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Search results

1000 results found for “periostin”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    OSTF1 Human

    Description:

    Osteoclast Stimulating Factor-1 Human Recombinant

    SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    Product # :

    CYT-630

    Price :

    Quantity :

    Shipping Method :

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    Description

    OSTF1 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 225 amino acids (1-217) and having a molecular mass of 25.1kDa. The OSTF1 is fused to an 8 amino acid His Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    OSTF1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH 8, 0.5mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OSTF1 is an intracellular protein produced by osteoclasts that induces bone resorption, via signaling cascade which results in the secretion of factors enhancing osteoclast formation and activity.

    • Synonyms

      SH3P2, OSF, OSTF-1, Osteoclast-stimulating factor 1, OSTF1, FLJ20559, bA235O14.1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MSKPPPKPVK PGEGGQVKVF RALYTFEPRT PDELYFEEGD IIYITDMSDT NWWKGTSKGR TGLIPSNYVA EQAESIDNPL HEAAKRGNLS WLRECLDNRV GVNGLDKAGS TALYWACHGG HKDIVEMLFT QPNIELNQQN KLGDTALHAA AWKGYADIVQ LFLAKGARTD LRNIEKKLAF DMATNAACAS LLKKKQGTDA VRTLSNAEDY LDDEDSDLEH 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.

    Ostf1 Human
  • View Data Sheet

    Name :

    Leptin tA Human

    Description:

    Leptin Antagonist Triple Mutant Human Recombinant

    Product # :

    CYT-352

    Price :

    Quantity :

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    • description
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    • biological activity
    • More Info

    Description

    Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Ta Human
  • View Data Sheet

    Name :

    CSTA Human, His

    Description:

    Cystatin A Human Recombinant, His tag

    Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    Product # :

    PRO-504

    Price :

    Quantity :

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    • More Info

    Description

    CSTA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a.) and having a molecular mass of 13.1kDa.CSTA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    More Info

    • Introduction

      Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.

    • Synonyms

      Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    • 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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.

    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.

    Csta Human His
  • View Data Sheet

    Name :

    TOR1A Human

    Description:

    Torsin Family 1 Member A Human Recombinant

    DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    Product # :

    PRO-1430

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    TOR1A Human Recombinant produced in E. coli is a single polypeptide chain containing 333 amino acids (21-332) and having a molecular mass of 38kDa. TOR1A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TOR1A 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.

    More Info

    • Introduction

      TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

    • Synonyms

      DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    • 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 MVEPISLGLA LAGVLTGYIY PRLYCLFAEC CGQKRSLSRE ALQKDLDDNL FGQHLAKKII LNAVFGFINN PKPKKPLTLS LHGWTGTGKN FVSKIIAENI YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA GAERITDVAL DFWRSGKQRE DIKLKDIEHA LSVSVFNNKN SGFWHSSLIH RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEIDEDIVSR VAEEMTFFPK EERVFSDKGC KTVFTKLDYY YDD.

    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.

    Tor1A Human
  • View Data Sheet

    Name :

    KRT20 Human, His

    Description:

    Cytokeratin 20 Human Recombinant, His Tag

    Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    Product # :

    PRO-1358

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    KRT20 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (1-424 a.a) and having a molecular mass of 50.9kDa. KRT20 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KRT20 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Human Cytokeratin 20 His Tag (KRT20) belongs to the keratin family. The keratins are intermediate filament proteins responsible for the structural integrity of epithelial cells and are subdivided into cytokeratins and hair keratins. The type I cytokeratins is comprised of acidic proteins that are organized in pairs of heterotypic keratin chains. KRT20 is a main cellular protein of mature enterocytes and goblet cells and is specifically expressed in the gastric and intestinal mucosa.

    • Synonyms

      Keratin, type I cytoskeletal 20, CD20, CK-20, CK20, K20, KRT21, Keratin, Cytokeratin-20, Keratin-20, Protein IT, KRT20.

    • 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 MGSMDFSRRS FHRSLSSSLQ APVVSTVGMQ RLGTTPSVYG GAGGRGIRIS NSRHTVNYGS DLTGGGDLFV GNEKMAMQNL NDRLASYLEK VRTLEQSNSK LEVQIKQWYE TNAPRAGRDY SAYYRQIEEL RSQIKDAQLQ NARCVLQIDN AKLAAEDFRL KYETERGIRL TVEADLQGLN KVFDDLTLHK TDLEIQIEEL NKDLALLKKE HQEEVDGLHK HLGNTVNVEV DAAPGLNLGV IMNEMRQKYE VMAQKNLQEA KEQFERQTAV LQQQVTVNTE ELKGTEVQLT ELRRTSQSLE IELQSHLSMK ESLEHTLEET KARYSSQLAN LQSLLSSLEA QLMQIRSNME RQNNEYHILL DIKTRLEQEI ATYRRLLEGE DVKTTEYQLS TLEERDIKKT RKIKTVVQEV VDGKVVSSEV KEVEENI.

    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.

    Krt20 Human His
  • View Data Sheet

    Name :

    Procalcitonin Mouse

    Description:

    Procalcitonin Mouse Recombinant

    Calcitonin, Calca, Calc.

    Product # :

    HOR-014

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    Description

    Procalcitonin Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val26-Ser136) containing 121 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 13.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Procalcitonin was filtered (0.4 µm) and lyophilized in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 94.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin, Calca, Calc.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASVPLRSILESS PGMATLSEEE VRLLAALVQD YMQMKARELE QEEEQEAEGS SLDSPRSKRC GNLSTCMLGT YTQDLNKFHT FPQTSIGVEA PGKKRDVAKD LETNHQSHFG N.

    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.

    Procalcitonin Mouse
  • View Data Sheet

    Name :

    Leptin Human, His

    Description:

    Leptin Human Recombinant, His Tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-287

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.

    • 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, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.

    • Solubility

      The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

    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 Human His
  • View Data Sheet

    Name :

    PSPN Mouse

    Description:

    Persephin Mouse Recombinant

    Persephin, PSPN.

    Product # :

    CYT-802

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    Description

    PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg. 

    More Info

    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG

    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.

    Pspn Mouse
  • View Data Sheet

    Name :

    PECI Human

    Description:

    Peroxisomal D3,D2-Enoyl-CoA Isomerase Human Recombinant

    EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.

    Product # :

    ENZ-531

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    Description

    PECI Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 42.3 kDa. The PECI is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PECI Human solution (1mg/ml) containing 20mM Tris-HCl, pH-8 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PECI is an enzyme that localized to the peroxisomal matrix and encloses one ACB (acyl-CoA-binding) domain. PECI is expressed abundantly in liver, heart and skeletal muscle. PECI functions to catalyze the isomerization of both 3-cis and 3-trans double bonds into the 2-trans form in an array of enoyl-CoA species. PECI takes part in the beta-oxidation of unsaturated fatty acids.

    • Synonyms

      EC 5.3.3.8, ACBD2, DRS1, HCA88, PECI, Peroxisomal 3,2-trans-enoyl-CoA isomerase, Dodecenoyl-CoA isomerase, Delta(3),delta(2)-enoyl-CoA isomerase, D3,D2-enoyl-CoA isomerase, Diazepam-binding inhibitor-related protein 1, DBI-related protein 1, DRS-1, Hepatocellular carcinoma-associated antigen 88, Renal carcinoma antigen NY-REN-1, KIAA0536, dJ1013A10.

    • 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 MNRTAMRASQ KDFENSMNQV KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL.

    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.

    Peci Human
  • View Data Sheet

    Name :

    Ipamorelin

    Description:

    Ipamorelin

    Ipamorelin

    Product # :

    HOR-024

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    Description

    Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Introduction

      Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.

    • Synonyms

      Ipamorelin

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Aib-His-D-2-Nal-D-Phe-Lys-NH2.

    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.

    Ipamorelin
  • View Data Sheet

    Name :

    DKK3 Antibody

    Description:

    Mouse Anti Human Dickkopf-Related Protein 3

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    ANT-707

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    Formulation

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

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human DKK3 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human DKK3 protein (22-350 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT103B5AT.

    • Applications

      DKK3 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      DKK3 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Dkk3 Antibody
  • View Data Sheet

    Name :

    CXCL4 Variant 1 Human

    Description:

    Platelet Factor-4 Variant 1 Human Recombinant

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-243

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    Description

    CXCL4 Variant-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa. The CXCL4 Variant-1 is fused to 6xHis tag at N-Terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized without additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets . Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily. Human PF4 is used for the proof of induced thrombocytopenia. Furthermore it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Human CXCL4 although stable at 25°C 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

    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.

    Cxcl4 Variant 1
  • View Data Sheet

    Name :

    Noggin Human

    Description:

    Noggin Human Recombinant

    SYM1, SYNS1, NOG.

    Product # :

    CYT-475

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    Description

    Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect  is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.

    More Info

    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
      EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
      RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
      TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

    • Background

      Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.

      Abstract:

      Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.

      Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.

      This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.

      Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.

      Molecular Characteristics of Noggin :

      1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.

      Inhibition of BMP Signaling by Noggin:

      1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.

      Physiological Functions of Noggin:

      1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.

      Therapeutic Implications of Noggin:

      1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.

      Clinical Studies and Translational Research:

      1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.

    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.

    Noggin Human
  • View Data Sheet

    Name :

    STC 2 Human, His

    Description:

    Stanniocalcin-2 Human Recombinant, His Tag

    Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    Product # :

    HOR-008

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    Description

    STC 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (25-302 a.a.) and having a molecular mass of 33kDa. STC 2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STC 2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.25M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.

    • Synonyms

      Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    • 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 MGSTDATNPP EGPQDRSSQQ KGRLSLQNTA EIQHCLVNAG DVGCGVFECF ENNSCEIRGL HGICMTFLHN AGKFDAQGKS FIKDALKCKA HALRHRFGCI SRKCPAIREM VSQLQRECYL KHDLCAAAQE NTRVIVEMIH FKDLLLHEPY VDLVNLLLTC GEEVKEAITH SVQVQCEQNW GSLCSILSFC TSAIQKPPTA PPERQPQVDR TKLSRAHHGE AGHHLPEPSS RETGRGAKGE RGSKSHPNAH ARGRVGGLGA QGPSGSSEWE DEQSEYSDIR R.

    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.

    Stc 2 Human His
  • View Data Sheet

    Name :

    PEDF Human, His

    Description:

    Pigment Epithelium-Derived Factor Human Recombinant, His Tag

    Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    CYT-552

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    Description

    PEDF Human Recombinant produced in E.Coli containing a natural variant M72T is a single, non-glycosylated, polypeptide chain containing 420 amino acids (20-418 a.a.) and having a total molecular mass of 46.7 kDa. PEDF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PEDF solution contains 20mM Tris-HCl buffer(pH 8.0), 0.1M NaCl , and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      PEDF is a neurotrophic protein that induces extensive neuronal differentiation in retinoblastoma cells. SerpinF1 is a potent inhibitor of angiogenesis. EPC1 doesn’t undergo the stressed to relaxed conformation transition characteristic as of the active serpins since it exhibits no serine protease inhibitory activity.
      Aqueous humour level of asymmetric dimethylarginine is correlated with PEDF in humans. ADMA and PEDF levels are increased in response to inflammation in uveitis.
      Lack of PEDF expression is a potent factor for the enhancement of tumor growth and angiogenesis in breast cancer.
      PEDF & VEGF genes contribute to the development of diabetic retinopathy.
      PEDF and VEGF structural changes in blood vessel wall play an important role in the pathophysiology of PD patients.
      PEDF-overexpressing tumors exhibited reduced intratumoral angiogenesis.
      SerpinF1 is a new promising approach for the treatment of osteosarcoma.
      Levels of the natural ocular anti-angiogenic factor SentrinF1 (PEDF) is associated with proliferative retinopathy.
      VEGF secreted by retinal pigment epithelial cells upregulates PEDF expression via VEGFR-1 in an autocrine manner.
      Sentrin-F1 concentration in the aqueous humor of diabetic patients predicts who will develop progression of retinopathy.
      PEDF blocks angiogenic effects of leptin through its anti-oxidative properties.

    • Synonyms

      Pigment epithelium-derived factor, PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQNPASPPEE GSPDPDSTGA LVEEEDPFFK VPVNKLAAAV SNFGYDLYRV RSSMSPTTNV LLSPLSVATA LSALSLGAEQ RTESIIHRAL YYDLISSPDI HGTYKELLDT VTAPQKNLKS ASRIVFEKKL RIKSSFVAPL EKSYGTRPRV LTGNPRLDLQ EINNWVQAQM KGKLARSTKE IPDEISILLL GVAHFKGQWV TKFDSRKTSL EDFYLDEERT VRVPMMSDPK AVLRYGLDSD LSCKIAQLPL TGSMSIIFFL PLKVTQNLTL IEESLTSEFI HDIDRELKTV QAVLTVPKLK LSYEGEVTKS LQEMKLQSLF DSPDFSKITG KPIKLTQVEH RAGFEWNEDG AGTTPSPGLQ PAHLTFPLDY HLNQPFIFVL RDTDTGALLF IGKILDPRGP.

    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.

    Serpinf1 Human His
  • View Data Sheet

    Name :

    CCNB2 Human

    Description:

    Cyclin-B2 Human Recombinant

    G2/mitotic-specific cyclin-B2, HsT17299, cyclin B2.

    Product # :

    PKA-035

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    Description

    CCNB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 422 amino acids (1-398) and having a molecular mass of 47.9 kDa.CCNB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CCNB2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCNB2 is a member of the cyclin family. CCNB2 is vital for regulation of the cell cycle at the G2/M (mitosis) transition. CCNB2 cooperates with the CDK1 protein kinase to create a serine/threonine kinase holoenzyme complex recognized as maturation promoting factor (MPF).

    • Synonyms

      G2/mitotic-specific cyclin-B2, HsT17299, cyclin B2.

    • 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 MGSHMALLRR PTVSSDLENI DTGVNSKVKS HVTIRRTVLE EIGNRVTTRA AQVAKKAQNT KVPVQPTKTT NVNKQLKPTA SVKPVQMEKL APKGPSPTPE DVSMKEENLC QAFSDALLCK IEDIDNEDWE NPQLCSDYVK DIYQYLRQLE VLQSINPHFL DGRDINGRMR AILVDWLVQV HSKFRLLQET LYMCVGIMDR FLQVQPVSRK KLQLVGITAL LLASKYEEMF SPNIEDFVYI TDNAYTSSQI REMETLILKE LKFELGRPLP LHFLRRASKA GEVDVEQHTL AKYLMELTLI DYDMVHYHPS KVAAAASCLS QKVLGQGKWN LKQQYYTGYT ENEVLEVMQH MAKNVVKVNE NLTKFIAIKN KYASSKLLKI SMIPQLNSKA VKDLASPLIG RSc

    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.

    Ccnb2 Human
  • View Data Sheet

    Name :

    CCNI Human

    Description:

    Cyclin-I Human Recombinant

    Cyclin-I, CCNI, CYC1, CYI.

    Product # :

    PKA-318

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    Description

    CCNI Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (1-377 a.a) and having a molecular mass of 44.9kDa.CCNI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCN1 is a part of the extremely conserved cyclin family, whose members are characterized by a remarkable periodicity in protein abundance through the cell cycle. Cyclins which function as regulators of CDK kinases, shows the highest similarity with cyclin G. Different cyclins display diverse expression and degradation patterns which contribute to the chronological coordination of every mitotic event. The transcript of CCN1was found to be expressed continually during cell cycle progression.

    • Synonyms

      Cyclin-I, CCNI, CYC1, CYI.

    • Physical Appearance

      Sterile Filtered clear 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 MGSMKFPGPL ENQRLSFLLE KAITREAQMW KVNVRKMPSN QNVSPSQRDE VIQWLAKLKY QFNLYPETFA LASSLLDRFL ATVKAHPKYL SCIAISCFFL AAKTVEEDER IPVLKVLARD SFCGCSSSEI LRMERIILDK LNWDLHTATP LDFLHIFHAI AVSTRPQLLF SLPKLSPSQH LAVLTKQLLH CMACNQLLQF RGSMLALAMV SLEMEKLIPD WLSLTIELLQ KAQMDSSQLI HCRELVAHHL STLQSSLPLN SVYVYRPLKH TLVTCDKGVF RLHPSSVPGP DFSKDNSKPE VPVRGTAAFY HHLPAASGCK QTSTKRKVEE MEVDDFYDGI KRLYNEDNVS ENVGSVCGTD LSRQEGHASP CPPLQPVSVM.

    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.

    Ccni Human
  • View Data Sheet

    Name :

    Procalcitonin Rhesus

    Description:

    Procalcitonin Rhesus Recombinant

    Calcitonin.

    Product # :

    HOR-016

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    Description

    Procalcitonin Rhesus Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Ala26-Asn140) containing 125 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 14kDa.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.

    • Synonyms

      Calcitonin.

    • 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 0.5 mg/ml and let the lyophilized pellet dissolve completely. Procalcitonin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASAPFRSALESS PDPATLSEEE ARLLLAALVQ DYVQMKASEL EQEQETEGSS LDSPRSKRCG NLSTCMLGTY TQDFNKFHTF PQTAIGVGAP GKKRDMSSDL ERNRRRYVSM PQDAN.

    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.

    Procalcitonin Rhesus
  • View Data Sheet

    Name :

    SERPING1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1401

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    Description

    SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • 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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.

    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.

    Serping1 Human
  • View Data Sheet

    Name :

    TREM2 Antibody

    Description:

    Triggering receptor expressed on myeloid cells 2, Mouse Anti Human

    Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    Product # :

    ANT-429

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    Formulation

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

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    • Introduction

      TREM2 is a membrane protein that forms a receptor signaling complex with TYROBP. TREM2 may be involved in chronic inflammation by triggering the production of constitutive inflammatory cytokines. Defects in the TREM2 gene are a source of polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL).

    • Synonyms

      Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.

    • Immunogen

      Anti-human TREM2 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human TREM2 amino acids 19-161 purified from E. coli.

    • Ig Subclass

      Mouse IgG3 heavy chain and κ light chain.

    • Clone

      P2B5AT.

    • Applications

      TREM2 antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000.Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      TREM2 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.

    Trem2 Antibody
  • View Data Sheet

    Name :

    PPIF Human

    Description:

    Cyclophilin-F Human Recombinant

    Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    Product # :

    ENZ-385

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    • More Info

    Description

    PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPIF solution containing 20mM Tris-HCl pH-7.5, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIF is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIF accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIF is key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.

    • Synonyms

      Oeptidylprolyl Isomerase F, PPIF, CYP-D, CYP3, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase mitochondrial, Cyclophilin F, FLJ90798, MGC117207, peptidylprolyl isomerase F.

    • 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 CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.

    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.

    Ppif Human
  • View Data Sheet

    Name :

    CCNB1 Human

    Description:

    Cyclin-B1 Human Recombinant

    G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.

    Product # :

    PKA-037

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    • More Info

    Description

    CCNB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 457 amino acids (1-433) and having a molecular mass of 50.9 kDa.CCNB1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CCNB1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cyclin B1 (CCNB1) is a regulatory protein involved in mitosis. CCNB1 creates a complex with p34(cdc2) to form the maturation-promoting factor (MPF). CCNB1 is vital for the control of the cell cycle at the G2/M (mitosis) transition. CCNB1 builds up steadily during the G2 and is immediately destroyed at mitosis. The 2 alternative transcripts produce a constitutively expressed transcript and a cell cycle-regulated transcript which is expressed predominantly during G2/M phase. These transcripts are a result of alternate transcription initiation sites.

    • Synonyms

      G2/mitotic-specific cyclin-B1, cyclin B1, CCNB.

    • 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 MGSHMALRVT RNSKINAENK AKINMAGAKR VPTAPAATSK PGLRPRTALG DIGNKVSEQL QAKMPMKKEA KPSATGKVID KKLPKPLEKV PMLVPVPVSE PVPEPEPEPE PEPVKEEKLS PEPILVDTAS PSPMETSGCA PAEEDLCQAF SDVILAVNDV DAEDGADPNL CSEYVKDIYA YLRQLEEEQA VRPKYLLGRE VTGNMRAILI DWLVQVQMKF RLLQETMYMT VSIIDRFMQN NCVPKKMLQL VGVTAMFIAS KYEEMYPPEI GDFAFVTDNT YTKHQIRQME MKILRALNFG LGRPLPLHFL RRASKIGEVD VEQHTLAKYL MELTMLDYDM VHFPPSQIAA GAFCLALKIL DNGEWTPTLQ HYLSYTEESL LPVMQHLAKN VVMVNQGLTK HMTVKNKYAT SKHAKISTLP QLNSALVQDL AKAVAKV.

    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.

    Ccnb1 Human
  • View Data Sheet

    Name :

    Leptin Rabbit

    Description:

    Leptin Rabbit Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-507

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    • More Info

    Description

    Leptin Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    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-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 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 Rabbit
  • View Data Sheet

    Name :

    TPO Human, Biotin

    Description:

    Thyroid Peroxidase Human Recombinant, Biotinylated

    Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    Product # :

    ENZ-1082

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    • More Info

    Description

    Thyroid Peroxidase Human Recombinant produced in SF9 is a Biotinylated, glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 93 kDa (excluding glycosylation). The TPO is expressed with a -6xHis tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

    • Synonyms

      Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG-type human auto-antibodies.2. Auto-antibodies to TPO recognize conformation-dependent epitopes.3. Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Thyroid Peroxidase Enzyme
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