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Search results

638 results found for “mip (ccl3,4,9,15)”

Name

Description

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  • View Data Sheet

    Name :

    COMMD9 Human

    Description:

    COMM Domain Containing 9 Human Recombinant

    COMM Domain Containing Protein 9, FLJ31106, HSPC166, COMM9.

    Product # :

    PRO-1244

    Price :

    Quantity :

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    • description
    • source
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    Description

    COMMD9 Human Recombinant produced in E. coli is a single polypeptide chain containing 221 amino acids (1-198) and having a molecular mass of 24.2 kDa. COMMD9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The COMMD9 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      COMM domain-containing protein 9 (COMMD9), is a part of the COMMD family. The COMMD family is a group of evolutionary conserved proteins that share a common COMM domain at their extreme C-terminus, which provides an interface for protein-protein interactions. COMMD9 is a 198 amino acid ubiquitously expressed protein which contains one COMM domain and involved in signaling events all over the cell.

    • Synonyms

      COMM Domain Containing Protein 9, FLJ31106, HSPC166, COMM9.

    • 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 MGSMAALTAE HFAALQSLLK ASSKDVVRQL CQESFSSSAL GLKKLLDVTC SSLSVTQEEA EELLQALHRL TRLVAFRDLS SAEAILALFP ENFHQNLKNL LTKIILEHVS TWRTEAQANQ ISLPRLVDLD WRVDIKTSSD SISRMAVPTC LLQMKIQEDP SLCGDKPSIS AVTVELSKET LDTMLDGLGR IRDQLSAVAS K.

    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.

    Commd9 Human
  • View Data Sheet

    Name :

    CNTF Human

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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    • source
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    • biological activity
    • More Info
    • Citations

    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    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 stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    Citations

    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 HCNTF 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-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

      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.

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of CNTF Recombinant 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.

    Cntf Human
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.

    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.

    Cfl2 Human
  • View Data Sheet

    Name :

    CTHRC1 Human, Sf9

    Description:

    Collagen Triple Helix Repeat Containing 1 Human Recombinant, Sf9

    Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    Product # :

    PRO-2606

    Price :

    Quantity :

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    • description
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    Description

    CTHRC1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 222 amino acids (31-243a.a.) and having a molecular mass of 24.1kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). CTHRC1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTHRC1 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Collagen triple helix repeat-containing protein 1 or CTHRC1 acts as a negative regulator of collagen matrix deposition. The protein is secreted from a 28kDa protein which is glycosylated and very conserved from lower chordates to mammals. CTHRC1 is found qualitatively in plasma of healthy human subjects. CTHRC1 plasma levels are also significantly elevated during pregnancy, in diabetes, in inflammatory and infectious conditions, in subjects with acute myeloid leukemia but not in subjects with solid cancers.CTHRC1 is highly connected with calcified tissues and cartilaginous matrix, but not with endothelial cells.

    • Synonyms

      Collagen triple helix repeat-containing protein 1 isoform 1, CTHRC1, Protein NMTC1.

    • 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

      ADPSEIPKGK QKAQLRQREV VDLYNGMCLQ GPAGVPGRDG SPGANGIPGT PGIPGRDGFK GEKGECLRES FEESWTPNYK QCSWSSLNYG IDLGKIAECT FTKMRSNSAL RVLFSGSLRL KCRNACCQRW YFTFNGAECS GPLPIEAIIY LDQGSPEMNS TINIHRTSSV EGLCEGIGAG LVDVAIWVGT CSDYPKGDAS TGWNSVSRII IEELPKHHHH 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.

    Cthrc1 Protein
  • View Data Sheet

    Name :

    C4BPB Human

    Description:

    Complement Component 4 Binding Protein, Beta Human Recombinant

    C4b-binding protein beta chain, C4BPB, C4BP.

    Product # :

    PRO-1174

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    Description

    C4BPB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (18-252 a.a) and having a molecular mass of 29kDa.C4BPB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    C4BPB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Complement Component 4 Binding Protein, Beta (C4BPB) belongs to a superfamily of proteins composed primarily of tandemly arrayed short consensus repeats of approximately 60 amino acids. C4BPB has a regulatory role in the coagulation system also, mediated via the beta-chain binding of protein S, a vitamin K-dependent protein which functions as a cofactor of activated protein C. A single, unique beta-chain of the C4BPB assembles with 7 identical alpha-chains into the principal isoform of C4BPB, which is a multimeric protein that controls activation of the complement cascade via the classical pathway. C4BPB binds as a cofactor to C3b/C4b inactivator (C3bINA), which subsequently hydrolyzes the complement fragment C4b. In addition, C4BPB accelerates the degradation of the C4bC2a complex (C3 convertase) by detaching the complement fragment C2a. Furthermore, C4BPB interacts with anticoagulant protein S and with serum amyloid P component.

    • Synonyms

      C4b-binding protein beta chain, C4BPB, C4BP.

    • 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 MGSHMSDAEH CPELPPVDNS IFVAKEVEGQ ILGTYVCIKG YHLVGKKTLF CNASKEWDNT TTECRLGHCP DPVLVNGEFS SSGPVNVSDK ITFMCNDHYI LKGSNRSQCL EDHTWAPPFP ICKSRDCDPP GNPVHGYFEG NNFTLGSTIS YYCEDRYYLV GVQEQQCVDG EWSSALPVCK LIQEAPKPEC EKALLAFQES KNLCEAMENF MQQLKESGMT MEELKYSLEL KKAELKAKLL.

    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.

    C4Bpb Human
  • View Data Sheet

    Name :

    LCN2 Human

    Description:

    Neutrophil Gelatinase Associated Lipocalin/Lipocalin-2 Human Recombinant

    Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    Product # :

    ENZ-783

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    Description

    LCN2 Human Recombinant produced in E.Coli is a homodimeric non-glycosylated polypeptide chains consisting of two 178 amino acids and having a molecular mass of 41.0kDa.

    Source

    Escherichia Coli.

    Formulation

    LCN2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4, with 0.05 % Tween-20.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human TF-1 cells is less than 0.5ng/ml, corresponding to a specific activity of > 2.0 × 1,000,000 IU/mg.

    Citations

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    • Introduction

      Recombinant Human Lipocalin-2 also called Neutrophil Gelatinase Associated Lipocalin (NGAL) belongs to a family of lipocans which include 25 proteins (including a1-microglobulin and b-lactoglobulin), which are characterized by their ability to bind small lipophilic substances in their hydrophobic core.
      They thereby serve as transporters of substances like retinal, biliverdins & prostaglandins. There are indications that NGAL is involved in modulation of the inflammatory response and is found in the plasma of patients after stroke.

    • Synonyms

      Neutrophil gelatinase-associated lipocalin, NGAL, p25, 25 kDa alpha-2-microglobulin-related subunit of MMP-9, Lipocalin-2, Oncogene 24p3, LCN2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LCN2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCN2 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.

    • Amino Acid Sequence

      QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG LPENHIVFPV PIDQCIDG

    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.

    Human Lcn2
  • View Data Sheet

    Name :

    TIMP2 Human, Sf9

    Description:

    Tissue Inhibitor of Metalloprotease 2 Human Recombinant, Sf9

    TIMP Metallopeptidase Inhibitor 2, Tissue Inhibitor Of Metalloproteinases 2, CSC-21K, Tissue Inhibitor Of Metalloproteinase 2, TIMP-2, DDC8, Metalloproteinase inhibitor 2.

    Product # :

    ENZ-936

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    Description

    TIMP2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (27-220a.a.) and having a molecular mass of 22.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TIMP2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIMP2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

    • Synonyms

      TIMP Metallopeptidase Inhibitor 2, Tissue Inhibitor Of Metalloproteinases 2, CSC-21K, Tissue Inhibitor Of Metalloproteinase 2, TIMP-2, DDC8, Metalloproteinase inhibitor 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

      CSCSPVHPQQ AFCNADVVIR AKAVSEKEVD SGNDIYGNPI KRIQYEIKQI KMFKGPEKDI EFIYTAPSSA VCGVSLDVGG KKEYLIAGKA EGDGKMHITL CDFIVPWDTL STTQKKSLNH RYQMGCECKI TRCPMIPCYI SSPDECLWMD WVTEKNINGH QAKFFACIKR SDGSCAWYRG AAPPKQEFLD IEDPHHHHHH.

    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.

    Timp2 Human Sf9
  • View Data Sheet

    Name :

    ARL4A Human

    Description:

    ADP-Ribosylation Factor-Like 4A Human Recombinant

    ADP-ribosylation factor-like protein 4A, ARL4A.

    Product # :

    PRO-895

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    Description

    ARL4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.7 kDa.The ARL4A is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARL4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARL4A is related Specifically to ARL6 and ARL7 and belongs to the ARF-like protein (ARL) subfamily of small GTPases. However, unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4A takes part in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.

    • Synonyms

      ADP-ribosylation factor-like protein 4A, ARL4A.

    • 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 MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE KLHDMIIKRR KMLRQQKKKR

    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.

    Arl4A Human
  • View Data Sheet

    Name :

    GPI Human, Active

    Description:

    Glucose-6-Phosphate Isomerase Human Recombinant, BioActive

    Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.

    Product # :

    ENZ-1148

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    Description

    GPIHuman Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 578 amino acids (1-558) and having a molecular mass of 65.3 kDa.GPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPI solution (1 mg/ml) contains 10% Glycerol, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 400unit/mg.It is defined by the increase of NADPH in absorbance at 340 nm, resulting from the reduction of NADP. 1 unit will convert 1.0 umole of D-Fructose 6-phosphate to D-glucose 6- phosphate per minute at pH 7.4 at 37˚C.

    Citations

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    • Introduction

      GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.

    • Synonyms

      Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.

    • 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 MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ

    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.

    Gpi Enzyme
  • View Data Sheet

    Name :

    CDK-4 Human

    Description:

    Cyclin-Dependent Kinase 4 Human Recombinant

    Cell division protein kinase 4, CDK4, EC 2.7.11.22, Cyclin-dependent kinase 4, PSK-J3, CMM3,CDK-4, MGC14458.

    Product # :

    PKA-325

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    Description

    Cyclin-Dependent Kinase 4 Human Recombinant is expressed in E. coli as a full-length protein having a molecular weight of 38 kDa fused to an amino terminal hexahistidine tag. The CDK4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CDK4 is supplied in 10mM Bis-Tris Propane pH9.0 and 50% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    Single band on Western Blot.

    Citations

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    • Introduction

      Cyclin-dependent kinase 4 combines with the protein cyclin D to form a protein complex that promotes the passage of cells through the G1 checkpoint in the cell growth cycle. This cellular activity is regulated by the protein p16 produced by p16INK4a. Normally, p16 controls cell growth by inhibiting the activity of the CDK4–cyclin D complex and stopping cells at the G1 checkpoint.

    • Synonyms

      Cell division protein kinase 4, CDK4, EC 2.7.11.22, Cyclin-dependent kinase 4, PSK-J3, CMM3,CDK-4, MGC14458.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

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

    Cdk4 Human
  • View Data Sheet

    Name :

    EXOSC3 Human

    Description:

    Exosome Component 3 Human Recombinant

    bA3J10.7, CGI-102, hRrp-40, p10, PCH1B, RP11-3J10.8, RRP40, Rrp40p, Exosome complex component RRP40, Exosome component 3, Ribosomal RNA-processing protein 40, EXOSC3.

    Product # :

    PRO-1981

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    Description

    EXOSC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275 a.a) and having a molecular mass of 32.0kDa. EXOSC3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EXOSC3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Exosome Component 3 (EXOSC3) is a non-catalytic component of the human exosome, a complex with 3'-5' exoribonuclease activity. EXOSC3 takes part in various RNA processing and degradation activities including degradation of histone mRNA. Linked pseudogenes of EXOSC3 are located on chromosome 19 and 21.

    • Synonyms

      bA3J10.7, CGI-102, hRrp-40, p10, PCH1B, RP11-3J10.8, RRP40, Rrp40p, Exosome complex component RRP40, Exosome component 3, Ribosomal RNA-processing protein 40, EXOSC3.

    • 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 MGSMAEPASV AAESLAGSRA RAARTVLGQV VLPGEELLLP EQEDAEGPGG AVERPLSLNA RACSRVRVVC GPGLRRCGDR LLVTKCGRLR HKEPGSGSGG GVYWVDSQQK RYVPVKGDHV IGIVTAKSGD IFKVDVGGSE PASLSYLSFE GATKRNRPNV QVGDLIYGQF VVANKDMEPE MVCIDSCGRA NGMGVIGQDG LLFKVTLGLI RKLLAPDCEI IQEVGKLYPL EIVFGMNGRI WVKAKTIQQT LILANILEAC EHMTSDQRKQ IFSRLAES.

    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.

    Exosc3 Human
  • View Data Sheet

    Name :

    IL9 Human, Sf9 Active

    Description:

    Interleukin 9 Human Recombinant, Sf9, Active

    Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

    Product # :

    CYT-1143

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    Description

    IL-9 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 132 amino acids (19-144 aa) and having a molecular mass of 14.9kDa.IL-9 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL-9 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

    SDS-PAGE

    IL9 Human, Sf9 Active - Product image 1

    Citations

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    • Introduction

      Interleukin-9 is a protein that acts as one of the regulators of hematopoiesis. IL-9 is an enhancer of cells and megakaryoblastic leukemic cells’ growth. Among this protein’s producers we can find cells like mast cells, Treg, NKT cells, Th17, Th2, ILC2, and Th9 cells in various amounts. Th9 are the primary CD4 cells (T cells) that IL-9 is produced in.

    • Synonyms

      Interleukin 9, Protein Il9, Il9, HP40, Cytokine P40, T-cell growth factor P40

    • 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

      QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
      TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH

    • Background

      What is the molecular weight/Mw of IL9 HUMAN, SF9 ACTIVE Protein?
      IL9 HUMAN, SF9 ACTIVE Protein has a total Mw of 14.9kDa.

      What is the source or expression system of IL9 HUMAN, SF9 ACTIVE Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL9 HUMAN, SF9 ACTIVE Protein?
      IL9 HUMAN, SF9 ACTIVE Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL9 HUMAN, SF9 ACTIVE Protein?
      Determined by cell proliferation assay using MO7e human megakaryocytic leukemic cells. ED50 range for this effect is ≤ 0.3 ng/ml.

      What is the amino acid sequence of IL9 HUMAN, SF9 ACTIVE Protein?
      QGCPTLAGIL DINFLINKMQ EDPASKCHCS ANVTSCLCLG IPSDNCTRPC FSERLSQMTN
      TTMQTRYPLI FSRVKKSVEV LKNNKCPYFS CEQPCNQTTA GNALTFLKSL LEIFQKEKMR GMRGKIHHHH HH.

      What applications can IL9 HUMAN, SF9 ACTIVE Protein be used in?
      IL9 HUMAN, SF9 ACTIVE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL9 HUMAN, SF9 ACTIVE Protein?
      The endotoxin level is minimal, IL9 HUMAN, SF9 ACTIVE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL9 HUMAN, SF9 ACTIVE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL9 HUMAN, SF9 ACTIVE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Interleukin 9 Human
  • View Data Sheet

    Name :

    ALCAM (CD166) Mouse

    Description:

    Activated Leukocyte Cell Adhesion Molecule (CD166) Mouse Recombinant

    Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    Product # :

    PRO-2749

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    Description

    ALCAM mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 739 amino acids (28-527a.a.) and having a molecular mass of 83.1kDa. ALCAM is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ALCAM protein solution (0.25mg/ml) contains 50% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to block the adhesion of Jurkat human acute T cell leukemia cells to immobilized Recombinant Human CD6. When cells are added to 1 ug/ml of mouse ALCAM binded to CD6, this effect is more to 50%.

    Citations

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    • Introduction

      CD166 antigen isoform 2 (ALCAM) is a type 1 membrane glycoprotein and belongs to the immunoglobulin superfamily. ALCAM is expressed on thymic epithelium, microvascular endothelium, activated lymphocytes and monocytes, and monocyte-derived dendritic cells. CD166 and CD6 interaction plays a role in T cell development and T cell regulation, as well as in the binding of T cells and B cells to activated leukocytes.

    • Synonyms

      Activated leukocyte cell adhesion molecule, ALCAM, Alcam, CD166 antigen, CD166 antigen isoform1, CD166, Protein DM-GRASP, AI853494 Protein, MuSC, SC1, BEN.

    • 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

      WYTVNSAYGD TIVMPCRLDV PQNLMFGKWK YEKPDGSPVF IAFRSSTKKS VQYDDVPEYK DRLSLSENYT LSIANAKISD EKRFVCMLVT EDNVFEAPTL VKVFKQPSKP EIVNKAPFLE TDQLKKLGDC ISRDSYPDGN ITWYRNGKVL QPVEGEVAIL FKKEIDPGTQ LYTVTSSLEY KTTRSDIQMP FTCSVTYYGP SGQKTIYSEQ EIFDIYYPTE QVTIQVLPPK NAIKEGDNIT
      LQCLGNGNPP PEEFMFYLPG QPEGIRSSNT YTLTDVRRNA TGDYKCSLID KRNMAASTTI TVHYLDLSLN PSGEVTKQIG DTLPVSCTIS ASRNATVVWM KDNIRLRSSP SFSSLHYQDA GNYVCETALQ EVEGLKKRES LTLIVEGKPQ IKMTKKTDPS GLSKTIICHV EGFPKPAIHW TITGSGSVIN QTEESPYING RYYSKIIISP EENVTLTCTA ENQLERTVNS LNVSAISIPE
      HDEADDISDE NREKVNDQAK LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK 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.

    Cd166 Mouse
  • View Data Sheet

    Name :

    LIF Rat

    Description:

    Leukemia Inhibitory Factor Rat Recombinant

    Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    Product # :

    CYT-731

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    Description

    Leukemia Inhibitory Factor (LIF) Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.8 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LIF Rat was lyophilized from 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    Purity

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

    Biological Activity

    The activity of rat LIF is determined by the ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of rat LIF in this assay is 0.5ng/mL.

    Citations

    More Info

    • Introduction

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

    • Synonyms

      Leukemia inhibitory factor, Cholinergic neuronal differentiation factor, Lif.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      SPLPITPVNA TCAIRHPCHG NLMNQIKSQL AQLNGSANAL FISYYTAQGE PFPNNVDKLC APNMTDFPPF HANGTEKTKL VELYRMVTYL GASLTNITWD QKNLNPTAVS LQIKLNATTD VMRGLLSSVL CRLCNKYHVG HVDVPCVPDN SSKEAFQRKK LGCQLLGTYK QVISVLAQAF .

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

    Lif Rat
  • View Data Sheet

    Name :

    PSMD9 Human

    Description:

    Proteasome 26S Subunit, Non-ATPase 9 Human Recombinant

    p27, Rpn4, 26S proteasome non-ATPase regulatory subunit 9, 26S proteasome regulatory subunit p27, PSMD9.

    Product # :

    ENZ-666

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    Description

    PSMD9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-223) and having a molecular mass of 27.1kDa. PSMD9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSMD9 solution (1mg/ml) contains 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.

    Citations

    More Info

    • Introduction

      PSMD9 is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. PSMD9 acts as a chaperone through the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex compilation, PSMD9 is part of an intermediate PSMD9:PSMC6:PSMC3 module, also called modulator trimer complex. PSMD9 is released during the further base assembly process.

    • Synonyms

      p27, Rpn4, 26S proteasome non-ATPase regulatory subunit 9, 26S proteasome regulatory subunit p27, PSMD9.

    • 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 MGSMSDEEAR QSGGSSQAGV VTVSDVQELM RRKEEIEAQI KANYDVLESQ KGIGMNEPLV DCEGYPRSDV DLYQVRTARH NIICLQNDHK AVMKQVEEAL HQLHARDKEK QARDMAEAHK EAMSRKLGQS ESQGPPRAFA KVNSISPGSP ASIAGLQVDD EIVEFGSVNT QNFQSLHNIG SVVQHSEGKP LNVTVIRRGE KHQLRLVPTR WAGKGLLGCN IIPLQR.

    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.

    Psmd9 Human
  • View Data Sheet

    Name :

    IL35 Human

    Description:

    Interleukin-35 Human Recombinant

    Product # :

    CYT-842

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    Description

    IL35 Human Recombinant produced in HEK 293 cells is comprised of a p35 subunit from IL-12 (Accession # p29459) and a EBI3 (Accession # q14213) subunit from IL-27. IL35 is a heterodimeric polypeptide chain containing 406 amino acids, with a predicted molecular weight of 45.8 kDa.

    Source

    HEK 293 cells.

    Formulation

    Lyophilized from a concentrated solution containing 10mM Na2PO4 pH 7.5 and 30mM NaCl.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Interleukin-35 is a glycosylated, disulfide-linked, heterodimeric protein comprised of the p35 subunit of IL-12 (IL-12 alpha) and the beta subunit of IL-27 (EBI3). IL35 is expressed by regulatory T-cells (Tregs), macrophages and some trophoblast and dendritic cells. IL-35 is produced in response to inflammation and generally serves as an inflammation suppressor. Interleukin-35 curbs inflammation by applying multiple activities, including the stimulation of regulatory T-cells and the inhibition of Th17 cells.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL35 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL35 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 IL35 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EBI3 subunit:RKGPPAALTL PRVQCRASRY PIAVDCSWTL PPAPNSTSPV SFIATYRLGM AARGHSWPCL QQTPTSTSCT ITDVQLFSMA PYVLNVTAVH PWGSSSSFVP FITEHIIKPD PPEGVRLSPL AERQLQVQWE PPGSWPFPEI FSLKYWIRYK RQGAARFHRV GPIEATSFIL RAVRPRARYY VQVAAQDLTD YGELSDWSLP ATATMSLGKp35 subunit:RNLPVATPDP GMFPCLHHSQ NLLRAVSNML QKARQTLEFY PCTSEEIDHE DITKDKTSTV EACLPLELTK NESCLNSRET SFITNGSCLA SRKTSFMMAL CLSSIYEDLK MYQVEFKTMN AKLLMDPKRQ IFLDQNMLAV IDELMQALNF NSETVPQKSS LEEPDFYKTK IKLCILLHAF RIRAVTIDRV MSYLNAS

    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.

    Il35 Human
  • View Data Sheet

    Name :

    PCBD1 Human

    Description:

    Pterin-4-Alpha-Carbinolamine Dehydratase Human Recombinant

    DCOH, PCBD, PCD, PHS.

    Product # :

    ENZ-552

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    Description

    PCBD1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 124 amino acids (1-104 a.a.) and having a molecular mass of 14.1kDa.PCBD1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCBD1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PCBD1 enzyme takes part in phenylalanine hydroxylation. PCBD1 deficiency results in hyperphenylalaninemia. PCBD1 enzyme controls the homodimerization of HNF1. PCBD1 takes part in tetrahydrobiopterin biosynthesis. PCBD1 prevents the formation of 7-pterins and accelerate the formation of quinonoid-BH2. PCBD1 is a coactivator for HNF1A-dependent transcription.

    • Synonyms

      DCOH, PCBD, PCD, PHS.

    • 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 MAGKAHRLSA EERDQLLPNL RAVGWNELEG RDAIFKQFHF KDFNRAFGFM TRVALQAEKL DHHPEWFNVY
      NKVHITLSTH ECAGLSERDI NLASFIEQVA VSMT.

    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.

    Pcbd1 Human
  • View Data Sheet

    Name :

    AICDA Antibody

    Description:

    Activation-induced cytidine deaminase, Mouse Anti Human

    Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    Product # :

    ANT-411

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      AICDA is an RNA-editing deaminase which belongs to the cytidine deaminase family. AICDA is involved in somatic hypermutation, gene conversion, and class-switch recombination of immunoglobulin genes. Defects in the AICDA gene are the cause of autosomal recessive hyper-IgM immunodeficiency syndrome type 2 (HIGM2).

    • Synonyms

      Activation-induced cytidine deaminase, Cytidine aminohydrolase, AICDA, AID, ARP2, CDA2, HIGM2.

    • Immunogen

      Anti-human AICDA mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human AICDA amino acids 1-54 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P2D3AT.

    • Applications

      AICDA antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.

    • 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

      AICDA antibody was purified from mouse ascitic fluids by protein-G 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.

    Aicda Antibody
  • View Data Sheet

    Name :

    MYD88 Antibody

    Description:

    Myeloid Differentiation Primary Response 88, Mouse Anti Human

    Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.

    Product # :

    ANT-464

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.01% Sodium Azide.

    Citations

    More Info

    • Introduction

      Myeloid differentiation primary response gene 88 (MYD88) is a cytosolic adapter protein, which has a central role in the innate and adaptive immune response. MYD88 functions as a vital signal transducer in the interleukin-1 and Toll-like receptor signaling pathways. MYD88 acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. The MYD88 protein increases IL-8 transcription. MYD88 is involved in IL-18-mediated signaling pathway. MYD88 activates IRF1, resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. MYD88 is comprised of an N-terminal death domain and a C-terminal Toll-interleukin1 receptor domain. Patients with defects in the MYD88 gene have an increased susceptibility to pyogenic bacterial infections.

    • Synonyms

      Myeloid differentiation primary response protein MyD88, MYD88, MYD88D.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human MYD88 mAb, clone PAT22F11A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human MYD88 protein 1-309 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and Kappa light chain.

    • Clone

      PAT22F11A.

    • Applications

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

    • 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

      MYD88 antibody was purified from mouse ascitic fluids by protein-G 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.

    Myd88 Antibody
  • View Data Sheet

    Name :

    IL9 Rat

    Description:

    Interleukin-9 Rat Recombinant

    Interleukin 9, Protein Il9, Il9.

    Product # :

    CYT-748

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    Description

    Interleukin-9 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 14.3kDa.The IL-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL9 protein was 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

    The ED50 as determined by a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

    Citations

    More Info

    • Introduction

      Factor that is thought to be a regulator of hematopoiesis. It has been shown to enhance the growth of human mast cells and megakaryoblastic leukemic cells as well as murine helper t-cell clones. IL-9 is a glycoprotein with a molecular weight of 32-39 that is derived from T-cells, and maps to human chromosome 5.

    • Synonyms

      Interleukin 9, Protein Il9, Il9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL9 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 9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.

    • Background

      What is the molecular weight/Mw of IL9 RAT Protein?
      IL9 RAT Protein has a total Mw of 14.3kDa.

      What is the source or expression system of IL9 RAT Protein?
      Escherichia Coli.

      What is the Purity of IL9 RAT Protein?
      IL9 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL9 RAT Protein?
      The ED50 as determined by a cell proliferation assay using murine TS1 cells is less than 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg.

      What is the amino acid sequence of IL9 RAT Protein?
      MQRCSTSWGI QHTSYLIENL KDDPSSKCSC SANVTSCLCL PIPSDDCTTP CFQEGMSQVT NATQQSKFSP FFFRVKRIVE TLKSNKCQFF SCEKPCNQTT AGNTVSFLKS LLKTFQKTEV QVQRSRA.

      What applications can IL9 RAT Protein be used in?
      IL9 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL9 RAT Protein?
      The endotoxin level is minimal, IL9 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL9 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL9 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 9 Rat
  • View Data Sheet

    Name :

    GCLM Antibody

    Description:

    Glutamate-Cysteine Ligase, Modifier Subunit, Mouse Anti Human

    Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    Product # :

    ANT-089

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      Glutamate-cysteine ligase (GCLM) is the first rate limiting enzyme of glutathione synthesis. The GCLM enzyme is comprised of 2 subunits, a heavy catalytic subunit and a light regulatory subunit. GCLM deficiency is associated with some forms of hemolytic anemia.

    • Synonyms

      Glutamate--cysteine ligase regulatory subunit, GCS light chain, Gamma-ECS regulatory subunit, Gamma-glutamylcysteine synthetase regulatory subunit, Glutamate--cysteine ligase modifier subunit, GCLM, GLCLR.

    • Immunogen

      Anti-human GCLM mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human GCLM amino acids 1-274 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and kappa light chain.

    • Clone

      P2D12AT.

    • 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

      GCLM antibody was purified from mouse ascitic fluids by protein-G 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.

    Gclm Antibody
  • View Data Sheet

    Name :

    PPIH Human

    Description:

    Cyclophilin-H Human Recombinant

    Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    Product # :

    ENZ-379

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.

    Purity

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

    Biological Activity

    Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    Citations

    More Info

    • Introduction

      PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.

    • Synonyms

      Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    • 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).Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.

    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.

    Ppih Human
  • View Data Sheet

    Name :

    IL15 Rat

    Description:

    Interleukin-15 Rat Recombinant

    IL-15, MGC9721.

    Product # :

    CYT-345

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    Description

    Interleukin-15 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 13533 Dalton. The IL-15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM Tris, pH-8.5.

    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 stimulation of the proliferation of CTLL-2 was found to be < 10 ng/ml, corresponding to a Specific Activity of 100,000IU/mg.

    Citations

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and interleukine 2 share many biological activities. They are found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between this cytokine and IL2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. Studies of the mouse counterpart suggested that this cytokine may increase the expression of apoptosis inhibitor BCL2L1/BCL-x(L), possibly through the transcription activation activity of STAT6, and thus prevent apoptosis. Two alternatively spliced transcript variants of this gene encoding the same protein have been reported.

    • Synonyms

      IL-15, MGC9721.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-15 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL15 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-15 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-Asn-Trp-Ile-Asp.

    • Background

      What is the molecular weight/Mw of IL15 RAT Protein?
      IL15 RAT Protein has a total Mw of 13.5kDa.

      What is the source or expression system of IL15 RAT Protein?
      Escherichia Coli.

      What is the Purity of IL15 RAT Protein?
      IL15 RAT Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL15 RAT Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of CTLL-2 was found to be < 10 ng/ml, corresponding to a Specific Activity of 100,000IU/mg.

      What is the amino acid sequence of IL15 RAT Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Asn-Trp-Ile-Asp.

      What applications can IL15 RAT Protein be used in?
      IL15 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL15 RAT Protein?
      The endotoxin level is minimal, IL15 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL15 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL15 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 15 Rat
  • View Data Sheet

    Name :

    TADA3 Human

    Description:

    Transcriptional Adaptor 3 Human Recombinant

    Transcriptional adapter 3, ADA3 homolog, hADA3, STAF54, Transcriptional adapter 3-like, ADA3-like protein, TADA3, ADA3, TADA3L, Transcriptional adapter 3 isoform a, NGG1.

    Product # :

    PRO-1689

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    TADA3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (1-432) and having a molecular mass of 51.3 kDa.TADA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TADA3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 2mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Transcriptional adapter 3 (TATD3) is a subunit of 2 histone acetyltransferase complexes, which functions as a component of the PCAF complex. TATD3 is a transcriptional activator adaptor that is also associates with the tumor suppressor protein p53 and is essential for full activity of p53 and p53-mediated apoptosis.

    • Synonyms

      Transcriptional adapter 3, ADA3 homolog, hADA3, STAF54, Transcriptional adapter 3-like, ADA3-like protein, TADA3, ADA3, TADA3L, Transcriptional adapter 3 isoform a, NGG1.

    • 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 MGSMSELKDC PLQFHDFKSV DHLKVCPRYT AVLARSEDDG IGIEELDTLQ LELETLLSSA SRRLRVLEAE TQILTDWQDK KGDRRFLKLG RDHELGAPPK HGKPKKQKLE GKAGHGPGPG PGRPKSKNLQ PKIQEYEFTD DPIDVPRIPK NDAPNRFWAS VEPYCADITS EEVRTLEELL KPPEDEAEHY KIPPLGKHYS QRWAQEDLLE EQKDGARAAA VADKKKGLMG PLTELDTKDV DALLKKSEAQ HEQPEDGCPF GALTQRLLQA LVEENIISPM EDSPIPDMSG KESGADGAST SPRNQNKPFS VPHTKSLESR IKEELIAQGL LESEDRPAED SEDEVLAELR KRQAELKALS AHNRTKKHDL LRLAKEEVSR QELRQRVRMA DNEVMDAFRK IMAARQKKRT PTKKEKDQAW KTLKERESIL KLLDG.

    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.

    Tada3 Human
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