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  • Cytokines
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  • Tumor Necrosis Factor

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    B-Cell Activating Factor

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    Beta Defensin

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  • Bone Morphogenetic Protein

    Bone Morphogenetic Protein

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  • B type Natriuretic Peptide

    B type Natriuretic Peptide

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  • BST

    BST

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    Betacellulin

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    Insulin-Like Growth Factor

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    BCA-1/ BLC (CXCL13)

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    C-10 (CCL6)

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  • MEC (CCL28)

    MEC (CCL28)

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  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

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    CTACK (CCL27)

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    CXCL16

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    Platelet Factor-4 (CXCL4)

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    ENA-78 (CXCL5)

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    Eotaxin (CCL11,24,26)

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    Fractalkine (CX3CL1)

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    Pigment Epithelium-Derived Factor

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  • Actin

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    Complement Component

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    Eukaryotic Translation Initiation Factor

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    Anterior Gradient Protein

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    Heat Shock Protein

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    Ankyrin Repeat Domain

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  • Annexin

    Annexin

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  • Other Natural Proteins

    Other Natural Proteins

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  • Aprotinin

    Aprotinin

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  • Transferrin

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  • Avidin

    Avidin

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  • Anti Coagulation Factors

    Anti Coagulation Factors

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  • Natural Albumin

    Natural Albumin

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    Natural Coagulation Factors

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    Anti Human Heat Shock Protein

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    Anti Mouse Lymphocyte

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Search results

676 results found for “nanog”

Name

Description

Product #

Price

Quantity

Shipping Method

  • View Data Sheet

    Name :

    RGS10 Human

    Description:

    Regulator of G-Protein Signaling 10 Human Recombinant

    Regulator Of G-Protein Signaling 10, RGS10.

    Product # :

    PRO-890

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    RGS10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (1-181) and having a molecular mass of 23.7 kDa.The RGS10 is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RGS10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RGS10 is a member of the RGS family that regulate molecules which perform as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins can disengage G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. The nucleus localized RGS10 is associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but is unable to cooperate with the structurally and functionally distinct G-alpha subunits.

    • Synonyms

      Regulator Of G-Protein Signaling 10, RGS10.

    • 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 MGSHMFNRAV SRLSRKRPPS DIHDSDGSSS SSHQSLKSTA KWAASLENLL EDPEGVKRFR EFLKKEFSEE NVLFWLACED FKKMQDKTQM QEKAKEIYMT FLSSKASSQV NVEGQSRLNE KILEEPHPLM FQKLQDQIFN LMKYDSYSRF LKSDLFLKHK RTEEEEEDLP DAQTAAKRAS RIYNT

    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.

    Rgs10 Human
  • View Data Sheet

    Name :

    HSA Recombinant, Plant

    Description:

    Human Serum Albumin Recombinant, Plant

    Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    Product # :

    PRO-595

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    HSA Human Recombinant produced in Plant is a non-glycosylated, polypeptide chain containing 585 amino acids and having a molecular mass of 67 kDa. The optimum concentration for recombinant Albumin to be used in cell culture ranges between 0.5gr to 2gr per liter. The recombinant Albumin is purified by proprietary chromatographic techniques.

    Source

    Rice Grain.

    Formulation

    The Recombinant Albumin was lyophilized with sodium chloride. A 10% w/v solution when dissolved in water will contain 50mM NaCl.

    Purity

    Greater than 98% as determined by SDS-PAGE.

    More Info

    • Introduction

      Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume. Mutations in this gene on chromosome 4 result in various anomalous proteins. Albumin is a globular unglycosylated serum protein of molecular weight 65,000. The human albumin gene is 16,961 nucleotides long from the putative 'cap' site to the first poly (A) addition site. It is split into 15 exons which are symmetrically placed within the 3 domains that are thought to have arisen by triplication of a single primordial domain.
      HSA is widely used to stabilize blood volume generally from donors but the fear of contamination such as HIV & Hepatitis has enticed great interest in the recombinant form which is identical to the natural blood.

    • Synonyms

      Serum albumin, ALB, PRO0883, PRO0903, PRO1341, DKFZp779N1935, GIG20, GIG42, PRO1708, PRO2044, PRO2619, PRO2675, UNQ696, SA, HSA.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Recombinant Albumin although stable at 4°C for 3 weeks, should be stored at -18°C.Please prevent freeze-thaw cycles.

    • Applications

      Recombinant Albumin can be used as a media culture supplement at concentrations up to 5 grams per liter. Gradual adaptation of cell lines over several passages to a concentration of 0.5gr to 2gr per liter.

    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.

    Hsa Plant
  • View Data Sheet

    Name :

    RELM g Mouse, His

    Description:

    RELM-Gamma Mouse Recombinant, His Tag

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

    Product # :

    CYT-455

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.The lyophilized protein remains stable until the expiry date when stored at -20°C.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

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

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

    Relm Gamma Mouse
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    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.

    Avidin Recombinant
  • View Data Sheet

    Name :

    Ice pack

    Description:

    Antibacterial Gel Ice Pack

    Product # :

    ICE-002

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • More Info
    • about & Applications

    Description

    Antibacterial Gel Ice Pack
    Optimized for:
    • Life Science
    • Pharmaceuticals
    • Diagnostics
    • Lab Samples
    • Air Freight
    • Food Logistics
    • Agriculture
    • Healthcare
    • Medical Freight

    Dimensions: 20 X 15 cm , 7.9 × 5.9 inches
    Volume: ~500ml , 16.9 fl.oz
    Dry Weight: 12 gr

    For more information & How to Use

    about & Applications

    Ice Pack - Product image 1
    Ice Pack Applications - Product image 2
    Ice Pack How to use - Product image 3

    More Info

    • Introduction

      We save you transport fees !
      The ice packs are supplied dry/powder form.
      Each ice packs weighs only 12g.
      Once filled with water, can hold up to 500ml of water.

      Unique Features:
      2 layer thin vinyl
      1 way valve
      Repeatable freeze: thaw durability for professional cold-chain reliability
      Leak-free
      Puncture-Resistant
      Flexible outer film for safe transportation

    • Background

      1. What are gel ice packs used for?
      Gel ice packs are used to keep temperature-sensitive products cold during transportation. They are widely used for shipping recombinant proteins, antibodies, enzymes, reagents, biological samples, diagnostic kits, pharmaceuticals, vaccines, and other laboratory materials that require refrigerated conditions.
      ProSpec gel ice packs provide a reliable cooling source when used together with insulated shipping boxes, helping maintain the cold chain throughout transit.

      2. What are the best gel ice packs for shipping laboratory samples?
      The best gel ice packs provide long-lasting cooling, are reusable, leak-resistant, and maintain a stable temperature throughout transportation.
      For 30 years, ProSpec has used its own gel ice packs to ship laboratory products worldwide. Designed specifically for research and biotechnology applications, they help protect valuable temperature-sensitive products during domestic and international shipping.

      3. How do I keep biological samples cold during shipping?
      To maintain sample integrity, biological materials should be shipped inside a high-performance insulated shipping box together with properly frozen gel ice packs.
      For maximum thermal protection, ProSpec recommends combining its reusable gel ice packs with insulated shipping boxes constructed using Vacuum Insulated Panel (VIP) technology, which significantly reduces heat transfer and extends cooling performance.

      4. How long do gel ice packs stay cold?
      Cooling duration depends on several factors, including:
      • Number of gel ice packs
      • Type of insulated packaging
      • Ambient temperature
      • Shipment weight
      • Transit time
      Using ProSpec VIP insulated packaging together with ProSpec gel ice packs can significantly extend cooling duration compared to conventional insulated packaging.

      5. Are ProSpec gel ice packs reusable?
      Yes.
      ProSpec gel ice packs are designed for repeated use. After delivery, simply refreeze them before the next shipment.
      Reusable cooling packs reduce packaging costs, minimize waste, and provide an environmentally friendly solution for cold chain shipping.

      6. What are the advantages of gel ice packs compared to regular ice?
      Gel ice packs offer several important advantages over conventional ice:
      • Leak-resistant
      • Less risk of water damage
      • Reusable
      • Easy to freeze and store
      • Longer-lasting cooling
      • More uniform temperature distribution
      • Antibacterial material
      • Cleaner handling during shipping
      Unlike pre-filled packs, ProSpec gel ice packs are supplied as a powder. Simply add water, seal the pack, freeze it, and it is ready for use.

      7. What products should be shipped with gel ice packs?
      Gel ice packs are recommended for shipping:
      • Recombinant proteins
      • Cytokines
      • Growth factors
      • Antibodies
      • Enzymes
      • ELISA kits
      • Cell culture reagents
      • Diagnostic kits
      • Clinical samples
      • Biological specimens
      • Pharmaceuticals
      • Temperature-sensitive laboratory reagents

      8. How many gel ice packs do I need for shipping?
      The required number depends on:
      • Package dimensions
      • Shipping duration
      • Outside temperature
      • Product weight
      • Required storage temperature
      As a general guideline, approximately 30% to 40% of the insulated box volume should be occupied by gel ice packs. ProSpec can help determine the optimal configuration for your application.

      9. Are gel ice packs suitable for international shipping?
      Yes.
      ProSpec gel ice packs are designed for both domestic and international shipments. When combined with ProSpec VIP insulated shipping boxes, they help maintain cold chain integrity during long transportation routes, customs clearance, and unexpected shipping delays.

      10. Why choose ProSpec gel ice packs?
      ProSpec has been shipping temperature-sensitive research products around the world for more than two decades.
      Our cooling solutions are trusted because they provide:
      • Reliable cooling performance
      • Long-lasting temperature protection
      • Reusable design
      • Easy preparation and handling
      • Compatibility with VIP insulated shipping boxes
      • Ideal protection for laboratory, biotechnology, pharmaceutical, and diagnostic products
      • Proven performance in worldwide cold chain logistics

    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.

    Ice Pack ProSpecBio
  • View Data Sheet

    Name :

    H3N2 Hong Kong Recombinant

    Description:

    H3N2 Influenza A- Virus Hong Kong 4801/2014 Recombinant

    Product # :

    IHA-043

    Price :

    Quantity :

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    • description
    • source
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    Description

    Recombinant Full-Length H3N2 Hong Kong 4801/2014 is glycosylated with N-linked sugars, produced using baculovirus vectors in insect cells.

    Source

    Baculovirus Insect Cells.

    Formulation

    The Recombinant H3N2 A/ Hong Kong 4801/2014 solution contains 10mM Sodium phosphate, pH 7.4,150mM NaCl and 0.005% Tween-20.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      H3N2 is a subtype of the influenza A virus. Its name derives from the forms of the two kinds of proteinson the surface of its coat, hemagglutinin(H) and neuraminidase(N). H3N2 exchanges genes for internal proteins with other influenza subtypes. H3N2 has tended to dominate in prevalence over H1N1, H1N2, and influenza B. H3N2 strain descended from H2N2 by antigenic shift, in which genes from multiple subtypes re-assorted to form a new virus. Both the H2N2and H3N2 strains contained genesfrom avian influenzaviruses.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      H3N2 A/ Hong Kong 4801/2014 recombinant should be stored at 4°C. Do not freeze!

    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.

    H3N2 Hong Kong Recombinant
  • View Data Sheet

    Name :

    Recombinant VEGF Antibody

    Description:

    Recombinant Human Anti Vascular Endothelial Growth Factor

    Product # :

    ANT-601

    Price :

    Quantity :

    Shipping Method :

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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 :

    CCN1 Human

    Description:

    Cysteine-Rich Angiogenic Inducer 61 Human Recombinant

    CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    Product # :

    CYT-164

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    Description

    CYR61 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 357 amino acids and having a molecular mass of 39.5kDa.The CYR61 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

    More Info

    • Introduction

      CYR61 is a growth factor-inducible, immediate-early gene that has multifaceted activities in various cancers. CYR61 is a secreted, cysteine-rich, binding protein which is encoded by a growth factor-inducible immediate-early gene. Acting as an extracellular, matrix-associated signaling molecule, CYR61 promotes the adhesion of endothelial cells through interaction with integrin and enhances growth factor-induced DNA synthesis in the same cell type.

    • Synonyms

      CYR61, Protein CYR61, Cysteine-rich angiogenic inducer 61, IGF-binding protein 10, IGFBP-10, IBP-10, Protein GIG1, CCN family member 1, CCN1, GIG1, IGFBP10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CYR61 Human although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CYR61 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 CYR61 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
      PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

    • Background

      Title: Cysteine-Rich Angiogenic Inducer 61 Human Recombinant: A Potential Regulator of Angiogenesis

      Abstract:


      Cysteine-rich angiogenic inducer 61 (CYR61) is an important extracellular matrix-associated protein that plays a significant role in angiogenesis and cell adhesion. This research paper provides a comprehensive analysis of human recombinant CYR61, focusing on its production, characterization, and potential applications in regulating angiogenesis. The paper discusses the significance of CYR61 in physiological and pathological angiogenesis, including wound healing, tumor development, and cardiovascular diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYR61 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYR61 and its utility as a research tool and a potential regulator of angiogenesis.

      Introduction:


      Cysteine-rich angiogenic inducer 61 (CYR61) is an extracellular matrix-associated protein that plays a crucial role in angiogenesis, the formation of new blood vessels from pre-existing ones. Human recombinant CYR61, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CYR61 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYR61.

      Role in Angiogenesis:


      CYR61 is involved in various aspects of angiogenesis, including endothelial cell proliferation, migration, and tube formation. It interacts with integrins and other cell surface receptors to modulate signaling pathways involved in angiogenic processes. Recombinant CYR61 serves as a valuable tool for studying the mechanisms underlying angiogenesis and exploring its potential as a therapeutic target.

      Therapeutic Implications:


      The dysregulation of angiogenesis is associated with several pathological conditions, including cancer, cardiovascular diseases, and chronic wounds. Recombinant CYR61 has shown promise as a potential regulator of angiogenesis and a therapeutic agent. It can be used to promote or inhibit angiogenesis, depending on the specific context. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYR61 in various diseases, including cancer and ischemic disorders.

      Conclusion:


      Human recombinant CYR61 is a valuable research tool and a potential regulator of angiogenesis. Its production, characterization, and applications in modulating angiogenic processes contribute to our understanding of angiogenesis and the development of novel therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYR61 offer promising prospects for improving outcomes in cancer, cardiovascular diseases, and wound healing.

      What is the molecular weight/Mw of CCN1 Protein?
      CCN1 Protein has a total Mw of 39.5kDa.

      What is the source or expression system of CCN1 Protein?
      Escherichia Coli.

      What is the Purity of CCN1 Protein?
      CCN1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCN1 Protein?
      The ED50 was determined by the proliferation of mouse 3T3 cells is < 2.0 ug/ml, corresponding to a specific activity of > 500 units/mg.

      What is the amino acid sequence of CCN1 Protein?
      TCPAACHCPL EAPKCAPGVG LVRDGCGCCK VCAKQLNEDC SKTQPCDHTK GLECNFGASS TALKGICRAQ SEGRPCEYNS RIYQNGESFQ PNCKHQCTCI DGAVGCIPLC PQELSLPNLG CPNPRLVKVT GQCCEEWVCD EDSIKDPMED QDGLLGKELG FDASEVELTR NNELIAVGKG SSLKRLPVFG MEPRILYNPL QGQKCIVQTT SWSQCSKTCG TGISTRVTND NPECRLVKET RICEVRPCGQ PVYSSLKKGK KCSKTKKSPE PVRFTYAGCL SVKKYRPKYC GSCVDGRCCT
      PQLTRTVKMR FRCEDGETFS KNVMMIQSCK CNYNCPHANE AAFPFYRLFN DIHKFRD

      What applications can CCN1 Protein be used in?
      CCN1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCN1 Protein?
      The endotoxin level is minimal, CCN1 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.

    Cyr61 Human
  • View Data Sheet

    Name :

    ARTN Human

    Description:

    Artemin Human Recombinant

    ART, ARTN , EVN, NBN.

    Product # :

    CYT-306

    Price :

    Quantity :

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    Description

    Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.

    Purity

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

    Biological Activity

    The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

    More Info

    • Introduction

      The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.

    • Synonyms

      ART, ARTN , EVN, NBN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

    • Background

      Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications

      Abstract:

      Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.

      Introduction:

      Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.

      Artemin Signaling and Mechanisms:

      Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.

      Artemin in Neurological Disorders:

      Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.

      Therapeutic Potential of Artemin Human Recombinant:

      Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.

      Challenges and Future Directions:

      While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.

      Conclusion:

      Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.

      What is the molecular weight/Mw of ARTN Protein?
      ARTN Protein has a total Mw of 24.2kDa.

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

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

      What is the Biological Activity of ARTN Protein?
      The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.

      What is the amino acid sequence of ARTN Protein?
      AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.

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

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

    Artemin Human
  • View Data Sheet

    Name :

    ELOB Mouse

    Description:

    Elongin B Mouse Recombinant

    Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

    Product # :

    PRO-2550

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    Description

    ELOB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 141 amino acids ( 1-118 a.a.) having a molecular mass of 15.6 kDa. The Recombinant Mouse ELOB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains PBS pH-7.4 containing 1mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elongin B (Elob) is a subunit of the transcription factor B (SIII) complex. SIII complex is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. The SIII complex comprised of a transcriptionally active subunit (A) and 2 regulatory subunits (B and C). Subunit A is transcriptionally active and its transcription activity is enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C. The von Hippel-Lindau tumor suppressor protein binds to elongin B and C and inhibits transcription elongation.

    • Synonyms

      Transcription elongation factor B polypeptide 2, TCEB2, RNA polymerase IItranscription factor SIII subunit B, SIII p18, EloB, Elongin 18 kDa subunit.

    • 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 MGSMDVFLMI RRHKTTIFTD AKESSTVFEL KRIVEGILKR PPEEQRLYKD DQLLDDGKTL GECGFTSQTA RPQAPATVGL AFRADDTFEA LRIEPFSSPP ELPDVMKPQD SGGSANEQAV Q

    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.

    Elongin B Human
  • View Data Sheet

    Name :

    NUP210 Human

    Description:

    Nucleopurin 210kDa Recombinant Human

    Nucleoporin 210kDa, KIAA0906, GP210, Nuclear envelope pore membrane protein POM 210, Nuclear pore protein gp210, nuclear pore membrane glycoprotein 210.

    Product # :

    PRO-109

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    Description

    Recombinant NUP210 protein is a construct carrying multiple concatenated copies of the short cytoplasmic gp210 C-terminus (which contains the autoreactive epitopes) and having a molecular mass of 27kDa (pH 9.8). NUP210 protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    NUP210 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      The NUP210 complex is a immense structure which spreads through the nuclear envelope, forming a doorway which regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the core components of the nuclear pore complex in eukaryotic cells. NUP210 is a membrane-spanning glycoprotein and is a major component of the nuclear pore complex.

    • Synonyms

      Nucleoporin 210kDa, KIAA0906, GP210, Nuclear envelope pore membrane protein POM 210, Nuclear pore protein gp210, nuclear pore membrane glycoprotein 210.

    • Stability

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

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test.

    • coating concentration

      0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with PBC sera or monoclonal anti-hexa-His-tag antibody.

    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.

    Nup210 Human
  • View Data Sheet

    Name :

    IL36G Mouse

    Description:

    Interleukin-36 Gamma Mouse Recombinant

    Interleukin-36 gamma, Interleukin-1 family member 9, IL-1F9, Il36g, Il1f9.

    Product # :

    CYT-745

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    • More Info

    Description

    IL36G Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 17.3kDa.The IL36G is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1M MOPS, 10 mM NaAC, pH7.6, 5 % Trehalose, 2 mM EDTA and 0.02 % Tween-20.

    Purity

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

    More Info

    • Introduction

      IL-36gamma belongs to the IL-1 family which includes IL-1b, IL-1a, IL-1ra, IL-18, IL-36 Ra (IL-1F5), IL-36a (IL-1F6), IL-36b (IL-1F8), IL-37 (IL-1F7) and 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. IL-36g is an 18-22 kDa, 169aa intracellular and secreted protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation sites. Human IL-36g shares 58%- 69% aa sequence homology with mouse, rat, bovine and equine IL-36g, and 23 - 57% aa sequence homology with other family members. The IL-36g receptor is a mixture of IL-1 Rrp2, mostly located in epithelia and keratinocytes, and the extensively expressed IL-1 RAcP. All IL-36 (a, b and g) activate N F-?B and MAPK pathways in an IL-1 Rrp2 dependent reaction. Additionally, IL-36g induces production of inflammatory cytokines and chemokines like CXCL8/IL-8.

    • Synonyms

      Interleukin-36 gamma, Interleukin-1 family member 9, IL-1F9, Il36g, Il1f9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL36g Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL36g 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 IL36g in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GRETPDFGEV FDLDQQVWIF RNQALVTVPR SHRVTPVSVT ILPCKYPESL EQDKGIAIYL GIQNPDKCLF CKEVNGHPTL LLKEEKILDL YHHPEPMKPF LFYHTRTGGT STFESVAFPG HYIASSKTGN PIFLTSKKGE YYNINFNLDI KS.

    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.

    Il36G Mouse
  • View Data Sheet

    Name :

    IL36RN Mouse

    Description:

    Interleukin-36 Receptor Antagonist Mouse Recombinant

    Product # :

    CYT-154

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    Description

    IL36RN Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a molecular mass of 17.0kDa.The IL36RN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. Measured by its ability to inhibit IL-36a, IL-36b or IL-36g induced IL-6 secretion by NIH-3T3 mouse embryonic fibroblast cells. The ED50 for this effect is typically 0.8-4ug/ml (corresponding to a specific activity of 250-125units/mg) in the presence of 15ng/ml of recombinant mouse IL-36b.

    More Info

    • Introduction

      IL36RA belongs to the IL-1 family of proteins. IL36RA is produced as a 156 aa protein which holds no signal sequence, no prosegment and no potential N-linked glycosylation site but, IL36RA is secreted as a 17 kDa monomer. Cells known to express IL36Ra/IL1F5 include monocytes, B cells, keratinocytes, dendritic cells/Langerhans cells and gastric fundus Parietal and Chief cells.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL 36RN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL 36RN 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 IL36RN in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAEKVIKGEE ISVVPNRALD ASLSPVILGV QGGSQCLSCG TEKGPILKLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTSPEADQPV RLTQIPEDPA WDAPITDFYF QQCD

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    Il36Ra Mouse
  • View Data Sheet

    Name :

    IFNG Equine

    Description:

    Interferon-Gamma Equine Recombinant

    Interferon gamma, IFN-gamma, IFNG.

    Product # :

    CYT-739

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    Description

    Recombinant Equine Interferon-gamma produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 143 amino acids and having a molecular mass of 16.7kDa.The IFN-gamma Equine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

    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 an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

    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 I interferons.

    • Synonyms

      Interferon gamma, IFN-gamma, IFNG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interferon-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 Interferon-gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ.

    • Background

      What is the molecular weight/Mw of IFNG EQUINE Protein?
      IFNG EQUINE Protein has a total Mw of 16.7kDa.

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

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

      What is the Biological Activity of IFNG EQUINE Protein?
      The ED50 as determined by an anti-viral assay using human HeLa cells infected with encephalomyocarditis (EMC) virus is less than 10.0 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

      What is the amino acid sequence of IFNG EQUINE Protein?
      QAAFFKEIEN LKEYFNASNP DVGDGGPLFL DILKNWKEDS DKKIIQSQIV SFYFKLFENL KDNQVIQKSM DTIKEDLFVK FFNSSTSKLE DFQKLIQIPV NDLKVQRKAI SELIKVMNDL SPKANLRKRK RSQNPFRGRR ALQ.
      What applications can IFNG EQUINE Protein be used in?
      IFNG EQUINE Protein can probably be used in western blot, ELISA and Lateral Flow.

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


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    Interferon Gamma Equine
  • View Data Sheet

    Name :

    FCGR3A Human

    Description:

    CD16a Human Recombinant

    Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.

    Product # :

    PRO-1150

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    Description

    FCGR3A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (18-208 a.a) and having a molecular mass of 26kDa.FCGR3A is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    FCGR3A protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.

    • Synonyms

      Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.

    • 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 KDRWGSHMRT EDLPKAVVFL EPQWYRVLEK DSVTLKCQGA YSPEDNSTQW FHNESLISSQ ASSYFIDAAT VDDSGEYRCQ TNLSTLSDPV QLEVHIGWLL LQAPRWVFKE EDPIHLRCHS WKNTALHKVT YLQNGKGRKY FHHNSDFYIP KATLKDSGSY FCRGLFGSKN VSSETVNITI TQGLAVSTIS SFFPPGYQ.

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    Fcgr3A Human
  • View Data Sheet

    Name :

    IL36RN Human

    Description:

    Interleukin-36 Receptor Antagonist Human Recombinant

    Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    Product # :

    CYT-009

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    Description

    IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

    Purity

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

    Biological Activity

    As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

    More Info

    • Introduction

      Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

    • Synonyms

      Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/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-Val-Leu-Ser-Gly.

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

    Il1F5 Human
  • View Data Sheet

    Name :

    TNF a Canine

    Description:

    Tumor Necrosis Factor-Alpha Canine Recombinant

    Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    Product # :

    CYT-140

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    Description

    TNF-a Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.3 kDa. The TNF-a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    The Specific Activity is >3.3×105 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    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, tumorigenesis and 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.

    • Synonyms

      Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VKSSSRTPSD KPVAHVVANP EAEGQLQWLS RRANALLANG VELTDNQLIV PSDGLYLIYS QVLFKGQGCP STHVLLTHTI SRFAVSYQTK VNLLSAIKSP CQRETPEGTE AKPWYEPIYL GGVFQLEKGD RLSAEINLPN YLDFAESGQV YFGIIAL.

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    Tnf A Canine
  • View Data Sheet

    Name :

    TNF a Rhesus Macaque

    Description:

    Tumor Necrosis Factor-Alpha Rhesus Macaque Recombinant

    Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    Product # :

    CYT-737

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    Description

    TNF-a Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17.3kDa.The TNFA Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4 and 5% trehalose.

    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 a cytotoxicity assay using murine L929 cells is less than 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg in the presence of actinomycin D.

    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, tumorigenesis and 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.

    • Synonyms

      Tumor necrosis factor, Cachectin, TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, TNF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VRSSSRTPSD KPVAHVVANP QAEGQLQWLN RRANALLANG VELTDNQLVV PSEGLYLIYS QVLFKGQGCP SNHVLLTHTI SRIAVSYQTK VNLLSAIKSP CQRETPEGAE AKPWYEPIYL GGVFQLEKGD RLSAEINLPD YLDFAESGQV YFGIIAL.

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    Tnf A Rhesus Macaque
  • View Data Sheet

    Name :

    TNFR (22-211) Human

    Description:

    Tumor Necrosis Factor Receptor (22-211 a.a.) Human Recombinant

    CD120a, FPF, MS5, p55, p55-R, p60, TBP1, TNF-R, TNF-R-I, TNF-R55, TNFAR, TNFR1, TNFR1-d2,TNFR55, TNFR60, Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor superfamily member 1A.

    Product # :

    CYT-851

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    Description

    TNFR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (22-211 a.a) and having a molecular mass of 23.6kDa.TNFR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFR protein solution (1mg/ml) containing 20mM Tirs-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TNFR1 belongs to the TNF-receptor superfamily. TNFR1 is a receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha.
      There are 2 types of soluble TNF receptors: sTNFR-I and sTNFR-II, which act to neutralize the biological activities of TNF alpha and TNF beta. The levels of these soluble receptors seem to increase as a result of shedding of the extracellular domains of the membrane bound receptors. TNF-a, TNFR1 and TNFR2 have roles in cellular differentiation. TNFR1 and TNFR2 function in cell type-specific renal injury.
      TNFR1 is capable of signaling both cell survival and apoptosis. TNFR1-induced apoptosis requires 2 sequential signaling complexes. TNFR1 is capable of activating NF-kappaB, mediate apoptosis, and function as a regulator of inflammation. Oxidative stress promotes TNFR1 and TNFR2 self-interaction, ligand-independent and enhanced ligand-dependent TNF signaling. TNFR1 contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase. Human TNFR1 has a major region which controls cell surface expression. High levels of soluble TNF receptors are found in the amniotic fluid of pregnant women.
      Germline mutations of the extracellular domains of TNFR1 are linked to the autosomal dominant periodic fever syndrome. The impaired receptor clearance is believed to be a mechanism of the disease. Familial hibernian fever (FHF) is caused by defects in TNFRSF1A gene.

    • Synonyms

      CD120a, FPF, MS5, p55, p55-R, p60, TBP1, TNF-R, TNF-R-I, TNF-R55, TNFAR, TNFR1, TNFR1-d2,TNFR55, TNFR60, Tumor necrosis factor receptor superfamily member 1A, Tumor necrosis factor receptor superfamily member 1A.

    • 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 MGSIYPSGVI GLVPHLGDRE KRDSVCPQGK YIHPQNNSIC CTKCHKGTYL YNDCPGPGQD TDCRECESGS FTASENHLRH CLSCSKCRKE MGQVEISSCT VDRDTVCGCR KNQYRHYWSE NLFQCFNCSL CLNGTVHLSC QEKQNTVCTC HAGFFLRENE CVSCSNCKKS LECTKLCLPQ IENVKGTEDS GTT.

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    Tnfr 22 211 Human
  • 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

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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 :

    TNFSF14 Mouse

    Description:

    LIGHT Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 14, CD258, Tnfsf14, Light.

    Product # :

    CYT-826

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    • source
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    Description

    TNFSF14 Mouse Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids and having a molecular mass of 18.4kDa.

    Source

    Escherichia Coli.

    Formulation

    TNFSF14 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4.

    Purity

    Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cytotoxicity assay using human HT-29 cells is less than 2µg/ml, corresponding to a specific activity of > 500 IU/mg in the presence of murine anti-polyHistidine monoclonal antibody and rHuIFN-g.

    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 ligand superfamily member 14, CD258, Tnfsf14, Light.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNFSF14 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 TNFSF14 in sterile 100mM HAc not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DGGKGSWEKL IQDQRSHQAN PAAHLTGANA SLIGIGGPLL WETRLGLAFL RGLTYHDGAL VTMEPGYYYV YSKVQLSGVG CPQGLANGLP ITHGLYKRTS RYPKELELLV SRRSPCGRAN SSRVWWDSSF LGGVVHLEAG EEVVVRVPGN RLVRPRDGTR SYFGAFMV.

    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.

    Tnfsf14 Mouse
  • View Data Sheet

    Name :

    Leptin tA Mouse, PEG

    Description:

    Leptin Antagonist Triple Mutant Pegylated Mouse Recombinant

    Product # :

    CYT-566

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa.The Mouse Leptin antagonist was mutated, resulting in L39A/D40A/F41A mutant.The Mouse Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Mouse Leptin triple anatagonist runs as a 48 kDa.Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin triple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Antagonist Triple Mutant Mouse Recombinant half-life in circulation after SC injection was over 20 hours.
    Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Leptin Antagonist Triple Mutant Mouse Recombinant in vitro activity is 5-6 fold lower than the non-pegylated antagonist, though in vivo it has profound weight gain effect (as compared to the non-pegylated antagonist), resulting mainly from increased food intake.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Mouse Peg
  • View Data Sheet

    Name :

    ANPEP Mouse

    Description:

    Alanyl Aminopeptidase Membrane Mouse Recombinant

    Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.

    Product # :

    ENZ-1134

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    Description

    ANPEP Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 943 amino acids (33-966 a.a.) and having a molecular mass of 107.5 kDa. ANPEPis expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ANPEP protein solution ( 0.5mg/ml ) contains PBS (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 4,000pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1pmole of H-AlaAMC to Alanine and AMC per minute at pH7.5 at 25C.

    More Info

    • Introduction

      ANPEP or aminopeptidase N, is an enzyme, found in the small-intestinal and renal microvillar membrane and other plasma membranes. The enzyme has a critical part in the digestion of peptides after their hydrolysis by gastric and pancreatic proteases. ANPEP is also part ofthe processing of different peptides as well as peptide hormones, neuropeptides & chemokines. The protein takes part in angiogenesis, enhancing cholesterol crystallization &amino acid transport by formatting with SLC6A19 transport protein and regulating its activity.

    • Synonyms

      Anpep, AP-M, AP-N, Apn, Cd13, P150, mAPN, Alanyl aminopeptidase, Aminopeptidase M, Membrane protein p161, Microsomal aminopeptidase, CD13, Lap-1, Lap1, aminopeptidase N.

    • 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

      ADPYAQEKNR NAENSATAPT LPGSTSATTA TTTPAVDESK PWNQYRLPKT LIPDSYRVIL RPYLTPNNQG LYIFQGNSTV RFTCNQTTDV IIIHSKKLNY TLKGNHRVVL RTLDGTPAPN IDKTELVERT EYLVVHLQGS LVEGRQYEMD SQFQGELADD LAGFYRSEYM EGDVKKVVAT TQMQAADARK SFPCFDEPAM KAMFNITLIY PNNLIALSNM LPKESKPYPE DPSCTMTEFH STPKMSTYLL AYIVSEFKNI SSVSANGVQI GIWARPSAID EGQGDYALNV TGPILNFFAQ HYNTSYPLPK SDQIALPDFN AGAMENWGLV TYRESSLVFD SQSSSISNKE RVVTVIAHEL AHQWFGNLVT VAWWNDLWLN EGFASYVEYL GADYAEPTWN LKDLMVLNDV YRVMAVDALA SSHPLSSPAD EIKTPDQIME LFDSITYSKG ASVIRMLSSF LTEDLFKKGL SSYLHTYQYS NTVYLDLWEH LQKAVNQQTA VQPPATVRTI MDRWILQMGF PVITVNTNTG EISQKHFLLD SKSNVTRPSE FNYIWIAPIP FLKSGQEDHY WLDVEKNQSA KFQTSSNEWI LLNINVTGYY LVNYDENNWK KLQNQLQTDL SVIPVINRAQ IIHDSFNLAS AKMIPITLAL DNTLFLVKEA EYMPWQAALS SLNYFTLMFD RSEVYGPMKR YLKKQVTPLF FYFQNRTNNW VNRPPTLMEQ YNEINAISTA CSSGLKECRD LVVELYSQWM KNPNNNTIHP NLRSTVYCNA IAFGGEEEWN FAWEQFRNAT LVNEADKLRS ALACSKDVWI LNRYLSYTLN PDYIRKQDTT STIISIASNV AGHPLVWDFV RSNWKKLFEN YGGGSFSFAN LIQGVTRRFS SEFELQQLEQ FKADNSATGF GTGTRALEQA LEKTRANIDW VKENKDAVFK WFTENSSHHH 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.

    Anpep Protein Mouse
  • View Data Sheet

    Name :

    CNTF Mouse

    Description:

    Ciliary-Neurotrophic Factor Mouse Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-139

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    Description

    Ciliary Neurotrophic Factor Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6kDa. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM

    • Background

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22.6kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.

      What is the amino acid sequence of CNTF Protein?
      MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM

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

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

    Cntf Mouse
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