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Search results

1000 results found for “Follistatin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    Flagellin FLA

    Description:

    Recombinant Flagellin Listeria Monocytogenes

    Product # :

    PRO-2772

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • source
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    Description

    Flagellin Listeria Monocytogenes Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of approximately 31.2kDa. The Flagellin FLA is fused to a 6xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Flagellin Listeria Monocytogenes 1mg/ml solution contains 10mM PBS (pH-7.2).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Listeria monocytogenes is a pathogenic bacteria that manufactures flagella.At 37 °C inside humans, it causes MogR to repress the expression of flagellar proteins, thus stopping the manufacturing of flagella. Though, in the low-temperatures externally of the host, the GmaR inactivates MogR, enabling flagellar formation.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Lyophilized Flagellin FLA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flagellin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent 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.

    Flagellin Fla
  • View Data Sheet

    Name :

    Thymosin alpha 1

    Description:

    Thymosin a1 Acetate

    Product # :

    HOR-243

    Price :

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    Shipping Method :

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    Description

    Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
      THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.

      What is the Purity of THYMOSIN-A1 HUMAN Protein?
      THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
      The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.

      What applications can THYMOSIN-A1 HUMAN Protein be used in?
      THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
      The endotoxin level is minimal, THYMOSIN-A1 HUMAN Protein was purified using conventional chromatography techniques.

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

    Thymosin Alpha 1
  • View Data Sheet

    Name :

    Triptorelin

    Description:

    Triptorelin Acetate

    Product # :

    HOR-238

    Price :

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    • description
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    Description

    Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.

    Formulation

    The protein (1 mg/ml) was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

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

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

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

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

    Triptorelin
  • View Data Sheet

    Name :

    Leptin Mouse, PEG

    Description:

    Pegylated Mouse Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-591

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • purity
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    • More Info
    • Citations

    Description

    Leptin Mono-Pegylated Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus. Pegylated Mouse Leptin contains PEG 20 kDa at its N-terminus and having a molecular mass of 35.6 kDa as determined by mass spectrometry. Since its enlarged hydrodymanic volume Pegylated Leptin runs on SDS-PAGE as A 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Pegylated Mouse Leptin half-life in circulation after SC injection was over 20 hours. Mouse Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

    The mouse Leptin was lyophilized from a concentrated (0.65mg/ml) solution containing 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Pegylated mouse Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated mouse Leptin in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    Citations

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile 0.4% NaHCO3 adjusted to pH-8.5 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Mouse Pegylated
  • View Data Sheet

    Name :

    Periostin Human

    Description:

    Periostin Human Recombinant

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-452

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    Description

    The OSF2 His-Tagged Fusion Protein Human is produced in E. coli, and its molecular weight is 75 kDa protein containing 648 amino acid residues of the human OSF-2 and 23 additional amino acid residues - HisTag, Xa - cleavage site.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MGHHHHHHHH HHSSGHIEGR HMRNNHYDKI LAHSRIRGRD QGPNVCALQQ ILGTKKKYFS TCKNWYKKSI CGQKTTVLYE CCPGYMRMEG MKGCPAVLPI DHVYGTLGIV GATTTQRYSD ASKLREEIEG KGSFTYFAPS NEAWDNLDSD IRRGLESNVN VELLNALHSH MINKRMLTKD LKNGMIIPSM YNNLGLFINH YPNGVVTVNC ARIIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFIEAEDDLS SFRAAAITSD ILEALGRDGH FTLFAPTNEA FEKLPRGVLE RFMGDKVASEALMKYHILNT LQCSESIMGG AVFETLEGNT IEIGCDGDSI TVNGIKMVNK KDIVTNNGVI HLIDQVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASALR PDGEYTLLAP VNNAFSDDTL SMVQRLLKLI LQNHILKVKV GLNELYNGQI LETIGGKQLR VFVYRTAVCI ENSCMEKGSK QGRNGAIHIF REIIKPAEKS LHEKLKQDKR FSTFLSLLEA ADLKELLTQP GDWTLFVPTN DAFKGMTSEE KEILIRDKNA LQNIILYHLT PGVFIGKGFE PGVTNILKTT QGSKIFLKEV NDTLLVNELK SKESDIMTTN GVIHVVDKLL YPADTPVGND QLLEILNKLI KYIQIKFVRG STFKEIPVTV Y.

    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.

    Periostin Human
  • View Data Sheet

    Name :

    HPCAL1 Human

    Description:

    Hippocalcin-Like 1 Human Recombinant

    Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3, VILIP-3

    Product # :

    PRO-254

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    Description

    HPCAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213amino acids (1-193a.a.) and having a molecular wieght of 24.4kDa. The HPCAL1 is fused to 20a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HPCAL1 protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0) containing 1mM DTT 0.2M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPCAL1, participates in neuron-specific calcium-binding proteins family found in the retina and brain. HPCAL1 is extremely comparable to human hippocalcin protein and almost equal to the rat and mouse hippocalcin like-1 proteins. HPCAL1 takes part in the calcium-dependent regulation of rhodopsin phosphorylation and can have importance in neuronal signalling in the central nervous system.

    • Synonyms

      Hippocalcin-Like 1, HLP2, BDR1, Calcium-Binding protein BDR-1, Visinin-Like protein 3,
      VILIP-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 MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF

    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.

    Hpcal1 Human
  • View Data Sheet

    Name :

    OSM Rat

    Description:

    Oncostatin-M Rat Recombinant

    Oncostatin-M, OSM, OncoM.

    Product # :

    CYT-169

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    Description

    OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.

    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 the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.

    Citations

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      Oncostatin-M, OSM, OncoM.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.

    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.

    Osm Rat
  • View Data Sheet

    Name :

    Periostin Human, HEK

    Description:

    Periostin Human Recombinant, HEK

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-835

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    Description

    Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.

    Purity

    Greater than 38.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

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

    • Amino Acid Sequence

      NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.

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

    Periostin Human Hek
  • View Data Sheet

    Name :

    PFDN5 Human

    Description:

    Prefoldin Subunit 5 Human Recombinant

    Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-1.

    Product # :

    PRO-901

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    Description

    PFDN5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (1-154 a.a.) and having a molecular mass of 19.5kDa.PFDN5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFDN5 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PFDN5 is a member of the prefoldin alpha subunit family. Prefoldin (PFDN) being a ubiquitously expressed heterohexameric co-chaperone, is required for proper folding of nascent proteins, in particular, tubulin and actin. PFDN5 is one of 6 subunits of prefoldin, which is a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides, thus allowing them to fold properly. The PFDN5 protein may also limit the transcriptional activity of the proto-oncogene c-Myc.

    • Synonyms

      Prefoldin subunit 5, C-Myc-binding protein Mm-1, Myc modulator 1, PFDN5, MM1, PFD5, MM-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 MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA.

    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.

    Pfdn5 Human
  • View Data Sheet

    Name :

    SOST Human

    Description:

    Sclerostin Human Recombinant

    Sclerostin, SOST, CDD, VBCH.

    Product # :

    PRO-1601

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    Description

    SOST Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 24-213) containing 200 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 22.8kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in 0.03M Acetate buffer pH-4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      Sclerostin, SOST, CDD, VBCH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH-4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASQGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY.

    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.

    Sost Human
  • View Data Sheet

    Name :

    Clusterin Mouse

    Description:

    Apolipoprotein-J Mouse Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-1172

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    Description

    Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

    Clusterin filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer and 50 mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 50.2kDa.

      What is the source or expression system of CLUSTERIN Protein?
      HEK293

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

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

      What is the amino acid sequence of CLUSTERIN Protein?
      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

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

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

    Clusterin Mouse
  • View Data Sheet

    Name :

    CETN3 Human

    Description:

    Centrin-3 Human Recombinant

    CEN3, CEN-3, CETN-3.

    Product # :

    PRO-533

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    Description

    CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

    • Synonyms

      CEN3, CEN-3, CETN-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 MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
      KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
      AIMTGDI.

    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.

    Cetn3 Human
  • View Data Sheet

    Name :

    CHGA Human

    Description:

    Chromogranin-A Human Recombinant

    CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.

    Product # :

    PRO-692

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    Description

    Recombinant Human CHGA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 114 amino acids (19-131 a.a) and having a molecular mass of 12.8 kDa. Chromgranin-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CHGA protein contains 20mM Tris-HCl buffer pH-8, and 10% glycerol.

    Purity

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

    Citations

    More Info

    • Introduction

      Chromgranin-A is part of the neuroendocrine secretory protein family. CHGA is located in secretory vesicles of neurons and endocrine cells. Chromgranin-A is a precursor to three biologically active peptides; vasostatin, pancreastatin, and parastatin. These peptides act as autocrine or paracrine negative modulators of the neuroendocrine system. Other peptides, including chromostatin, beta-granin, WE-14 and GE-25, are also derived from the full-length protein. Chromgranin-A has numerous biological activities on some tissues and organs and exerts a large spectrum of homeostatic actions, including antifungal and antimicrobial effect, modulation of cell adhesion, and inhibition of parathyroid hormone secretion.

    • Synonyms

      CGA, CHGA, Vasostatin-2, Pituitary secretory protein I, SP-I.

    • 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

      MLPVNSPMNK GDTEVMKCIV EVISDTLSKP SPMPVSQECF ETLRGDERIL SILRHQNLLK ELQDLALQGA KERAHQQKKH SGFEDELSEV LENQSSQAEL KEAVEEPSSK DVME.

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    Chromogranin A Human
  • View Data Sheet

    Name :

    PGC Human

    Description:

    Progastricsin-C Human Recombinant

    Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    Product # :

    ENZ-966

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    Description

    PGC produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (17-388 a.a.) and having a molecular mass of 41.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PGC is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PGC 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

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    • Introduction

      Progastricsin-C (PGC) is an aspartic proteinase which is synthesized in the gastric mucosa as inactive precursors. PGC is a part of the peptidase family A1 and contains a prosegment which is responsible for stabilizing the inactive form and preventing the entrance of the substrate to the active site. PGC is used as a biomarker for various gastric diseases including Helicobacter pylori related gastritis. PGC is also hydrolyzes various proteins.

    • Synonyms

      Progastricsin (Pepsinogen C), Pepsinogen C, EC 3.4.23.3, Pepsinogen Group II, Preprogastricsin, EC 3.4.23, Pepsin C, PGII, PEPC.

    • 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

      AVVKVPLKKF KSIRETMKEK GLLGEFLRTH KYDPAWKYRF GDLSVTYEPM AYMDAAYFGE ISIGTPPQNF LVLFDTGSSN LWVPSVYCQS QACTSHSRFN PSESSTYSTN GQTFSLQYGS GSLTGFFGYD TLTVQSIQVP NQEFGLSENE PGTNFVYAQF DGIMGLAYPA LSVDEATTAM QGMVQEGALT SPVFSVYLSN QQGSSGGAVV FGGVDSSLYT GQIYWAPVTQ ELYWQIGIEE FLIGGQASGW CSEGCQAIVD TGTSLLTVPQ QYMSALLQAT GAQEDEYGQF LVNCNSIQNL PSLTFIINGV EFPLPPSSYI LSNNGYCTVG VEPTYLSSQN GQPLWILGDV FLRSYYSVYD LGNNRVGFAT AALEHHHHHH.

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    Pgc Human
  • View Data Sheet

    Name :

    Leptin Mouse (D23L)

    Description:

    Leptin D23L Mutant Mouse Recombinant

    Product # :

    CYT-1249

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    Description

    Leptin Mutant D23L Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Mouse Leptin having a molecular mass of 16 kDa and was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Mouse is able to induce proliferation of BA/F3 cells stably transfected with the long form of human leptin receptor but its affinity toward this receptor was ~ 25-fold higher compared to non-mutated mouse leptin.

    Citations

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1mg/ml and up to 2mM and filter sterilization Mouse Leptin can be stored at 4°C for 2-3 months. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Mouse in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids is Ala-Val-Pro-Ile-Gln

    • Background

      Leptin’s main part is to regulate long-term energy balance. Leptin produced mainly by adipocytes and is encoded by the LEP gene. Leptin effects mainly on leptin receptors in the cell mambrane of different cells in the human body. The leptin receptor is found on various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviors which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value was calculated by DNA man program.

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

    Leptin Mouse Mutant
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    Citations

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    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 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 Brain-derived Neurotrophic Factor as a Reference Standard.

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    Bdnf Human
  • View Data Sheet

    Name :

    Flagellin FliA (H)

    Description:

    Flagellin FliA (H) Recombinant

    Product # :

    PRO-2718

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    Description

    Flagellin FliA (H) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 302 amino acids and having a molecular mass of approximately 33.1kDa.The Flagellin FliA (H) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE and HPLC analyses.

    Citations

    More Info

    • Introduction

      Flagellin FliA (H), also known as RNA polymerase sigma factor for flagellar operon, Sigma F and Sigma-28, is a part of the FliA subfamily or sigma-70 factor family. This sigma factor controls the expression of flagella-related genes. Flagellin FliA (H) regulates the expression of genes involved in virulence. Flagellin FliA (H) is an initiation factors which endorses the attachment of RNA polymerase to specific initiation sites and are then released.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MKGLKTGWIE KSVENIKTAY GIEPTGANKL KVTISDDGAY GVLASVTPKT GEFELHIDSS DFEKGDGESG NNIHGKLYDD RIIQHEMTHA VMNDALGIDK MNDLHDKNKL WFIEGTAEAM AGADERVKDI IGNDTQTGID NTKLSKLATR ADALLNGVSW NSSDEDYAAG YLMVKYIASK GIDLKAVMKE IKNTGASGLD NKIDLTNLKI DFKNNLENYI KDISKVHLDW DDDEKDVGSI LGSDHGHGDI KAEDVVKGTT PEKEQPLDKF KIIWPDDNSD NTTGKIQLQV GANEGQSITI LE

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    Flagellin Flia H
  • View Data Sheet

    Name :

    CST7 Human

    Description:

    Cystatin 7 Human Recombinant

    Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    Product # :

    PRO-2222

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    Description

    CST7 Human Recombinant produced in E. coli is a single polypeptide chain containing 132 amino acids (20-145) and having a molecular mass of 15.3kDa.CST7 is fused to a 7 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CST7 solution (0.5mg/1ml) contains phosphate buffered saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cystatin 7 (CST7) is a glycosylated cysteine protease inhibitor with a putative role in immune regulation through inhibition of a unique target in the hematopoietic system. Cystatin-7 is comprised of multiple cystatin-like sequences. The superfamily is comprised of 3 inhibitory families: the type 1 cystatins (stefins), type 2 cystatins and the kininogens. Some members are active cysteine protease inhibitors, while others have lost or possibly never had this inhibitory activity. Type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in various human fluids and secretions. CST7 protein expression has been observed in numerous human cancer cell lines established from malignant tumors.

    • Synonyms

      Cystatin-F, Cystatin-7, Cystatin-like metastasis-associated protein, CMAP, Leukocystatin, Cystatin 7, CST7, CMAP.

    • 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

      GPSPDTCSQD LNSRVKPGFP KTIKTNDPGV LQAARYSVEK FNNCTNDMFL FKESRITRAL VQIVKGLKYM LEVEIGRTTC KKNQHLRLDD CDFQTNHTLK QTLSCYSEVW VVPWLQHFEV PVLRCHHHHH HH.

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    Cst7 Human
  • View Data Sheet

    Name :

    NTS Human, sf9

    Description:

    Neurotensin Human Recombinant, sf9

    Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    Product # :

    PRO-2374

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    Description

    NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

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

    Citations

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    • Introduction

      Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.

    • Synonyms

      Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

    • 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

      ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

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    Nts Human Sf9
  • View Data Sheet

    Name :

    Visfatin Human

    Description:

    Visfatin Human Recombinant

    PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    Product # :

    CYT-318

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    Description

    Visfatin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 466 amino acids. The total molecular mass is 52.6kDa (calculated). The Visfatin is purified by Flag-affinity chromatography.

    Source

    Escherichia Coli.

    Formulation

    Visfatin was lyophilized with no additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by its ability to induce IL-6, IL-1 beta and TNF alpha production from human PBMCs at 100ng/ml.

    Citations

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    • Introduction

      Excess adiposity is the most important risk in the development of type 2 diabetes mellitus (T2DM). Adipose tissue produces several proteins (adipocytokines) such as leptin, adiponectin, resistin, tumor necrosis factor-a, and IL-6, that modulate sensitivity and appear to play an important role in the pathogenesis, diabetes, dyslipidemia, inflammation, and atherosclerosis. Visfatin, also known as pre-B cell colony-enhancing factor (PBEF), is a cytokine that is highly expressed in visceral fat and was originally isolated as a secreted factor that synergizes with IL-7 and stem cell factors to promote the growth of B cell precursors. Visfatin homologs have been identified in carp, invertebrate mollusks, and bacteria, as well as in vertebrates, including humans and the mouse. It has been postulated to play a role in innate immunity.
      Visfatin exerts mimetic effects that are dose-dependent and quantitatively similar to stimulating muscle and adipocyte glucose transport, and in inhibiting hepatocyte glucose production. Intravenous injection of recombinant visfatin in mice decreased plasma glucose in a dose-dependent fashion. In keeping with its mimetic effects, visfatin was as effective in reducing hyperglycemia in deficient diabetic mice. Visfatin was also found to be bound to and activate receptor, causing receptor phosphorylation and the activation of downstream signaling molecules. However, visfatin did not compete for binding to the receptor, indicating that the two proteins were recognized by different regions of the receptor. Thus, visfatin might play a role in glucose homeostasis and dysregulation in biosynthesis or signal transduction, and might contribute to the pathogenesis of diabetes.

    • Synonyms

      PBEF, Pre-B cell colony-enhancing factor, Nicotinamide phosphoribosyltransferase NAmPRTase, Nampt, MGC117256, DKFZP666B131, 1110035O14Rik.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

      Centrifuge vial before opening. When reconstituting the product, gently pipet and wash down the sides of the vial to ensure full recovery of the protein into solution. It is recommended to reconstitute the lyophilized product with 20 mM HCl at a concentration of 0.1 mg/mL, which can be further diluted into other aqueous solutions. Wait several minutes for full reconstitution and solubility.

    • Amino Acid Sequence

      MPPNTSKVYS YFECREKKTE NSKLRKVKYE ETVFYGLQYI LNKYLKGKVV TKEKIQEAKD VYKEHFQDDV FNEKGWNYIL EKYDGHLPIE IKAVPEGFVI PRGNVLFTVE NTDPECYWLT NWIETILVQS WYPITVATNS REQKKILAKY LLETSGNLDG LEYKLHDFGY RGVSSQETAG IGASAHLVNF KGTDTVAGLA LIKKYYGTKD PVPGYSVPAA EHSTITAWGK DHEKDAFEHI VTQFSSVPVS VVSDSYDIYN ACEKIWGEDL RHLIVSRSTQ APLIIRPDSG NPLDTVLKVL EILGKKFPVT ENSKGYKLLP PYLRVIQGDG VDINTLQEIV EGMKQKMWSI ENIAFGSGGG LLQKLTRDLL NCSFKCSYVV TNGLGINVFK DPVADPNKRS KKGRLSLHRT PAGNFVTLEE GKGDLEEYGQ DLLHTVFKNG KVTKSYSFDE IRKNAQLNIE LEAAHH.

    • Background

      About Visfatin Human


      Visfatin is a cytokine expressed in visceral fat that was originally isolated as a secreted
      element that synergized with stem cell factors and IL-7. One of its main functions is to
      enhance the development of B cell precursors.

      The cytokine is also known as the “Pre-B Cell Colony-Enhancing Factor (PBEF).” It has been
      identified in vertebrates, including mice and humans, and it’s being studied due to its link
      to inflammatory conditions, beta cell function, and cardiovascular disease.


      What’s the Function of Visfatin Human Recombinant?

      Visfatin human recombinant is produced in E. Coli. It’s a single, non-glycosylated,
      polypeptide chain that contains 466 amino acids, it’s purified by FLAG-affinity
      chromatography, and it contains a total molecular mass of 52.6 kDa.


      What Are the Main Applications of Visfatin Human Recombinant?

      The cytokine is being researched because of its involvement in glucose homeostasis,
      dysregulation in biosynthesis and signal transduction, and the pathogenesis of diabetes.
      Visfatin human recombinant is tailored exclusively for laboratory research, ensuring
      experts can get further answers regarding the cytokine’s involvement in different
      processes, including pathogenesis, diabetes, inflammation, dyslipidemia, and
      atherosclerosis.

      Findings can also help during the identification of high-risk people for cardiovascular
      disease and diabetes.

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    Visfatin Human
  • View Data Sheet

    Name :

    CST9 Human

    Description:

    Cystatin 9 Human Recombinant

    CLM, cystatin-9 (testatin), Cystatin-like molecule.

    Product # :

    PRO-955

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    Description

    CST9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (29-159) and having a molecular mass of 17.2 kDa.CST9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST9 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CST9 belongs to the CRES (cystatin-related epididymal spermatogenic) subfamily. The CRES (cystatin-related epididymal spermatogenic) protein outlines a new subgroup in the family 2 cystatins of the cystatin superfamily. A few members are active cysteine protease inhibitors, however others have lost or possibly never developed this inhibitory activity. CST9 takes part in hematopoietic differentiation or inflammation and is expressed in heart, placenta, lung, liver, skeletal muscle and pancreas. CST9 is upregulated by LPS in several cancer cell lines, such as promyelocytic leukemia (HL-60) and myelomonocytic leukemia.

    • Synonyms

      CLM, cystatin-9 (testatin), Cystatin-like molecule.

    • 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 MWCSEEEMGG NNKIVQDPMF LATVEFALNT FNVQSKEEHA YRLLRVLSSW REDSMDRKWR GKMVFSMNLQ LRQTVCRKFE DDIDNCPFQE SLELNNVRQG ISFPQVHSCG CCMGCGVGTG AADKAIPRDK GK.

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    Cst9 Human
  • View Data Sheet

    Name :

    PHB2 Human

    Description:

    Prohibitin 2 Human Recombinant

    BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    Product # :

    PRO-1533

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    Description

    PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.

    • Synonyms

      BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    • 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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.

    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.

    Phb2 Human
  • View Data Sheet

    Name :

    Flt3 Ligand Porcine

    Description:

    Flt3 Ligand Porcine Recombinant

    Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    Product # :

    CYT-1041

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

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

    Description

    Flt3-Ligand Porcine Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of approximately 17.3kDa. Flt3-Ligand is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein is lyophilized with 10mM Sodium Phosphate pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, FLK2, STK1, CD135, Stem Cell Tyrosine Kinase 1, FLT3LG, Flt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Porcine Flt3-Ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Flt3-Ligand 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 Flt3-L in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein has a total Mw of 17.3kDa.

      What is the source or expression system of FLT3 LIGAND PORCINE Protein?
      Escherichia Coli.

      What is the Purity of FLT3 LIGAND PORCINE Protein?
      FLT3 LIGAND PORCINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND PORCINE Protein?
      The biological functionality of FLT3 LIGAND PORCINE Protein will be determined in the future.

      What is the amino acid sequence of FLT3 LIGAND PORCINE Protein?
      MSPDCSFPHS PISSTFANTI RQLSDYLLQD YPVTVASNLQ DDELCGAFWR LVLAQRWMGQ LKTVAGSQMQ KLLEAVNTEI VFVTSCALQP LPSCLRFVQA NISHLLQDTS QQLVALKPWI TRRNFSRCLE LQCQPDPSTL LPPRSPGALE ATSLP.

      What applications can FLT3 LIGAND PORCINE Protein be used in?
      FLT3 LIGAND PORCINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND PORCINE Protein?
      The endotoxin level is minimal, FLT3 LIGAND PORCINE 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.

    Flt3 Ligand Porcine
  • View Data Sheet

    Name :

    Leptin qA Mouse, Antagonist

    Description:

    Leptin Quadruple Antagonist Mouse Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-1257

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Leptin Quadruple Antagonist Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino, an additional Ala at N-terminus and having a molecular mass of ~ 16 kDa. The Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. Leptin Quadruple Antagonist Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Mouse Leptin Quadruple anatagonist was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Leptin Quadruple Antagonist Mouse Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Mouse Leptin Quadruple Antagonist also inhibits various leptin effects in several in vitro bioassays. The inhibitory activity of Mouse Leptin Quadruple Antagonist was increased 14 to 60 fold as measured by various criteria such as binding properties to human leptin binding domain and in vitro and in vivo bioassays as compared to mouse leptin antagonist.

    Citations

    More Info

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids of mouse super-active leptin antagonist was determined and was found to be Ala-Val-Pro-Ile-Gln.

    • Background

      Leptin is produced by adipocytes and its main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene and effects mainly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor is found on a wide range of cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which lead to energy savings High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

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

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

    Leptin Mouse Antagonist
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