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Search results

1000 results found for “Neuroglobin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    CNN1 Human

    Description:

    Calponin 1, Basic, Smooth Muscle Human Recombinant

    Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-1.

    Product # :

    PRO-1129

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    • description
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    • More Info

    Description

    CNN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 305 amino acids (1-297) and having a molecular mass of 34.2 kDa.CNN1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CNN1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin.

    • Synonyms

      Calponin 1 basic smooth muscle, Calponin H1 smooth muscle, SMCC, Basic calponin, Sm-Calp, calponin-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGNNF MDGLKDGIIL CEFINKLQPG SVKKINESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPGKLREG RNIIGLQMGT NKFASQQGMT AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHA HNYYNSALEH HHHHH

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

    Cnn1 Human
  • View Data Sheet

    Name :

    NKp46 Antibody

    Description:

    Natural Cytotoxicity Receptor NKp46, Mouse Anti Human

    Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.

    Product # :

    ANT-303

    Price :

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    • formulation
    • More Info

    Formulation

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

    More Info

    • Introduction

      A natural cytotoxicity receptor (NCR) NKp46 has been shown to represent a novel NK cell-specific molecule involved in human NK cell activation. The natural cytotoxicity receptors (NCRs) are a recently characterized family of Ig-like activation receptors that appear to be major triggering receptors in tumor cell recognition. The three known NCRs include NKp46 and NKp30, which are expressed on circulating NKcells, and NKp44, which is expressed only on activating NK cells. NKp46 has been implicated in NK cell-mediated lysis of several autologous tumor cells, pathogen-infected cell lines and mononuclear phagocytes infected with an intracellular bacterium. The Lysis of tumor cells by NK-cells involves recognition by NKp46 of heparan sulfate moieties of membrane heparan sulfate proteoglycans. Furthermore, NKp46 is a surface receptor involved in NK-cell cell death by apoptosis. NKp46 has two extracellular Ig-like domains followed by a ~40 residue stalk region, a type I transmembrane domain, and a short cytoplasmic tail. The extracellular Ig-like domain of NKp46 (22-255aa) is purified by FPLC gel-filtration chromatography, after refolding of the isolated inclusion bodies in a redox buffer. In addition, engagement of the antigen with the monoclonal antibody stimulates intracellular calcium levels and the synthesis of cytokines. CD59 is an NKp46 coreceptor (by physical association) together they activate cytotoxicity of human NK-cells, their engagement results in tyrosine phosphorylation of CD3-zeta chains associated with NKp46. Reduced cell surface expression of NKp46 and other NK-cell receptors is linked to the impaired NK-cell cytolytic function in viremic HIV-1 infection.

    • Synonyms

      Natural cytotoxicity triggering receptor 1, Natural killer cell p46-related protein, hNKp46, NK-p46, NKp46, NK cell-activating receptor, Lymphocyte antigen 94 homolog, CD335 antigen, NCR1, LY94, NCRNKp46, CD335.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human NKp46 mAb, is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human NKp46 amino acids 22-255 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      Pn1D9AT.

    • Applications

      NKp46 antibody has been tested by immunofluorescent staining with flow cytometric analysis and by Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      NKp46 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.

    Nkp46 Antibody
  • View Data Sheet

    Name :

    HN1 Human

    Description:

    Hematological And Neurological Expressed 1 Human Recombinant

    ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.

    Product # :

    PRO-1434

    Price :

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    • More Info

    Description

    HN1 Human Recombinant produced in E. coli is a single polypeptide chain containing 174 amino acids (1-154) and having a molecular mass of 18.1kDa. HN1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HN1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hematological and neurological expressed 1 protein (HN1) is a small protein which is extremely preserved among species. HN1 expression is upregulated in regenerating neural tissues, including the axotomized adult rodent facial motor nerve and dedifferentiating retinal pigment epithelial cells of the Japanese newt. HN1 is also expressed in several tissues during embryonic development as well as in regions of the adult brain which display high plasticity.

    • Synonyms

      ARM2, HN1A, Hematological and neurological expressed 1 protein, Androgen-regulated protein 2, HN1.

    • 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 MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPTEQ PVRKNKMASN IFGTPEENQA SWAKSAGAKS SGGREDLESS GLQRRNSSEA SSGDFLDLKG EGDIHENVDT DLPGSLGQSE EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG.

    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.

    Hn1 Human
  • View Data Sheet

    Name :

    CRYGC Human

    Description:

    Crystallin, Gamma C Human Recombinant

    Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    Product # :

    PRO-1095

    Price :

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    • description
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    • More Info

    Description

    CRYGC Human Recombinant produced in E. coli is a single polypeptide chain containing 198 amino acids (1-174) and having a molecular mass of 23.5kDa.CRYGC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CRYGC solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CRYGC is a member of the beta/gamma-crystallin family. Mammalian lens crystallins are distributed into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Gamma-crystallins are a homogeneous group of extremely symmetrical, monomeric proteins usually missing connecting peptides and terminal extensions and are differentially regulated after early development. Three pseudogenes (gamma-E,F,G) and four gamma-crystallin genes (gamma-A,B,C,D) are structured in a genomic sector as a gene cluster. Gamma-crystallins are involved in cataract formation as a result of aging or mutations in specific genes. Mutations in CRYGC result in cataract Coppock-like (CCL) and cataract autosomal dominant (ADC).

    • Synonyms

      Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.

    • 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 MGSHMGKITF YEDRAFQGRS YETTTDCPNL QPYFSRCNSI RVESGCWMLY ERPNYQGQQY LLRRGEYPDY QQWMGLSDSI RSCCLIPQTV SHRLRLYERE DHKGLMMELS EDCPSIQDRF HLSEIRSLHV LEGCWVLYEL PNYRGRQYLL RPQEYRRCQD WGAMDAKAGS LRRVVDLY

    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.

    Crygc Human
  • View Data Sheet

    Name :

    HMGB3 Human

    Description:

    High-Mobility Group Box 3 Human Recombinant

    High Mobility Group Box 3, High-Mobility Group (Nonhistone Chromosomal) Protein 4, Non-Histone Chromosomal Protein, High Mobility Group Protein B3, High Mobility Group Protein 4, HMG-2a, HMG-4.

    Product # :

    PRO-1623

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    Description

    HMGB3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-180) and having a molecular mass of 22.8kDa.HMGB3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HMGB3 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      HMGB3 is a member of the high mobility group (HMG) protein superfamily. HMGB3 holds DNA-binding HMG box domains, as do HMG1 and HMG2, and like the rest of the HMG protein superfamily members has a vital part in DNA replication, transcription and nucleosome assembly.

    • Synonyms

      High Mobility Group Box 3, High-Mobility Group (Nonhistone Chromosomal) Protein 4, Non-Histone Chromosomal Protein, High Mobility Group Protein B3, High Mobility Group Protein 4, HMG-2a, HMG-4.

    • 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 MGSMAKGDPK KPKGKMSAYA FFVQTCREEH KKKNPEVPVN FAEFSKKCSE RWKTMSGKEK SKFDEMAKAD KVRYDREMKD YGPAKGGKKK KDPNAPKRPP SGFFLFCSEF RPKIKSTNPG ISIGDVAKKL GEMWNNLNDS EKQPYITKAA KLKEKYEKDV ADYKSKGKFD GAKGPAKVAR KKV.

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    Hmgb3 Human
  • View Data Sheet

    Name :

    ProNGF Human

    Description:

    Pro-Nerve Growth Factor Human Recombinant

    Human Pro-NGF, ProNGF, NGFB.

    Product # :

    CYT-426

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    Description

    Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Human Pro-NGF, ProNGF, NGFB.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF 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 ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA.

    • Background

      Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis

      Abstract:

      Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.

      Introduction:

      Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.

      Characteristics and Processing Mechanisms:

      Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.

      Production and Manipulation of Pro-NGF Human Recombinant:

      Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.

      Implications in Neuroregulation and Disease Pathogenesis:

      Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.

      Conclusion:

      Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.

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

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

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


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

      What is the amino acid sequence of ProNGF Protein?
      MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
      TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
      SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
      KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
      VCVLSRKAVRRA

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

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

    Pro Ngf Human
  • View Data Sheet

    Name :

    SEMG1 Human

    Description:

    Semenogelin I Human Recombinant

    CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

    Product # :

    PRO-1732

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    Description

    SEMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 462 amino acids (24-462) and having a molecular mass of 52kDa. SEMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SEMG1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 0.5M NaCl, 10% glycerol, 250mM Imidazole, 0.1mM PMSF and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      SEMG1 is the predominant protein in semen. The secreted protein takes part in the formation of a gel matrix which encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes SEMG1 into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to shift more freely. 2 transcript variants encoding different isoforms have been found for SEMG1.

    • Synonyms

      CT103, dJ172H20.2, SEMG, SGI, Semenogelin-1, Semenogelin I, SEMG1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT.

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    Semg1 Human
  • View Data Sheet

    Name :

    MYOZ1 Human

    Description:

    Myozenin 1 Human Recombinant

    CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.

    Product # :

    PRO-1652

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    Description

    MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.

    • Synonyms

      CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE EL.

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    Myoz1 Human
  • View Data Sheet

    Name :

    NPL Human

    Description:

    N-acetylneuraminate Pyruvate Lyase Human Recombinant

    N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    Product # :

    ENZ-125

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    Description

    NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NPL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.

    • Synonyms

      N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    • 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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.

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    Npl Human
  • View Data Sheet

    Name :

    NUBP1 Human

    Description:

    Nucleotide Binding Protein 1 Human Recombinant

    Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.

    Product # :

    PRO-2203

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    Description

    NUBP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-320 a.a) and having a molecular mass of 36.9kDa.NUBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques

    Source

    Escherichia Coli.

    Formulation

    NUBP1protein solution (1mg/ml) in Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 (NUBP1) is Involved in the regulation of centrosome duplication similarity. NUBP1 is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. NUBP1 is necessary for maturation of extra mitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer constructs a Fe-S scaffold complex, mediating the de novo compilation of a Fe-S cluster and its transfer to target apoproteins.

    • Synonyms

      Cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 , NBP, NBP1, NBP35, Nucleotide-binding protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEEVPHD CPGADSAQAG RGASCQGCPN QRLCASGAGA TPDTAIEEIK EKMKTVKHKI LVLSGKGGVG KSTFSAHLAH GLAEDENTQI ALLDIDICGP SIPKIMGLEG EQVHQSGSGW SPVYVEDNLG VMSVGFLLSS PDDAVIWRGP KKNGMIKQFL RDVDWGEVDY LIVDTPPGTS DEHLSVVRYL ATAHIDGAVI ITTPQEVSLQ DVRKEINFCR KVKLPIIGVV ENMSGFICPK CKKESQIFPP TTGGAELMCQ DLEVPLLGRV PLDPLIGKNC DKGQSFFIDA PDSPATLAYR SIIQRIQEFC NLHQSKEENL ISS.

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    Nubp1 Human
  • View Data Sheet

    Name :

    BNIP1 Human

    Description:

    BCL2/Adenovirus E1B 19kDa Interacting Protein 1 Human Recombinant

    BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.

    Product # :

    PRO-2150

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    Description

    BNIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199 a.a) and having a molecular mass of 25.2kDa. BNIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BNIP1 protein solution (1.0 mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      BNIP1 belongs to the of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. BNIP1 interacts with the E1B 19 kDa protein, which defends cells from virally-induced cell death. In addition, BNIP1 interacts with E1B 19 kDa-like sequences of BCL2 which is an additional apoptotic protector. Adding up, BNIP1 is implicated in vesicle transport into the endoplasmic reticulum. Alternative splicing results of BNIP1 in four protein products with identical N- and C-termini have been found.

    • Synonyms

      BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.

    • 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 MGSMAAPQDV HVRICNQEIV KFDLEVKALI QDIRDCSGPL SALTELNTKV KEKFQQLRHR IQDLEQLAKE QDKESEKQLL LQEVENHKKQ MLSNQASWRK ANLTCKIAID NLEKAELLQG GDLLRQRKTT KESLAQTSST ITESLMGISR MMAQQVQQSE EAMQSLVTSS RTILDANEEF KSMSGTIQLG RKLITKYNRR EL.

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    Bnip1 Human
  • View Data Sheet

    Name :

    STX1A Human

    Description:

    Syntaxin-1A Human Recombinant

    STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    Product # :

    PRO-574

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    Description

    Syntaxin-1A Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 226 amino acids (1-226) and having a molecular mass of 26.1 kDa.Recombinant Human STX1A contains N-terminal domain (Habc) and t_SNARE domain (H3 domain).

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH7.5, 10% glycerol, and 1mM DTT.

    Purity

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

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    • Introduction

      Syntaxin is membrane integrated Q-SNARE protein participating in exocytosis. Syntaxin is composed of an N-terminal regulatory domain (Habc), a SNARE domain (known as H3), and a single C-terminal transmembrane domain. The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex. Synaptic vesicles store neurotransmitters that are released during calcium-regulated exocytosis. The specificity of neurotransmitter release requires the localization of both synaptic vesicles and calcium channels to the presynaptic active zone. Syntaxins function in this vesicle fusion process. Syntaxins also serve as a substrate for botulinum neurotoxin type C, a metalloprotease that blocks exocytosis and has high affinity for a molecular complex that includes the alpha-latrotoxin receptor which produces exocytosis.

    • Synonyms

      STX1, HPC-1, p35-1, Syntaxin-1A, Neuron-specific antigen HPC-1, STX-1A, STX1A.

    • 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

      MKDRTQELRT AKDSDDDDDV AVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQ.

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    Stx1A Human
  • View Data Sheet

    Name :

    Frataxin Human

    Description:

    Frataxin Human Recombinant

    FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.

    Product # :

    PRO-761

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    Description

    Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.

    • Synonyms

      FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.

    • 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 MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.

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    Frataxin Human
  • View Data Sheet

    Name :

    MANF Mouse

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Mouse Recombinant

    Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    Product # :

    CYT-827

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    • More Info

    Description

    MANF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 18.2kDa.

    Source

    Escherichia Coli.

    Formulation

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

    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 a cell proliferation assay using rat C6 cells is less than 10µg/ml, corresponding to a specific activity of >100 IU/mg.

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    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Arginine-rich protein, Protein ARMET, Manf, Armet.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LRPGDCEVCI SYLGRFYQDL KDRDVTFSPA TIEEELIKFC REARGKENRL CYYIGATDDA ATKIINEVSK PLAHHIPVEK ICEKLKKKDS QICELKYDNQ IDLSTVDLKK LRVKELKKIL DDWGEMCKGC AEKSDYIRKI NELMPKYAPK AASARTDL.

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    Manf Mouse
  • View Data Sheet

    Name :

    NTRK2 Human

    Description:

    Neurotrophic Receptor Tyrosine Kinase 2 Human Recombinant

    GP145-TrkB, trk-B, TRKB, NTRK2

    Product # :

    CYT-1159

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    Description

    NTRK2 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 407 amino acids (32-430a.a) and having a molecular mass of 45.2kDa.NTRK2 is fused to an 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NTRK2 solution (0. 5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurotrophic Receptor Tyrosine Kinase 2, also referred to NTRK2, is a tyrosine-protein kinase receptor which takes part in the development & the maturation of the central and the peripheral nervous systems through regulation of neuron survival, migration, proliferation, differentiation and synapse formation & plasticity. NTRK2 acts in learning and memory by regulating both short term synaptic function and long-term potentiation. The substrates that are known for the TRK family receptors are: SHC1, PI-3 kinase and PLC-gamma-1.

    • Synonyms

      GP145-TrkB, trk-B, TRKB, NTRK2

    • 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

      CPTSCKCSAS RIWCSDPSPG IVAFPRLEPN SVDPENITEI FIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAHKAF LKNSNLQHIN FTRNKLTSLS RKHFRHLDLS ELILVGNPFT CSCDIMWIKT LQEAKSSPDT QDLYCLNESS KNIPLANLQI PNCGLPSANL AAPNLTVEEG KSITLSCSVA GDPVPNMYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVKGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL IAKNEYGKDE KQISAHFMGW PGIDDGANPN YPDVIYEDYG TAANDIGDTT NRSNEIPSTD VTDKTGREHL EHHHHHH

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    Ntrk2 Human
  • View Data Sheet

    Name :

    Streptavidin-NC

    Description:

    Streptavidin-NC Recombinant

    Product # :

    PRO-338

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    Description

    Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.

    Source

    Escherichia Coli.

    Formulation

    The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Liquid formulation.

    • Stability

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

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    Streptavidin Nc
  • View Data Sheet

    Name :

    Mouse OX40L

    Description:

    OX40 Ligand Mouse Recombinant

    Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    Product # :

    CYT-1191

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    Description

    OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.OX40L is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its binding ability in a functional ELISA with Human TNFRSF4 (CAT# cyt-1039).

    More Info

    • Introduction

      OX40 Ligandis a part of the tumor necrosis factor (TNF)receptor family. OX40L receptor is OX40 which is expressed predominantly on activated CD4+ T cells.OX40 Ligandis expressed on various antigen-presenting cells such asmacrophages, DC2sand activated Blymphocytes. Expression of OX40 is momentary following engagement of T cell receptors. The ligation of OX40-OX40L stimulates proliferation anddifferentiation of activated B cells,increases immunoglobulin secretion and is also a sourceof survival signal for T cells and enables the development of memory T cells.

    • Synonyms

      Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l

    • 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

      ADPSSSPAKD PPIQRLRGAV TRCEDGQLFI SSYKNEYQTM EVQNNSVVIK CDGLYIIYLK GSFFQEVKID LHFREDHNPI SIPMLNDGRR IVFTVVASLA FKDKVYLTVN APDTLCEHLQ INDGELIVVQ LTPGYCAPEG SYHSTVNQVP LHHHHHH

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    Ox40L Mouse
  • View Data Sheet

    Name :

    OX40L Human

    Description:

    OX40 Ligand Human Recombinant

    Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

    Product # :

    CYT-1226

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    Description

    OX40L Human Recombinant is a single, glycosylated, polypeptide chain (51-183 a.a) containing a total of139 amino acids and having a molecular mass of 16.2 kDa. OX40L is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human OX40/TNFRSF4.

    More Info

    • Synonyms

      Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l.

    • 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

      QVSHRYPRIQ SIKVQFTEYK KEKGFILTSQ KEDEIMKVQN NSVIINCDGF YLISLKGYFS QEVNISLHYQ KDEEPLFQLK KVRSVNSLMV ASLTYKDKVY LNVTTDNTSL DDFHVNGGEL ILIHQNPGEF CVLHHHHHH.

    • Background

      OX40 Ligand (OX40L), a member of the tumor necrosis factor (TNF) superfamily, plays a pivotal role in regulating immune responses and orchestrating the delicate balance between activation and tolerance. The human recombinant form of OX40L has emerged as a potent tool in immunology, offering insights into its molecular intricacies and potential applications in therapeutic interventions. This research embarks on a journey to unravel the multifaceted role of OX40L Human Recombinant, shedding light on its structural attributes, signaling pathways, and its promising avenues in immunotherapy. By delving into the properties of OX40L, scientists aim to expand our understanding of immune modulation and open new frontiers in the treatment of immune-related disorders.

      Structural Insights into OX40L Human Recombinant:

      OX40L, as a trimeric transmembrane protein, exhibits a unique structural configuration that governs its interactions with the OX40 receptor on T cells. The human recombinant form, engineered for controlled study, provides a window into the three-dimensional intricacies of the ligand. Understanding its structure is pivotal for deciphering how OX40L engages with its receptor and modulates immune responses.

      Immunomodulatory Signaling Pathways:

      OX40L binding to its cognate receptor OX40 on T cells triggers intricate signaling cascades that impact immune cell activation, proliferation, and cytokine production. The OX40-OX40L axis is a crucial regulator of T cell function, influencing both effector and regulatory T cell responses. Unraveling the specific pathways activated by OX40L Human Recombinant provides valuable insights into the modulation of immune responses in health and disease.

      Applications in Immunotherapy:

      The immunomodulatory properties of OX40L make it an attractive candidate for therapeutic interventions. OX40L Human Recombinant, in preclinical and clinical studies, is being explored for its potential in enhancing antitumor immune responses. By harnessing the ligand's ability to stimulate effector T cells and memory T cell formation, researchers aim to develop novel immunotherapies for cancer and other immune-related disorders.

      OX40L in Autoimmune Diseases:

      Conversely, OX40L's role in autoimmune diseases has spurred investigations into its inhibition as a therapeutic strategy. Blocking the OX40-OX40L interaction has shown promise in mitigating autoimmune responses, presenting a potential avenue for the development of treatments for conditions such as rheumatoid arthritis and inflammatory bowel disease.

      While the potential of OX40L Human Recombinant in immunotherapy is promising, challenges persist. Fine-tuning its applications, understanding potential side effects, and optimizing dosages are critical considerations for translational success. Additionally, comprehending the context-dependent nature of OX40L signaling is essential for tailoring therapeutic strategies to specific diseases and patient profiles.

      OX40L Human Recombinant stands at the forefront of immunomodulation research, offering a lens through which we can unravel the complexities of immune responses. Its structural insights, signaling pathways, and therapeutic applications position it as a key player in the evolving landscape of immunotherapy. As researchers continue to dissect the molecular nuances of OX40L, they not only expand our understanding of immune regulation but also pave the way for transformative advancements in the treatment of cancer and autoimmune diseases, shaping the future of precision medicine and immunotherapy.

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    Ox40L Human
  • View Data Sheet

    Name :

    GPNMB Human, Sf9

    Description:

    Glycoprotein Nmb Human Recombinant, Sf9

    Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.

    Product # :

    PRO-2394

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    Description

    GPNMB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 462 amino acids (22-474a.a.) and having a molecular mass of 51.8kDa. GPNMB is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GPNMB 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.

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    • Introduction

      Glycoprotein Nmb (GPNMB) is a member of the PMEL/NMB family. GPNMB is a type I transmembrane glycoprotein which exhibits homology to the pMEL17 precursor, a melanocyte-specific protein. GPNMB is expressed in the lowly metastatic human melanoma cell lines and xenografts but has no expression in the highly metastatic cell lines. GPNMB might be involved in growth delay and reduction of metastatic potential. GPNMB is up-regulated in a number of cancer cells, including in glioblastoma multiforme. GPNMB is expressed in many melanoma cells, as well as in tissue macrophages, including liver Kuppfer cells and lung alveolar macrophages, in podocytes and in some cells of the ciliary body of the eye (at protein level). GPNMB is hardly detectable in the healthy brain.

    • Synonyms

      Transmembrane glycoprotein NMB, Transmembrane glycoprotein HGFIN, GPNMB, HGFIN, NMB, Glycoprotein (transmembrane) nmb.

    • 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

      ADPAKRFHDV LGNERPSAYM REHNQLNGWS SDENDWNEKL YPVWKRGDMR WKNSWKGGRV QAVLTSDSPA LVGSNITFAV NLIFPRCQKE DANGNIVYEK NCRNEAGLSA DPYVYNWTAW SEDSDGENGT GQSHHNVFPD GKPFPHHPGW RRWNFIYVFH TLGQYFQKLG RCSVRVSVNT ANVTLGPQLM EVTVYRRHGR AYVPIAQVKD VYVVTDQIPV FVTMFQKNDR NSSDETFLKD LPIMFDVLIH DPSHFLNYST INYKWSFGDN TGLFVSTNHT VNHTYVLNGT FSLNLTVKAA APGPCPPPPP PPRPSKPTPS LGPAGDNPLE LSRIPDENCQ INRYGHFQAT ITIVEGILEV NIIQMTDVLM PVPWPESSLI DFVVTCQGSI PTEVCTIISD PTCEITQNTV CSPVDVDEMC LLTVRRTFNG SGTYCVNLTL GDDTSLALTS TLISVPHHHH HH.

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    Gpnmb Human Sf9
  • View Data Sheet

    Name :

    Norovirus Group-2 P-Domain

    Description:

    Norovirus Group-2 Capsid P-Domain Recombinant

    Product # :

    NRV-216

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    Description

    The Recombinant Norovirus Group-2 Capsid P-Domain, E.Coli derived, VA387 Strain contains a.a. from 225-520 having a Mw of 30kDa. The protein is fused to a 6xHis tag at N-terminal and purified by chromatography techniques. P-domain (225-520 a.a.) forms P1- P2-P1 structure. P-domain has a receptor binding region to recognize human histo-blood group antigens (HBGAs). P-domain expressed in bacteria can spontaneously form a P dime and a P particle aggregated by 12 P dimmers. P-particle displays an enhanced binding activity to HBGAs higher than virus-like particle (VLP) formed by the full length capsid.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffer and 17mM K2CO3.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    More Info

    • Introduction

      Human norovirus is classified into two groups, group 1& group 2. Norwalk virus is the species which belongs to group 1 and was discovered in 1968 at Ohio. Norovirus is a familiar virus which causes human gastroenteritis with the following symptoms vomiting, diarrhea and sickness. CDC report revealed that there are 19-21 million Americans infected by Nororvirus annually with 800 deaths, 1 in 15 people with infection. Around the world, this virus affects about 267 million people and causes over 200,000 deaths each year; these losses are mostly in less developed countries and in the very young, elderly and immuno-suppressed population, though, most cases are self-limited with a full recovery within just a few days. Norovirus is extremely contagious and can spread from human to human through infected food, water or contaminated surfaces. The outbreaks usually occur from November-April, while the peak is in January. Norovirus is a positive sense RNA virus with 7.5 kb nucleotides, encoding a major structural protein VP1 with 50-55kDa. The full length of VP1 capsid comprises the internal N-terminal, Hinge, shell (S) and protruding (P) domains. P domain from 225 to 520 forms P1- P2-P1 structure. Moreover, P domain has a receptor binding region which recognizes human histo-blood group antigens (HBGAs). P domain expressed in bacteria can spontaneously form a P dime as well as a P particle aggregated by 12 P dimmers. P particle displays an increased binding activity to HBGAs higher than virus-like particle (VLP) formed by the full-length capsid. For norovirus vaccine development, we consider P domain as a good candidate.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      The Recombinant Norovirus Group-2 P-Domain although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

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    Norovirus Group 2 P Domain
  • View Data Sheet

    Name :

    AOC1 Human

    Description:

    Amine Oxidase Copper Containing 1 Human Recombinant

    Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1

    Product # :

    PRO-2657

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    Description

    AOC1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (20-751 a.a) containing a total of 738 amino acids, having a molecular mass of 84.2kDa. AOC1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The AOC1 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Amine Oxidase Copper Containing 1 or AOC1 is n enzyme, part of the copper-containing amine oxidase group of proteins. AOC1 is responsible for oxidation of many different biogenic amines, such as neurotransmitters, xenobiotic amines & histamine. Dietary histamine intolerance and histaminosis can be caused from AOC1 deficiencies. This enzyme can also cause Tumor Progression by AKT & EMT transduction promotion in stomach cancer.

    • Synonyms

      Amiloride-sensitive amine oxidase (copper-containing), DAO, Diamine oxidase, Amiloride-binding protein 1, Amine oxidase copper domain-containing protein 1, Histaminase, Kidney amine oxidase, KAO, ABP, ABP1, DAO1

    • 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

      EPSPGTLPRK AGVFSDLSNQ ELKAVHSFLW SKKELRLQPS STTTMAKNTV FLIEMLLPKK YHVLRFLDKG ERHPVREARA VIFFGDQEHP NVTEFAVGPL PGPCYMRALS PRPGYQSSWA SRPISTAEYA LLYHTLQEAT KPLHQFFLNT TGFSFQDCHD RCLAFTDVAP RGVASGQRRS WLIIQRYVEG YFLHPTGLEL LVDHGSTDAG HWAVEQVWYN GKFYGSPEEL ARKYADGEVD VVVLEDPLPG GKGHDSTEEP PLFSSHKPRG DFPSPIHVSG PRLVQPHGPR FRLEGNAVLY GGWSFAFRLR SSSGLQVLNV HFGGERIAYE VSVQEAVALY GGHTPAGMQT KYLDVGWGLG SVTHELAPGI DCPETATFLD TFHYYDADDP VHYPRALCLF EMPTGVPLRR HFNSNFKGGF NFYAGLKGQV LVLRTTSTVY NYDYIWDFIF YPNGVMEAKM HATGYVHATF YTPEGLRHGT RLHTHLIGNI HTHLVHYRVD LDVAGTKNSF QTLQMKLENI TNPWSPRHRV VQPTLEQTQY SWERQAAFRF KRKLPKYLLF TSPQENPWGH KRTYRLQIHS MADQVLPPGW QEEQAITWAR YPLAVTKYRE SELCSSSIYH QNDPWHPPVV FEQFLHNNEN IENEDLVAWV TVGFLHIPHS EDIPNTATPG NSVGFLLRPF NFFPEDPSLA SRDTVIVWPR DNGPNYVQRW IPEDRDCSMP PPFSYNGTYR PVHHHHHH

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    Aoc1 Human
  • View Data Sheet

    Name :

    NDRG3 Human

    Description:

    N-Myc Downstream Regulated 3 Human Recombinant

    Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    Product # :

    PRO-2100

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    Description

    NDRG3 Human Recombinant produced in E. coli is a single polypeptide chain containing 386 amino acids (1-363) and having a molecular mass of 42.4 kDa.NDRG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NDRG3 solution (0.25mg/1ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      N-Myc Downstream Regulated 3, also known as NDRG3, is a protein coding gene which is a part of the NDRG family and is expressed greatly in brain. NDRG2 is an important paralog of NDRG3.

    • Synonyms

      Protein NDRG3, N-myc downstream-regulated gene 3 protein, NDRG3, N-Myc Downstream Regulated 3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDELQDV QLTEIKPLLN DKEHDIETTH GVVHVTIRGL PKGNRPVILT YHDIGLNHKS CFNAFFNFED MQEITQHFAV CHVDAPGQQE GAPSFPTGYQ YPTMDELAEM LPPVLTHLSL KSIIGIGVGA GAYILSRFAL NHPELVEGLV LINVDPCAKG WIDWAASKLS GLTTNVVDII LAHHFGQEEL QANLDLIQTY RMHIAQDINQ DNLQLFLNSY NGRRDLEIER PILGQNDNKS KTLKCSTLLV VGDNSPAVEA VVECNSRLNP INTTLLKMAD CGGLPQVVQP GKLTEAFKYF LQGMGYIPSA SMTRLARSRT HSTSSSLGSG ESPFSRSVTS NQSDGTQESC ESPDVLDRHQ TMEVSC.

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    Ndrg3 Human
  • View Data Sheet

    Name :

    ASCC1 Human

    Description:

    Activating Signal Cointegrator 1 Complex Subunit 1 Human Recombinant

    Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.

    Product # :

    PRO-1682

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    Description

    ASCC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-357) and having a molecular mass of 43.6 kDa.ASCC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASCC1 solution (0.5mg/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.

    More Info

    • Introduction

      ASCC1 is a subunit of the triggering signal cointegrator 1 (ASC-1) complex which is a transcriptional coactivator. ASC-1 complex takes a vital part in gene transactivation using various transcription factors such as activating protein 1 (AP-1), nuclear factor kappa-B (NF-kB) and serum response factor (SRF). ASCC1 has an N-terminal KH-type RNA-binding motif, essential for AP-1 transactivation by the ASC-1 complex. Alterations in ASCC1 result in Barrett esophagus and esophageal adenocarcinoma.

    • Synonyms

      Activating signal cointegrator 1 complex subunit 1, ASC1p50, CGI-18, p50, ASC-1 complex subunit p50, Trip4 complex subunit p50, ASCC1.

    • 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 MGSMEVLRPQ LIRIDGRNYR KNPVQEQTYQ HEEDEEDFYQ GSMECADEPC DAYEVEQTPQ GFRSTLRAPS LLYKHIVGKR GDTRKKIEME TKTSISIPKP GQDGEIVITG QHRNGVISAR TRIDVLLDTF RRKQPFTHFL AFFLNEVEVQ EGFLRFQEEV LAKCSMDHGV DSSIFQNPKK LHLTIGMLVL LSEEEIQQTC EMLQQCKEEF INDISGGKPL EVEMAGIEYM NDDPGMVDVL YAKVHMKDGS NRLQELVDRV LERFQASGLI VKEWNSVKLH ATVMNTLFRK DPNAEGRYNL YTAEGKYIFK ERESFDGRNI LKLFENFYFG SLKLNSIHIS QRFTVDSFGN YASCGQIDFS.

    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.

    Ascc1 Human
  • View Data Sheet

    Name :

    NTRK2 Mouse

    Description:

    Neurotrophic Receptor Tyrosine Kinase 2 Mouse Recombinant

    TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor

    Product # :

    CYT-919

    Price :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NTRK2 Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 409 amino acids (32-429a.a.) and having a molecular mass of 45.7kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa under reducing conditions).NTRK2 Mouse is expressed with an 11 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    NTRK2 Mouse protein solution (0.5mg/ml) contains PBS pH 7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NTRK2 plays a role in the growth and the development of the central and the peripheral nervous systems using the regulation of neuron proliferation, migration, survival, differentiation, and synapse production. NTRK2 is a receptor for B-DNF and NT4. NTRK2 binds to neurotrophin-3 which regulates neuron survival through NTRK2. NTRK-2 activates numerous effectors such as SHC-1, SH2B-1, PLCG-1 and SH2B-2 that control overlapping signaling cascades.

    • Synonyms

      TrkB, NTRK2, NTRK-2, Tyrosine Kinase Receptor B, BDNF/NT-3 Growth Factors Receptor

    • 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

      CPTSCKCSSA RIWCTEPSPG IVAFPRLEPN SVDPENITEI LIANQKRLEI INEDDVEAYV GLRNLTIVDS GLKFVAYKAF LKNSNLRHIN FTRNKLTSLS RRHFRHLDLS DLILTGNPFT CSCDIMWLKT LQETKSSPDT QDLYCLNESS KNMPLANLQI PNCGLPSARL AAPNLTVEEG KSVTLSCSVG GDPLPTLYWD VGNLVSKHMN ETSHTQGSLR ITNISSDDSG KQISCVAENL VGEDQDSVNL TVHFAPTITF LESPTSDHHW CIPFTVRGNP KPALQWFYNG AILNESKYIC TKIHVTNHTE YHGCLQLDNP THMNNGDYTL MAKNEYGKDE RQISAHFMGR PGVDYETNPN YPEVLYEDWT TPTDIGDTTN KSNEIPSTDV ADQSNREHAA ALEHHHHHH.

    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.

    Bdnf Mouse
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