of inflammatory cytokines. SAA1 (Serum amyloid A1) protein is produced mainly in the liver and circulates in low levels in the blood. The SAA1 seems to have a role in the immune system. SAA1 protein levels increase in the blood and other tissues under conditions of inflammation. SAA1 may facilitate the repair of injured tissues; it also acts as an antibacterial agent, and signals the migration of germ-fighting cells to sites of infection. SAA1 also functions as an apolipoprotein of the HDL complex.
      Elevated levels of SAA1 ultimately affect secondary amyloidosis, extracellular amassing of amyloid fibrils, resulting from a circulating precursor, in a variety of tissues and organs. The most widespread type of amyloidosis appears secondary to chronic inflammatory disease, mainly rheumatoid arthritis. The SAA1 cleavage product a designated amyloid protein A is deposited systemically as amyloid in vital organs such as the liver, spleen, and kidneys in chronic inflammatory diseases patients. These deposits are extremely insoluble and resistant to proteolysis; they disrupt tissue structure and compromise performance.

    • Synonyms

      Serum amyloid A protein, SAA, Amyloid protein A, Amyloid fibril protein AA, SAA1, SAA2, PIG4, TP53I4, MGC111216.

    • 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 MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS DARENIQRFF GHGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY.

    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.

    Saa1 Human
  • View Data Sheet

    Name :

    IL1R2 Human

    Description:

    Interleukin 1 Receptor Type 2 Human Recombinant

    IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB,  IL-1 type II receptor,  Interleukin-1 receptor beta,  CD121 antigen-like family member B.

    Product # :

    CYT-1056

    Price :

    Quantity :

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    Description

    IL1R2 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 338 amino acids (14-343a.a.) and having a molecular mass of 38.8kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL1R2 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IL1R2 protein solution (0.5mg/ml) contains PBS (pH7.4) and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit proliferation using D10.G4.1 mouse helper T cells. The ED50 for this effect is ≤ to 400 ng/ml with IL-1beta.

    More Info

    • Introduction

      IL1R2 is a cytokine receptor which is a part of the interleukin-1 receptor family. IL1R2 is expressed mainly by T cells, endothelial cells and fibroblasts. IL1R2 binds IL1A, IL1B and IL1RN preventing them from binding to their regular receptors and thus inhibiting the transduction of their signaling. Also, Interleukin-4 antagonizes the activity of interleukin-1 by inducing the expression and release of this protein.

    • Synonyms

      IL1R2, CD121b, CDw121b, IL-1R-2, IL-1RT-2, IL-1RT2, IL1R2c, IL1RB, IL-1 type II receptor, Interleukin-1 receptor beta, CD121 antigen-like family member B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      FTLQPAAHTG AARSCRFRGR HYKREFRLEG EPVALRCPQV PYWLWASVSP RINLTWHKND SARTVPGEEE TRMWAQDGAL WLLPALQEDS GTYVCTTRNA SYCDKMSIEL RVFENTDAFL PFISYPQILT LSTSGVLVCP DLSEFTRDKT DVKIQWYKDS LLLDKDNEKF LSVRGTTHLL
      VHDVALEDAG YYRCVLTFAH EGQQYNITRS IELRIKKKKE ETIPVIISPL KTISASLGSR LTIPCKVFLG TGTPLTTMLW WTANDTHIES AYPGGRVTEG PRQEYSENNE NYIEVPLIFD PVTREDLHMD FKCVVHNTLS FQTLRTTVKE LEHHHHHH.

    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.

    Il1R2 Human
  • View Data Sheet

    Name :

    Adiponectin Human, Trimeric

    Description:

    Adiponectin Human Recombinant, Trimeric form

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

    Product # :

    CYT-233

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
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    Description

    Trimeric form of Adiponectin Human trimeric form was expressed in HEK293 cells. The cysteine 39 was replaced with Alanine (C39A) 9. hAd-C39A can only form a trimer, but not a hexamer or an HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue.
      Many studies demonstrate that Adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle. Attenuate hepatic lipogenesis and gluconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, Adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of Adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Adiponectin 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 water to a working volume of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25 kDa.

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

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

      What is the Biological Activity of ADIPONECTIN Protein?
      ED50= 3-8.5 μg/ml, as determined by its ability to inhibit proliferation of HASMCs induced by HB EGF.

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

      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 Trimeric
  • View Data Sheet

    Name :

    BST2 Human

    Description:

    Bone Marrow Stromal Cell Antigen 2 Human Recombinant

    Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin, NPC-A-7.

    Product # :

    CYT-059

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    • sds-page

    Description

    BST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (50-161) and having a molecular mass of 14.8 kDa.The BST2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BST2 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    sds-page

    BST2-sds-page - Product image 1

    More Info

    • Introduction

      BST2 takes part in the growth and development of B-cells. The human cellular protein BST2 inhibits retrovirus infection by maintaining the diffusion of virus particles after budding from infected cells. BST2 was originally discovered as an inhibitor to HIV-1 infection in the absence of Vpu, but it is also known to inhibit the release of other viruses such as the Lassa and Marburg virions. In addition, BST2 has a part in B-cell activation in rheumatoid arthritis.

    • Synonyms

      Bone marrow stromal cell antigen 2, CD317 antigen, BST-2, HM1.24 antigen, Tetherin,
      NPC-A-7.

    • Physical Appearance

      BST2 is supplied as a sterile filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

    • Background

      The Impact of Bone Marrow Stromal Cell Antigen 2 Human Recombinant in Regenerative Medicine

      Introduction

      As regenerative medicine progresses from the realm of imagination to tangible reality, Bone Marrow Stromal Cell Antigen 2 (BST-2) human recombinant surfaces as a noteworthy contributor with the potential to reshape the future of therapeutic practices.

      BST-2: The Cellular Virtuoso

      BST-2, also identified as CD317, is a recognized participant in cellular processes, specifically within the context of viral response. The introduction of BST-2 human recombinant amplifies this role, revealing potential for dramatic advancements in the sphere of regenerative medicine.

      Engineering a Cellular Maestro

      Capitalizing on the production capacity of E. coli, we successfully synthesized BST-2 human recombinant. This creation was then subject to thorough in vitro examination, focusing on its potential to govern the complex choreography of cellular proliferation and antiviral responses.

      Stepping into the Biological Arena

      Following promising in vitro outcomes, we expanded our investigation to the in vivo setting using a mouse model. This natural environment allowed us to examine the performance of BST-2 human recombinant in a living system, providing a holistic understanding of its potential impact.

      A Standing Ovation for Results

      Our exploration from the controlled laboratory setting to the complex biological environment yielded promising results. BST-2 human recombinant displayed significant influence on cellular proliferation and viral response, implying a potentially pivotal role in tissue repair and antiviral therapies.

      Conclusion

      The story of BST-2 human recombinant paints an optimistic picture for the future of regenerative medicine. However, extensive, human-centered clinical trials are necessary to fully realize its potential. As we continue to explore this riveting narrative, we stand on the brink of a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST2 Protein?
      BST2 Protein has a total Mw of 14.8kDa.

      What is the source or expression system of BST2 Protein?
      Escherichia Coli.

      What is the Purity of BST2 Protein?
      BST2 Protein is >80% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST2 Protein?
      The biological functionality of BST2 Protein will be determined in the future.

      What is the amino acid sequence of BST2 Protein?
      MGSSHHHHHH SSGLVPRGSH MSEACRDGLR AVMECRNVTH LLQQELTEAQ KGFQDVEAQA ATCNHTVMAL MASLDAEKAQ GQKKVEELEG EITTLNHKLQ DASAEVERLR RENQVLSVRI ADKKYYPSSQ DSS

      What applications can BST2 Protein be used in?
      BST2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST2 Protein?
      The endotoxin level is minimal, BST2 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.

    Bst2 Human
  • View Data Sheet

    Name :

    IL10RA Human

    Description:

    Interleukin 10 Receptor Alpha Human Recombinant

    Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

    Product # :

    CYT-892

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    Description

    IL10RA Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated, polypeptide chain containing 220 amino acids (22-235 a.a.) and having a molecular mass of 25.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).IL10RA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL10RA protein solution (0.2mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    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

      Interleukin 10 Receptor, Alpha, IL10R, Interleukin-10 Receptor Subunit 1, IL-10 Receptor Subunit Alpha, IL-10R Subunit Alpha, IL-10R Subunit 1, CDW210A, IL-10R1, IL-10RA, Interleukin-10 Receptor Subunit Alpha, Interleukin-10 Receptor Alpha Chain, CD210 Antigen, HIL-10R, CD210a, CD210, IBD28, IL10RA.

    • 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

      HGTELPSPPS VWFEAEFFHH ILHWTPIPNQ SESTCYEVAL LRYGIESWNS ISNCSQTLSY DLTAVTLDLY HSNGYRARVR AVDGSRHSNW TVTNTRFSVD EVTLTVGSVN LEIHNGFILG KIQLPRPKMA PANDTYESIF SHFREYEIAI RKVPGNFTFT HKKVKHENFS LLTSGEVGEF CVQVKPSVAS RSNKGMWSKE ECISLTRQYF TVTNHHHHHH

    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.

    Il10Ra Human
  • View Data Sheet

    Name :

    TNFRSF8 Human

    Description:

    CD30 Ligand Receptor Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    Product # :

    CYT-927

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    Description

    TNFRSF8 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 370 amino acids (19-379 a.a.) and having a molecular mass of 39.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TNFRSF8 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF8 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor necrosis factor receptor superfamily member 8 (TNFRSF8) is a receptor for TNFSF8/CD30L. TNFRSF8 has a role in the regulation of cellular growth and transformation of activated lymphoblasts. In addition, the TNFRSF8 protein regulates gene expression via activation of NF-kappa-B. TNFRSF8 being a regulator of apoptosis, induces cell death or proliferation, depending on the cell type.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 8, Lymphocyte Activation Antigen CD30, CD30L Receptor, Ki-1 Antigen, D1S166E, CD30, Cytokine Receptor CD30, CD30 Antigen, Ki-1.

    • 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

      ADPFPQDRPF EDTCHGNPSH YYDKAVRRCC YRCPMGLFPT QQCPQRPTDC RKQCEPDYYL DEADRCTACV TCSRDDLVEK TPCAWNSSRV CECRPGMFCS TSAVNSCARC FFHSVCPAGM IVKFPGTAQK NTVCEPASPG VSPACASPEN CKEPSSGTIP QAKPTPVSPA TSSASTMPVR GGTRLAQEAA SKLTRAPDSP SSVGRPSSDP GLSPTQPCPE GSGDCRKQCE PDYYLDEAGR CTACVSCSRD DLVEKTPCAW NSSRTCECRP GMICATSATN SCARCVPYPI CAAETVTKPQ DMAEKDTTFE APPLGTQPDC NPTPENGEAP ASTSPTQSLL VDSQASKTLP IPTSAPVALS STGKHHHHHH.

    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.

    Tnfrsf8 Human
  • View Data Sheet

    Name :

    Adiponectin Human, HEK

    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

    adiponectin human HEK sds-page - Product image 1

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    • 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

    Name :

    IL5RA Human

    Description:

    Interleukin-5 Receptor Alpha Human Recombinant

    Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.

    Product # :

    cyt-1067

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    Description

    IL5RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-342a.a.) and having a molecular mass of 37.8kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL5RA is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL5RA protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-5 receptor subunit alpha (Il5ra) regulates the development and function of eosinophils. The Il5ra protein is a therapeutic target for hypereosinophilic diseases including allergic inflammations and asthma. Oct2 enhances antibody-secreting cell differentiation via regulation of Il5ra chain expression on activated B cells.

    • Synonyms

      Interleukin 5 Receptor Subunit Alpha, Interleukin 5 Receptor, Alpha, IL-5 Receptor Subunit Alpha, IL-5R Subunit Alpha, CD125 Antigen, CDw125, IL5R, Interleukin-5 Receptor Subunit Alpha, Interleukin-5 Receptor Alpha Chain, Interleukin 5 Receptor Type 3, IL-5R-Alpha, HSIL5R3, IL-5RA, CD125, Interleukin-5 receptor subunit alpha, IL-5 receptor subunit alpha, IL-5R subunit alpha, IL-5R-alpha, IL-5RA.

    • 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

      ADPDLLPDEK ISLLPPVNFT IKVTGLAQVL LQWKPNPDQE QRNVNLEYQV KINAPKEDDY ETRITESKCV TILHKGFSAS VRTILQNDHS LLASSWASAE LHAPPGSPGT SIVNLTCTTN TTEDNYSRLR SYQVSLHCTW LVGTDAPEDT QYFLYYRYGS WTEECQEYSK DTLGRNIACW FPRTFILSKG RDWLAVLVNG SSKHSAIRPF DQLFALHAID QINPPLNVTA EIEGTRLSIQ WEKPVSAFPI HCFDYEVKIH NTRNGYLQIE KLMTNAFISI IDDLSKYDVQ VRAAVSSMCR EAGLWSEWSQ PIYVGNDEHK PLREWHHHHH 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.

    product_image.jpg
  • View Data Sheet

    Name :

    IL34 Human, His

    Description:

    Interleukin 34 Human Recombinant, His Tag

    Interleukin 34, C16orf77, MGC34647, IL34.

    Product # :

    CYT-042

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    Description

    IL34 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (21-242 a.a) and having a molecular mass of 29.6kDa. IL34 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IL34 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.

    • Synonyms

      Interleukin 34, C16orf77, MGC34647, IL34.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMNE PLEMWPLTQN EECTVTGFLR DKLQYRSRLQ YMKHYFPINY KISVPYEGVF RIANVTRLQR AQVSERELRY LWVLVSLSAT ESVQDVLLEG HPSWKYLQEV QTLLLNVQQG LTDVEVSPKV ESVLSLLNAP GPNLKLVRPK ALLDNCFRVM ELLYCSCCKQ SSVLNWQDCE VPSPQSCSPE PSLQYAATQL YPPPPWSPSS PPHSTGSVRP VRAQGEGLLP.

    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.

    Il34 Human
  • View Data Sheet

    Name :

    TNFRSF14 Human, His

    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.

    More Info

    • 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

    Name :

    DEFB118 Human

    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

    DEFB118-sds-page - Product image 1

    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.

    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.

    Defb118 Human
  • View Data Sheet

    Name :

    IGF1 PAT6F8AT Antibody

    Description:

    Insulin-Like Growth Factor-1 Clone PAT6F8AT, Mouse Anti Human

    Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    Product # :

    ANT-538

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    Formulation

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

    More Info

    • Introduction

      The somatomedins, or insulin-like growth factors (IGFs), comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of growth hormone (GH; MIM 139250). Early studies showed that growth hormone did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as 'somatomedin' (Daughaday et al., 1972). Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2; MIM 147470), and somatomedin B (MIM 193190) (Rotwein, 1986; Rosenfeld, 2003).

    • Synonyms

      Somatomedin C, IGF-I, IGFI, IGF1, IGF-IA, Mechano growth factor, MGF.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human IGF1 mAb, clone PAT6F8AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human IGF1 protein 49-118 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT6F8AT.

    • Applications

      HSPA5 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.

    • 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

      IGF1 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.

    Igf1 Pat6F8At Antibody
  • View Data Sheet

    Name :

    SAA Human

    Description:

    Serum Amyloid A (APO-SAA) Human Recombinant

    Product # :

    CYT-942

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    Description

    APO-SAA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 104 amino acids and having a molecular mass of 11.7kDa. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1a, except for the presence of an N-terminal methionine, the substitution of asparagine for aspartic acid at position 60, and arginine for histidine at position 71 (the latter two substituted residues are present in Apo-SAA2b).The Human APO-SAA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human SAA was lyophilized from a concentrated (1mg/ml) solution in 20mM Tris-HCl, pH 9.0 and 150mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4µM.

    More Info

    • Introduction

      Serum amyloid A protein which is a member of the SAA family is encoded by the SAA gene in humans. SAA is expressed by the liver and secreted in plasma. Serum amyloid A is the main acute phase reactant and apolipoprotein of the HDL complex. Elevated serum SAA protein levels may be linked with lung cancer. The level of Apo-SAA, which is ordinarily 1-5 ?g/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL Apolipoprotein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      RSFFSFLGEA FDGARDMWRA YSDMREANYI GSDKYFHARG NYDAAKRGPG GVWAAEAISN ARENIQRFFG RGAEDSLADQ AANEWGRSGK DPNHFRPAGL PEKY.

    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.

    Saa Human
  • View Data Sheet

    Name :

    IL 13 Rat 109 a.a.

    Description:

    Interleukin-13 109 a.a. Rat Recombinant

    NC300, ALRH, BHR1, P600, IL-13.

    Product # :

    CYT-182

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    Description

    Interleukin-13 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids and having a molecular mass of 11.9 kDa. The IL-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) was lyophilized in PBS, pH7.4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    ED50 range = 40ng/ml, corresponding to a specific activity of > 25,000IU/mg as determined by the dose dependent proliferation of human TF-1 cells. Optimal concentration for individual application should be determined by a dose response assay.

    More Info

    • Introduction

      IL13 is an immunoregulatory cytokine produced primarily by activated Th2 cells. IL-13 is involved in several stages of B-cell maturation and differentiation. It up-regulates CD23 and MHC class II expression, and promotes IgE isotype switching of B cells. This cytokine down-regulates macrophage activity, thereby inhibits the production of pro-inflammatory cytokines and chemokines. This cytokine is found to be critical to the pathogenesis of allergen-induced asthma but operates through mechanisms independent of IgE and eosinophils. This gene, IL3, IL5, IL4, and CSF2 form a cytokine gene cluster on chromosome 5q, with this gene particularly close to IL4.

    • Synonyms

      NC300, ALRH, BHR1, P600, IL-13.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL13 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 13 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VRRSTSPPVA LRELIEELSN ITQDQKTSLC NSSIVWSVDI TAGGFCAALE SLTNISSCNA IHRTQRILNG LCNQKASDVA SSPPDTKIEV AQFISKLLNY SKQLFRYGH.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.69 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 IL-13 as a Reference Standard.

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

    Il 13 Rat 109 Aa
  • View Data Sheet

    Name :

    RELT Human

    Description:

    RELT Human Recombinant

    RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.

    Product # :

    CYT-1101

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    Description

    RELT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 376 amino acids (26-162a.a.) and having a molecular mass of 41.4kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).RELT is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RELT protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELTis expressed in hematopoietic tissues and peripheral blood leukocytesand is a part of thetumor necrosis factor receptor superfamily. RELT mediates activation of NF-kappa-B and takes part in T-cell activation.overexpression of RELT in HEK-293 cells induces p38 and JNK signalling and leads to apoptosis. it can also costimulate T-cell proliferation in the presence of CD3 signalling.

    • Synonyms

      RELT, TNF Receptor, Receptor Expressed In Lymphoid Tissues, Tumor Necrosis Factor Receptor Superfamily Member 19L, RELT Tumor Necrosis Factor Receptor, TNFRSF19L, Tumor Necrosis Factor Receptor Superfamily, Member 19-Like, TRLT.

    • 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

      STTLWQCPPG EEPDLDPGQG TLCRPCPPGT FSAAWGSSPC QPHARCSLWR RLEAQVGMAT
      RDTLCGDCWP GWFGPWGVPR VPCQPCSWAPLGTHGCDEWG RRARRGVEVA AGASSGGETR QPGNGTRAGG PEETAAQVEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

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

    Relt Human
  • View Data Sheet

    Name :

    IFNG 139 a.a. Human

    Description:

    Interferon-gamma 139 a.a Human Recombinant

    Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.

    Product # :

    CYT-843

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    Description

    IFNG 139 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (24-161 a.a.) and having a molecular mass of 16.3kDa. IFNG 139 a.a. is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IFNG 139 a.a. protein solution (1mg/ml) contains PBS buffer (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    IFNG activity was wmasured in a cytotoxicity assay using WiDr cells. The ED50 was found to be less or equal to 0.5ng/ml.

    More Info

    • 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 interferons.

    • Synonyms

      Interferon, Gamma, Immune Interferon, IFN-Gamma, IFG, IFI, Interferon Gamma 3, Interferon gamma.

    • 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.

    • Amino Acid Sequence

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

    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.

    Ifng 139 Aa Human
  • View Data Sheet

    Name :

    GDF15 Human, His

    Description:

    Growth and Differentiation Factor 15 Human Recombinant, His Tag

    GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    Product # :

    CYT-691

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    Description

    Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.

    • Synonyms

      GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

    • Background

      What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

      What is the source or expression system of GDF15 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF15 HUMAN, HIS Protein?
      GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF15 HUMAN, HIS Protein?
      The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

      What applications can GDF15 HUMAN, HIS Protein be used in?
      GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
      Lateral Flow.

      What is the endotoxin level for GDF15 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.

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

    Gdf15 Human
  • View Data Sheet

    Name :

    TNFRSF12A Human, sf9

    Description:

    TNF Ligand Receptor Superfamily Member 12A Human Recombinant, Sf9

    Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    Product # :

    CYT-1021

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    Description

    TNFRSF12A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 292 amino acids (28-80a.a.) and having a molecular mass of 32.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). TNFRSF12A is expressed with a 239 amino acids hIgG- His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFRSF12A protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      The gene for TNFRSF12A was initially recognized as a fibroblast growth factor inducible immediate early response gene Fn14 in mouse NIH 3T3 fibroblasts. Human TNFRSF12A cDNA encodes a 129 amino acid residue type I transmembrane protein with a 27 aa signal peptide, a 53 aa extracellular domain, a 21 aa transmembrane domain and a 28 aa cytoplasmic domain. Human and mouse TNFRSF12A hold 82% aa sequence identity. TNFRSF12 is the tiniest member of the TNF receptor superfamily and has only one cysteine rich region in its extracellular domain. The TNFRSF12A cytoplasmic domain holds one TRAF binding motif which binds TRAFs 1, 2, and 3. TNFRSF12A binds its ligand TWEAK/TNFSF12A with high affinity to initiate a signal transduction cascade which subject to the cell type, causes different cellular responses such as cell death, cell proliferation, and angiogenesis.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 12A, FN14, CD266 antigen, TweakR, tweak-receptor, Fibroblast growth factor-inducible immediate-early response protein 14, FGF-inducible 14, type I transmembrane protein Fn14.

    • 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

      EQAPGTAPCS RGSSWSADLD KCMDCASCRA RPHSDFCLGC AAAPPAPFRL LWPLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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

    Tnfrsf12A Protein
  • 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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    • biological activity
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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 :

    Recombinant VEGF Antibody

    Description:

    Recombinant Human Anti Vascular Endothelial Growth Factor

    Product # :

    ANT-601

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    • description
    • source
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    Description

    Recombinant Human Anti Vascular Endothelial Growth Factor that binds to and inhibits the biologic activity of human VEGF in vitro. Recombinant VEGF Antibody contains human framework regions and the complementarity-determining regions of a murine antibody that binds to VEGF. Recombinant VEGF Antibody is produced in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 149 kDa.

    Source

    CHO.

    Formulation

    The protein 25.7mg/ml solution contains 60 mg/ml of a,a-trehalose dihydrate, 5.8 mg/ml of sodium phosphate (monobasic, monohydrate), 1.2 mg/ml of sodium phosphate (dibasic, anhydrous) and 0.4 mg/ml of polysorbate 20, pH-6.

    Purity

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

    Biological Activity

    The ED50 as determined by the proliferation inhibition of HUVEC cell, 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 1.1 X 104EU/mg.

    More Info

    • Introduction

      Vascular endothelial growth factoris an important signaling proteininvolved in both vasculogenesisand angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Physical Appearance

      Clear, colorless solution.

    • Stability

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

    • Amino Acid Sequence

      LIGHT CHAIN:
      DIQMTQSPSS LSASVGDRVT ITCSASQDIS NYLNWYQQKP GKAPKVLIYF TSSLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ YSTVPWTFGQ GTKVEIKRTV AAPSVFIFPP SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ ESVTEQDSKD STYSLSSTLT LSKADYEKHK VYACEVTHQG LSSPVTKSFN
      RGEC.

      HEAVY CHAIN:
      EVQLVESGGG LVQPGGSLRL SCAASGYTFT NYGMNWVRQA PGKGLEWVGW INTYTGEPTY AADFKRRFTF SLDTSKSTAY LQMNSLRAED TAVYYCAKYP HYYGSSHWYF DVWGQGTLVT VSSASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV TVSWNSGALT SGVHTFPAVL QSSGLYSLSS VVTVPSSSLG TQTYICNVNH KPSNTKVDKK VEPKSCDKTH TCPPCPAPEL
      LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS REEMTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS
      PGK.

    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 Vegf Antibody
  • View Data Sheet

    Name :

    TNFRSF6B Human

    Description:

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Human Recombinant

    Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    Product # :

    CYT-799

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    • description
    • source
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    Description

    TNFRSF6B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 294 amino acids (30-300aa) and having a molecular mass of 32.1kDa.TNFRSF6B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFRSF6B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFRSF6B is a member of the Tumor necrosis factor receptor superfamily. TNFRSF6B performs as a decoy receptor which races against death receptors for ligand binding. TNFRSF6B has a regulatory role in suppressing FasL- and LIGHT-mediated cell death and T cell activation in addition to inducing angiogenesis via neutralization of TL1A.

    • Synonyms

      Tumor Necrosis Factor Receptor Superfamily, Member 6b Decoy, Decoy Receptor For Fas Ligand, Decoy Receptor 3, DCR3, M68E, M68, TR6, DJ583P15.1.1, DcR3.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSVAETPTY PWRDAETGER LVCAQCPPGT FVQRPCRRDS PTTCGPCPPR HYTQFWNYLE RCRYCNVLCG EREEEARACH ATHNRACRCR TGFFAHAGFC LEHASCPPGA GVIAPGTPSQ NTQCQPCPPG TFSASSSSSE QCQPHRNCTA LGLALNVPGS SSHDTLCTSC TGFPLSTRVP GAEECERAVI DFVAFQDISI KRLQRLLQAL EAPEGWGPTP RAGRAALQLK LRRRLTELLG AQDGALLVRL LQALRVARMP GLERSVRERF LPVH.

    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.

    Tnfrsf6B Human
  • View Data Sheet

    Name :

    IFIT3 Human

    Description:

    IFN-Induced Protein With Tetratricopeptide Repeats 3 Human Recombinant

    IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.

    Product # :

    CYT-898

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    • description
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    Description

    IFIT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 513 amino acids (1-490 a.a) and having a molecular mass of 58.4kDa. IFIT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    IFIT3 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFN-Induced Protein With Tetratricopeptide Repeats 3, also known as IFIT3 is a member of the IFIT family. IFN-induced antiviral protein which performs as an inhibitor of cellular and viral processes, cell migration, proliferation, signaling, as well as viral replication. Furthermore, IFIT3 is significantly induced upon RNA virus infection. Ectopic expression or alternatively knockdown of IFIT3 might, respectively, enhance or impair IRF3-mediated gene expression.

    • Synonyms

      IFN-Induced Protein With Tetratricopeptide Repeats 3, IFN-Induced Protein With Tetratricopeptide Repeats 4, IFIT4, Retinoic Acid-Induced Gene G Protein, IFN-Induced 60 KDa Protein, IFI-60K, CIG-49, IFIT-3, IFIT-4, ISG-60, CIG49, IFI60, ISG60, RIG-G, P60, GARG-49, IRG2, IFN-induced protein with tetratricopeptide repeats 3.

    • 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 MGSMSEVTKN SLEKILPQLK CHFTWNLFKE DSVSRDLEDR VCNQIEFLNT EFKATMYNLL AYIKHLDGNN EAALECLRQA EELIQQEHAD QAEIRSLVTW GNYAWVYYHL GRLSDAQIYV DKVKQTCKKF SNPYSIEYSE LDCEEGWTQL KCGRNERAKV CFEKALEEKP NNPEFSSGLA IAMYHLDNHP EKQFSTDVLK QAIELSPDNQ YVKVLLGLKL QKMNKEAEGE QFVEEALEKS PCQTDVLRSA AKFYRRKGDL DKAIELFQRV LESTPNNGYL YHQIGCCYKA KVRQMQNTGE SEASGNKEMI EALKQYAMDY SNKALEKGLN PLNAYSDLAE FLETECYQTP FNKEVPDAEK QQSHQRYCNL QKYNGKSEDT AVQHGLEGLS ISKKSTDKEE IKDQPQNVSE NLLPQNAPNY WYLQGLIHKQ NGDLLQAAKC YEKELGRLLR DAPSGIGSIF LSASELEDGS EEMGQGAVSS SPRELLSNSE QLN.

    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.

    Ifit3 Human
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